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https://en.wikipedia.org/wiki/2-deoxy-D-gluconate%203-dehydrogenase | 2-deoxy-D-gluconate 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-deoxy-D-gluconate + NAD+ 3-dehydro-2-deoxy-D-gluconate + NADH + H+
Thus, the two substrates of this enzyme are 2-deoxy-D-gluconate and NAD+, whereas its 3 products are 3-dehydro-2-deoxy-D-gluconate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-deoxy-D-gluconate:NAD+ 3-oxidoreductase. This enzyme is also called 2-deoxygluconate dehydrogenase. This enzyme participates in pentose and glucuronate interconversions.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-hydroxy-3-oxopropionate%20reductase | In enzymology, a 2-hydroxy-3-oxopropionate reductase () is an enzyme that catalyzes the chemical reaction
(R)-glycerate + NAD(P)+ 2-hydroxy-3-oxopropanoate + NAD(P)H + H+
The 3 substrates of this enzyme are (R)-glycerate, NAD+, and NADP+, whereas its 4 products are 2-hydroxy-3-oxopropanoate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-glycerate:NAD(P)+ oxidoreductase. This enzyme is also called tartronate semialdehyde reductase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-hydroxymethylglutarate%20dehydrogenase | In enzymology, a 2-hydroxymethylglutarate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-2-hydroxymethylglutarate + NAD+ 2-formylglutarate + NADH + H+
Thus, the two substrates of this enzyme are (S)-2-hydroxymethylglutarate and NAD+, whereas its 3 products are 2-formylglutarate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-2-hydroxymethylglutarate:NAD+ oxidoreductase. This enzyme is also called HgD.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-oxoadipate%20reductase | In enzymology, a 2-oxoadipate reductase () is an enzyme that catalyzes the chemical reaction
2-hydroxyadipate + NAD+ 2-oxoadipate + NADH + H+
Thus, the two substrates of this enzyme are 2-hydroxyadipate and NAD+, whereas its 3 products are 2-oxoadipate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-hydroxyadipate:NAD+ 2-oxidoreductase. Other names in common use include 2-ketoadipate reductase, alpha-ketoadipate reductase, and 2-ketoadipate reductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-%28R%29-hydroxypropyl-CoM%20dehydrogenase | In enzymology, a 2-(R)-hydroxypropyl-CoM dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-(R)-hydroxypropyl-CoM + NAD+ 2-oxopropyl-CoM + NADH + H+
Thus, the two substrates of this enzyme are 2-(R)-hydroxypropyl-CoM and NAD+, whereas its 3 products are 2-oxopropyl-CoM, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-[2-(R)-hydroxypropylthio]ethanesulfonate:NAD+ oxidoreductase. This enzyme is also called 2-(2-(R)-hydroxypropylthio)ethanesulfonate dehydrogenase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-%28S%29-hydroxypropyl-CoM%20dehydrogenase | In enzymology, a 2-(S)-hydroxypropyl-CoM dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-(S)-hydroxypropyl-CoM + NAD+ 2-oxopropyl-CoM + NADH + H+
Thus, the two substrates of this enzyme are 2-(S)-hydroxypropyl-CoM and NAD+, whereas its 3 products are 2-oxopropyl-CoM, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-[2-(S)-hydroxypropylthio]ethanesulfonate:NAD+ oxidoreductase. This enzyme is also called 2-(2-(S)-hydroxypropylthio)ethanesulfonate dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3alpha%2817beta%29-hydroxysteroid%20dehydrogenase%20%28NAD%2B%29 | {{DISPLAYTITLE:3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)}}
In enzymology, a 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+) () is an enzyme that catalyzes the chemical reaction:
testosterone + NAD+ androst-4-ene-3,17-dione + NADH + H+
Thus, the two substrates of this enzyme are testosterone and NAD+, whereas its 3 products are androst-4-ene-3,17-dione, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3alpha(or 17beta)-hydroxysteroid:NAD+ oxidoreductase. Other names in common use include 3alpha,17beta-hydroxy steroid dehydrogenase, 3alpha(17beta)-HSD, and 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+). This enzyme participates in androgen and estrogen metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3alpha-hydroxy-5beta-androstane-17-one%203alpha-dehydrogenase | In enzymology, a 3alpha-hydroxy-5beta-androstane-17-one 3alpha-dehydrogenase () is an enzyme that catalyzes the chemical reaction
3alpha-hydroxy-5beta-androstane-17-one + NAD+ 5beta-androstane-3,17-dione + NADH + H+
Thus, the two substrates of this enzyme are 3alpha-hydroxy-5beta-androstane-17-one and NAD+, whereas its 3 products are 5beta-androstane-3,17-dione, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3alpha-hydroxy-5beta-steroid:NAD+ 3-oxidoreductase. Other names in common use include etiocholanolone 3alpha-dehydrogenase, etiocholanolone 3alpha-dehydrogenase, and 3alpha-hydroxy-5beta-steroid dehydrogenase. This enzyme participates in androgen and estrogen metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3alpha-hydroxycholanate%20dehydrogenase | In enzymology, a 3alpha-hydroxycholanate dehydrogenase () is an enzyme that catalyzes the chemical reaction
3alpha-hydroxy-5beta-cholanate + NAD+ 3-oxo-5beta-cholanate + NADH + H+
Thus, the two substrates of this enzyme are 3alpha-hydroxy-5beta-cholanate and NAD+, whereas its 3 products are 3-oxo-5beta-cholanate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3alpha-hydroxy-5beta-cholanate:NAD+ oxidoreductase. This enzyme is also called alpha-hydroxy-cholanate dehydrogenase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3alpha-hydroxyglycyrrhetinate%20dehydrogenase | In enzymology, a 3alpha-hydroxyglycyrrhetinate dehydrogenase () is an enzyme that catalyzes the chemical reaction
3alpha-hydroxyglycyrrhetinate + NADP+ 3-oxoglycyrrhetinate + NADPH + H+
Thus, the two substrates of this enzyme are 3alpha-hydroxyglycyrrhetinate and NADP+, whereas its 3 products are 3-oxoglycyrrhetinate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3alpha-hydroxyglycyrrhetinate:NADP+ 3-oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3alpha-hydroxysteroid%20dehydrogenase%20%28A-specific%29 | In enzymology, a 3alpha-hydroxysteroid dehydrogenase (A-specific) () is an enzyme that catalyzes the chemical reaction
androsterone + NAD(P)+ 5alpha-androstane-3,17-dione + NAD(P)H + H+
The 3 substrates of this enzyme are androsterone, NAD+, and NADP+, whereas its 4 products are 5alpha-androstane-3,17-dione, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor, more specifically it is part of the group of hydroxysteroid dehydrogenases. The systematic name of this enzyme class is 3alpha-hydroxysteroid:NAD(P)+ oxidoreductase (A-specific).
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3alpha-hydroxysteroid%20dehydrogenase%20%28B-specific%29 | In enzymology, a 3alpha-hydroxysteroid dehydrogenase (B-specific) () is an enzyme that catalyzes the chemical reaction
androsterone + NAD(P)+ 5alpha-androstane-3,17-dione + NAD(P)H + H+
The 3 substrates of this enzyme are androsterone, NAD+, and NADP+, whereas its 4 products are 5alpha-androstane-3,17-dione, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor, more specifically it is part of the group of hydroxysteroid dehydrogenases. The systematic name of this enzyme class is 3alpha-hydroxysteroid:NAD(P)+ oxidoreductase (B-specific). Other names in common use include hydroxyprostaglandin dehydrogenase, 3alpha-hydroxysteroid oxidoreductase, and sterognost 3alpha. This enzyme participates in 3 metabolic pathways: bile acid biosynthesis, c21-steroid hormone metabolism, and androgen and estrogen metabolism.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3alpha%28or%2020beta%29-hydroxysteroid%20dehydrogenase | In enzymology, a 3alpha(or 20beta)-hydroxysteroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
androstan-3alpha,17beta-diol + NAD+ 17beta-hydroxyandrostan-3-one + NADH + H+
Thus, the two substrates of this enzyme are androstan-3alpha,17beta-diol and NAD+, whereas its 3 products are 17beta-hydroxyandrostan-3-one, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3alpha(or 20beta)-hydroxysteroid:NAD+ oxidoreductase. Other names in common use include cortisone reductase, (R)-20-hydroxysteroid dehydrogenase, dehydrogenase, 20beta-hydroxy steroid, Delta4-3-ketosteroid hydrogenase, 20beta-hydroxysteroid dehydrogenase, 3alpha,20beta-hydroxysteroid:NAD+-oxidoreductase, NADH-20beta-hydroxysteroid dehydrogenase, and 20beta-HSD. This enzyme participates in bile acid biosynthesis and c21-steroid hormone metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3beta-hydroxy-5alpha-steroid%20dehydrogenase | In enzymology, a 3β-hydroxy-5α-steroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
3β-hydroxy-5α-pregnane-20-one + NADP+ 5α-pregnan-3,20-dione + NADPH + H+
Thus, the two substrates of this enzyme are 3β-hydroxy-5α-pregnane-20-one (allopregnanolone) and NADP+, whereas its 3 products are 5α-pregnan-3,20-dione, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3β-hydroxy-5α-steroid:NADP+ 3-oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3beta-hydroxy-5beta-steroid%20dehydrogenase | In enzymology, a 3beta-hydroxy-5beta-steroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
3beta-hydroxy-5beta-pregnane-20-one + NADP+ 5beta-pregnan-3,20-dione + NADPH + H+
Thus, the two substrates of this enzyme are 3beta-hydroxy-5beta-pregnane-20-one and NADP+, whereas its 3 products are 5beta-pregnan-3,20-dione, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3beta-hydroxy-5beta-steroid:NADP+ 3-oxidoreductase. Other names in common use include 3beta-hydroxysteroid 5beta-oxidoreductase, and 3beta-hydroxysteroid 5beta-progesterone oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3beta%28or%2020alpha%29-hydroxysteroid%20dehydrogenase | In enzymology, a 3-β(or 20-α)-hydroxysteroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
5α-androstan-3β,17β-diol + NADP+ 17β-hydroxy-5α-androstan-3-one + NADPH + H+
This enzyme possesses the combined activities of the 3-β-hydroxysteroid dehydrogenase/Δ-5-4 isomerase and 20-α-hydroxysteroid dehydrogenase enzymes.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3%22-deamino-3%22-oxonicotianamine%20reductase | In enzymology, a 3"-deamino-3"-oxonicotianamine reductase () is an enzyme that catalyzes the chemical reaction
2'-deoxymugineic acid + NAD(P)+ 3"-deamino-3"-oxonicotianamine + NAD(P)H + H+
The 3 substrates of this enzyme are 2'-deoxymugineic acid, NAD+, and NADP+, whereas its 4 products are 3-deamino-3-oxonicotianamine, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-deoxymugineic acid:NAD(P)+ 3-oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-dehydro-L-gulonate%202-dehydrogenase | In enzymology, a 3-dehydro-L-gulonate 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction:
3-dehydro-L-gulonate + NAD(P)+ (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate + NAD(P)H + H+
The 3 substrates of this enzyme are 3-dehydro-L-gulonate, NAD+, and NADP+, whereas its 4 products are (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-dehydro-L-gulonate:NAD(P)+ 2-oxidoreductase. Other names in common use include 3-keto-L-gulonate dehydrogenase, 3-ketogulonate dehydrogenase, 3-keto-L-gulonate dehydrogenase, and 3-ketogulonate dehydrogenase. This enzyme participates in pentose and glucuronate interconversions and ascorbate and aldarate metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3-dehydrosphinganine%20reductase | 3-dehydrosphinganine reductase () also known as 3-ketodihydrosphingosine reductase (KDSR) or follicular variant translocation protein 1 (FVT1) is an enzyme that in humans is encoded by the KDSR gene.
Function
3-dehydrosphinganine reductase catalyzes the chemical reaction:
sphinganine + NADP+ 3-dehydrosphinganine + NADPH + H+
Thus, the two substrates of this enzyme are sphinganine and NADP+, whereas its 3 products are 3-dehydrosphinganine, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in sphingolipid metabolism.
Tissue distribution
Follicular lymphoma variant translocation 1 is a secreted protein which is weakly expressed in hematopoietic tissue.
Clinical significance
FVT1 shows a high rate of transcription in some T cell malignancies and in phytohemagglutinin-stimulated lymphocytes. The proximity of FVT1 to BCL2 suggests that it may participate in the tumoral process.
References
External links
Further reading
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-hydroxy-2-methylbutyryl-CoA%20dehydrogenase | In enzymology, a 3-hydroxy-2-methylbutyryl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ 2-methylacetoacetyl-CoA + NADH + H+
Thus, the two substrates of this enzyme are (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA and NAD+, whereas its 3 products are 2-methylacetoacetyl-CoA, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA:NAD+ oxidoreductase. Other names in common use include 2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase, 2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase, and 2-methyl-3-hydroxy-butyryl CoA dehydrogenase. This enzyme participates in valine, leucine and isoleucine degradation.
Structural studies
As of 20 January 2010, 6 structure have been solved for this class of enzymes, with the PDB accession code , , , , , .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3-hydroxyacyl-CoA%20dehydrogenase | In enzymology, a 3-hydroxyacyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-3-hydroxyacyl-CoA + NAD+ 3-oxoacyl-CoA + NADH + H+
Thus, the two substrates of this enzyme are (S)-3-hydroxyacyl-CoA and NAD+, whereas its 3 products are 3-oxoacyl-CoA, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor.
Isozymes
In humans, the following genes encode proteins with 3-hydroxyacyl-CoA dehydrogenase activity:
HADH – Hydroxyacyl-Coenzyme A dehydrogenase
HSD17B10 – 3-Hydroxyacyl-CoA dehydrogenase type-2
EHHADH – Peroxisomal bifunctional enzyme
HSD17B4 – Peroxisomal multifunctional enzyme type 2
Function
3-Hydroxyacyl CoA dehydrogenase is classified as an oxidoreductase. It is involved in fatty acid metabolic processes. Specifically it catalyzes the third step of beta oxidation; the oxidation of L-3-hydroxyacyl CoA by NAD+. The reaction converts the hydroxyl group into a keto group.
The end product is 3-ketoacyl CoA.
Metabolic pathways
This enzyme participates in 8 metabolic pathways:
fatty acid elongation in mitochondria
fatty acid metabolism
valine, leucine and isoleucine degradation
lysine degradation
tryptophan metabolism
benzoate degradation via coa ligation
butanoate metabolism
caprolactam degradation
Nomenclature
The systematic name of this enzyme class is (S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase. Other names in common use |
https://en.wikipedia.org/wiki/3-hydroxybenzyl-alcohol%20dehydrogenase | In enzymology, a 3-hydroxybenzyl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction
3-hydroxybenzyl alcohol + NADP+ 3-hydroxybenzaldehyde + NADPH + H+
Thus, the two substrates of this enzyme are 3-hydroxybenzyl alcohol and NADP+, whereas its 3 products are 3-hydroxybenzaldehyde, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-hydroxybenzyl-alcohol:NADP+ oxidoreductase. Other names in common use include m-hydroxybenzyl alcohol dehydrogenase, m-hydroxybenzyl alcohol (NADP+) dehydrogenase, and m-hydroxybenzylalcohol dehydrogenase. This enzyme participates in toluene and xylene degradation.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-Hydroxybutyrate%20dehydrogenase | In enzymology, 3-hydroxybutyrate dehydrogenase () is an enzyme that catalyzes the chemical reaction:
(R)-3-hydroxybutanoate + NAD+ acetoacetate + NADH + H+
Thus, the two substrates of this enzyme are (R)-3-hydroxybutanoate and NAD+, whereas its three products are acetoacetate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor.
This enzyme participates in the synthesis and degradation of ketone bodies and the metabolism of butyric acid.
Classification
This enzyme has a classification number of EC 1.1.1.30. The first digit means that this enzyme is an oxidoreductase which means the purpose is to catalyze oxidation and reduction reaction pathways. The following two 1s indicate the subclass and sub-sub of the enzyme. In this case, 1.1.1 means this enzyme is an oxidoreductase that acts on the CH-OH group of the donor molecule using NAD(+) or NADP(+) as the acceptor. The 4th number, or 30 in this case, is the serial number of the enzyme to define it within its sub-subclass. 3-Hydroxybutryate dehydrogenase is also known as beta-hydroxybutyric dehydrogenase and is abbreviated BHBDH. Other common synonyms are shown below.
The systematic name of this enzyme class is (R)-3-hydroxybutanoate:NAD+ oxidoreductase. Other names in common use include:
NAD+-β-hydroxybutyrate dehydrogenase
hydroxybutyrate oxidoreductase
β-hydroxybutyrate dehydrogenase
D-β-hydroxybutyrate dehydrogenase
|
https://en.wikipedia.org/wiki/3-Hydroxybutyryl-CoA%20dehydrogenase | In enzymology, a 3-hydroxybutyryl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-3-hydroxybutanoyl-CoA + NADP+ 3-acetoacetyl-CoA + NADPH + H+
Thus, the two substrates of this enzyme are (S)-3-hydroxybutanoyl-CoA and NADP+; its 3 products are acetoacetyl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-3-hydroxybutanoyl-CoA:NADP+ oxidoreductase. Other names in common use include beta-hydroxybutyryl coenzyme A dehydrogenase, L-(+)-3-hydroxybutyryl-CoA dehydrogenase, BHBD, dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine, dinucleotide phosphate), L-(+)-3-hydroxybutyryl-CoA dehydrogenase, and beta-hydroxybutyryl-CoA dehydrogenase. This enzyme participates in benzoate degradation via coa ligation and butanoate metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3-hydroxyisobutyrate%20dehydrogenase | In enzymology, a 3-hydroxyisobutyrate dehydrogenase () also known as β-hydroxyisobutyrate dehydrogenase or 3-hydroxyisobutyrate dehydrogenase, mitochondrial (HIBADH) is an enzyme that in humans is encoded by the HIBADH gene.
3-Hydroxyisobutyrate dehydrogenase catalyzes the chemical reaction:
3-hydroxy-2-methylpropanoate + NAD+ 2-methyl-3-oxopropanoate + NADH + H+
Thus, the two substrates of this enzyme are 3-hydroxy-2-methylpropanoate and NAD+, whereas its 3 products are 2-methyl-3-oxopropanoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-hydroxy-2-methylpropanoate:NAD+ oxidoreductase. This enzyme participates in valine, leucine and isoleucine degradation.
Function
3-hydroxyisobutyrate dehydrogenase is a tetrameric mitochondrial enzyme that catalyzes the NAD+-dependent, reversible oxidation of 3-hydroxyisobutyrate, an intermediate of valine catabolism, to methylmalonate semialdehyde.
Structural studies
As of late 2007, five structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human 3-hydroxyisobutyrate dehydrogenase, mitochondrial
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure
Human proteins |
https://en.wikipedia.org/wiki/3-hydroxypimeloyl-CoA%20dehydrogenase | In enzymology, a 3-hydroxypimeloyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
3-hydroxypimeloyl-CoA + NAD+ 3-oxopimeloyl-CoA + NADH + H+
Thus, the two substrates of this enzyme are 3-hydroxypimeloyl-CoA and NAD+, whereas its 3 products are 3-oxopimeloyl-CoA, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-hydroxypimeloyl-CoA:NAD+ oxidoreductase. This enzyme participates in benzoate degradation via coa ligation.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-hydroxypropionate%20dehydrogenase | In enzymology, a 3-hydroxypropionate dehydrogenase () is an enzyme that catalyzes the chemical reaction
3-hydroxypropanoate + NAD+ 3-oxopropanoate + NADH + H+
Thus, the two substrates of this enzyme are 3-hydroxypropanoate and NAD+, whereas its 3 products are 3-oxopropanoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-hydroxypropanoate:NAD+ oxidoreductase. This enzyme participates in beta-alanine metabolism and propanoate metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-Ketosteroid%20reductase | In enzymology, a 3-keto-steroid reductase () is an enzyme that catalyzes the chemical reaction
4alpha-methyl-5alpha-cholest-7-en-3beta-ol + NADP+ 4alpha-methyl-5alpha-cholest-7-en-3-one + NADPH + H+
Thus, the two substrates of this enzyme are 4alpha-methyl-5alpha-cholest-7-en-3beta-ol and NADP+, whereas its 3 products are 4alpha-methyl-5alpha-cholest-7-en-3-one, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3beta-hydroxy-steroid:NADP+ 3-oxidoreductase. This enzyme is also called 3-KSR. This enzyme participates in biosynthesis of steroids.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-methylbutanal%20reductase | In enzymology, a 3-methylbutanal reductase () is an enzyme that catalyzes the chemical reaction
3-methylbutan-1-ol + NAD(P)+ 3-methylbutanal + NAD(P)H + H+
The three substrates of this enzyme are 3-methylbutan-1-ol (isoamyl alcohol), NAD+, and NADP+, whereas its four products are 3-methylbutanal, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-methylbutanol:NAD(P)+ oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-amino-6-%285-phosphoribosylamino%29uracil%20reductase | In enzymology, a 5-amino-6-(5-phosphoribosylamino)uracil reductase () is an enzyme that catalyzes the chemical reaction
5-amino-6-(5-phosphoribitylamino)uracil + NADP+ 5-amino-6-(5-phosphoribosylamino)uracil + NADPH + H+
Thus, the two substrates of this enzyme are 5-amino-6-(5-phosphoribitylamino)uracil and NADP+, whereas its 3 products are 5-amino-6-(5-phosphoribosylamino)uracil, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5-amino-6-(5-phosphoribitylamino)uracil:NADP+ 1'-oxidoreductase. This enzyme is also called aminodioxyphosphoribosylaminopyrimidine reductase. This enzyme participates in riboflavin metabolism.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/6-endo-hydroxycineole%20dehydrogenase | In enzymology, a 6-endo-hydroxycineole dehydrogenase () is an enzyme that catalyzes the chemical reaction
6-endo-hydroxycineole + NAD+ 6-oxocineole + NADH + H+
Thus, the two substrates of this enzyme are 6-endo-hydroxycineole and NAD+, whereas its 3 products are 6-oxocineole, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 6-endo-hydroxycineole:NAD+ 6-oxidoreductase. This enzyme participates in terpenoid biosynthesis.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/6-hydroxyhexanoate%20dehydrogenase | In enzymology, a 6-hydroxyhexanoate dehydrogenase () is an enzyme that catalyzes the chemical reaction
6-hydroxyhexanoate + NAD+ 6-oxohexanoate + NADH + H+
Thus, the two substrates of this enzyme are 6-hydroxyhexanoate and NAD+, whereas its 3 products are 6-oxohexanoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 6-hydroxyhexanoate:NAD+ oxidoreductase. This enzyme participates in caprolactam degradation.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/6-pyruvoyltetrahydropterin%202%27-reductase | In enzymology, a 6-pyruvoyltetrahydropterin 2'-reductase () is an enzyme that catalyzes the chemical reaction
6-lactoyl-5,6,7,8-tetrahydropterin + NADP+ 6-pyruvoyltetrahydropterin + NADPH + H+
Thus, the two substrates of this enzyme are 6-lactoyl-5,6,7,8-tetrahydropterin and NADP+, whereas its 3 products are 6-pyruvoyltetrahydropterin, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 6-lactoyl-5,6,7,8-tetrahydropterin:NADP+ 2'-oxidoreductase. Other names in common use include 6-pyruvoyltetrahydropterin reductase, 6PPH4(2'-oxo) reductase, 6-pyruvoyl tetrahydropterin (2'-oxo)reductase, 6-pyruvoyl-tetrahydropterin 2'-reductase, and pyruvoyl-tetrahydropterin reductase. This enzyme participates in folate biosynthesis.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/7alpha-hydroxysteroid%20dehydrogenase | In enzymology, a 7alpha-hydroxysteroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + NAD+ 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
Thus, the two substrates of this enzyme are 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate and NAD+, whereas its 3 products are 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 7alpha-hydroxysteroid:NAD+ 7-oxidoreductase. Other names in common use include 7alpha-hydroxy steroid dehydrogenase, and 7alpha-HSDH.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/7beta-hydroxysteroid%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:7beta-hydroxysteroid dehydrogenase (NADP+)}}
In enzymology, a 7beta-hydroxysteroid dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
a 7beta-hydroxysteroid + NADP+ a 7-oxosteroid + NADPH + H+
Thus, the two substrates of this enzyme are 7beta-hydroxysteroid and NADP+, whereas its 3 products are 7-oxosteroid, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 7beta-hydroxysteroid:NADP+ 7-oxidoreductase. Other names in common use include NADP+-dependent 7beta-hydroxysteroid dehydrogenase, and 7beta-hydroxysteroid dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/8-oxocoformycin%20reductase | In enzymology, a 8-oxocoformycin reductase () is an enzyme that catalyzes the chemical reaction
coformycin + NADP+ 8-oxocoformycin + NADPH + H+
Thus, the two substrates of this enzyme are coformycin and NADP+, whereas its 3 products are 8-oxocoformycin, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is coformycin:NADP+ 8-oxidoreductase. This enzyme is also called 8-ketodeoxycoformycin reductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28-%29-borneol%20dehydrogenase | In enzymology, a (−)-borneol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(−)-borneol + NAD (−)-camphor + NADH + H
Thus, the two substrates of this enzyme are (−)-borneol and NAD, whereas its 3 products are (−)-camphor, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (−)-borneol:NAD oxidoreductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28%2B%29-borneol%20dehydrogenase | In enzymology, a (+)-borneol dehydrogenase () is an enzyme that increases the rate of, or catalyzes, the chemical reaction
(+)-borneol + NAD (+)-camphor + NADH + H
Thus, the two substrates of this enzyme are (+)-borneol and NAD, whereas its 3 products are (+)-camphor, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (+)-borneol:NAD oxidoreductase. This enzyme is also called bicyclic monoterpenol dehydrogenase.
References
External links
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28-%29-menthol%20dehydrogenase | A (−)-menthol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(−)-menthol + NADP (−)-menthone + NADPH + H,
i.e., catalyses the breakdown of menthol. Thus, the two substrates of this enzyme are (−)-menthol and NADP, whereas its 3 products are (−)-menthone, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (−)-menthol:NADP oxidoreductase. This enzyme is also called monoterpenoid dehydrogenase. This enzyme participates in monoterpenoid biosynthesis.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28%2B%29-neomenthol%20dehydrogenase | In enzymology, a (+)-neomenthol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(+)-neomenthol + NADP (−)-menthone + NADPH + H
Thus, the two substrates of this enzyme are (+)-neomenthol and NADP, whereas its 3 products are (−)-menthone, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (+)-neomenthol:NADP oxidoreductase. This enzyme is also called monoterpenoid dehydrogenase. This enzyme participates in monoterpenoid biosynthesis.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28R%29-2-hydroxyacid%20dehydrogenase | In enzymology, a (R)-2-hydroxyacid dehydrogenase () is an enzyme that catalyzes the chemical reaction
(2R)-3-sulfolactate + NAD(P) 3-sulfopyruvate + NAD(P)H + H
The 3 substrates of this enzyme are (2R)-3-sulfolactic acid, NAD, and NADP, whereas its 4 products are 3-sulfopyruvic acid, NADH, NADPH, and H. This enzyme is important in the metabolism of archaea, particularly their biosynthesis of coenzymes such as coenzyme M, tetrahydromethanopterin and methanofuran.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (R)-2-hydroxyacid:NAD(P) oxidoreductase. Other names in common use include (R)-sulfolactate:NAD(P) oxidoreductase, L-sulfolactate dehydrogenase, ComC, and (R)-sulfolactate dehydrogenase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/%28R%29-2-hydroxy-fatty-acid%20dehydrogenase | In enzymology, a (R)-2-hydroxy-fatty-acid dehydrogenase () is an enzyme that catalyzes the chemical reaction
(R)-2-hydroxystearate + NAD 2-oxostearate + NADH + H
Thus, the two substrates of this enzyme are (R)-2-hydroxystearate and NAD, whereas its 3 products are 2-oxostearate, NADH, and H. This reaction is important in fatty acid metabolism.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (R)-2-hydroxystearate:NAD oxidoreductase. Other names in common use include D-2-hydroxy fatty acid dehydrogenase, and 2-hydroxy fatty acid oxidase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28R%29-3-hydroxyacid-ester%20dehydrogenase | In enzymology, a (R)-3-hydroxyacid-ester dehydrogenase () is an enzyme that catalyzes the chemical reaction
ethyl (R)-3-hydroxyhexanoate + NADP ethyl 3-oxohexanoate + NADPH + H
Thus, the two substrates of this enzyme are ethyl (R)-3-hydroxyhexanoate and NADP, whereas its 3 products are ethyl 3-oxohexanoate, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is ethyl-(R)-3-hydroxyhexanoate:NADP 3-oxidoreductase. This enzyme is also called 3-oxo ester (R)-reductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28R%29-4-hydroxyphenyllactate%20dehydrogenase | (R)-4-hydroxyphenyllactate dehydrogenase () is an enzyme that catalyzes a chemical reaction
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+ 3-(4-hydroxyphenyl)pyruvate + NAD(P)H + H
The 3 substrates of this enzyme are (R)-3-(4-hydroxyphenyl)lactate, NAD, and NADP, whereas its 4 products are 3-(4-hydroxyphenyl)pyruvate, NADH, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (R)-3-(4-hydroxyphenyl)lactate:NAD(P) 2-oxidoreductase. Other names in common use include (R)-aromatic lactate dehydrogenase, and D-hydrogenase, D-aryllactate. This enzyme participates in tyrosine and phenylalanine catabolism.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28R%29-aminopropanol%20dehydrogenase | In enzymology, a (R)-aminopropanol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(R)-1-aminopropan-2-ol + NAD aminoacetone + NADH + H
Thus, the two substrates of this enzyme are (R)-1-aminopropan-2-ol and NAD, whereas its 3 products are aminoacetone, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (R)-1-aminopropan-2-ol:NAD oxidoreductase. Other names in common use include L-aminopropanol dehydrogenase, 1-aminopropan-2-ol-NAD dehydrogenase, L()-1-aminopropan-2-ol:NAD oxidoreductase, 1-aminopropan-2-ol-dehydrogenase, DL-1-aminopropan-2-ol: NAD dehydrogenase, and L()-1-aminopropan-2-ol-NAD/NADP oxidoreductase. This enzyme participates in glycine, serine and threonine metabolism. It requires potassium as a cofactor.
References
EC 1.1.1
NADH-dependent enzymes
Potassium enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-%28imidazol-5-yl%29lactate%20dehydrogenase | In enzymology, a 3-(imidazol-5-yl)lactate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-3-(imidazol-5-yl)lactate + NAD(P)+ 3-(imidazol-5-yl)pyruvate + NAD(P)H + H+
The 3 substrates of this enzyme are (S)-3-(imidazol-5-yl)lactate, NAD+, and NADP+, whereas its 4 products are 3-(imidazol-5-yl)pyruvate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-3-(imidazol-5-yl)lactate:NAD(P)+ oxidoreductase. This enzyme is also called imidazol-5-yl lactate dehydrogenase.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-2-hydroxy-fatty-acid%20dehydrogenase | In enzymology, a (S)-2-hydroxy-fatty-acid dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-2-hydroxystearate + NAD 2-oxostearate + NADH + H
Thus, the two substrates of this enzyme are (S)-2-hydroxystearate and NAD, whereas its 3 products are 2-oxostearate, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (S)-2-hydroxystearate:NAD oxidoreductase. Other names in common use include dehydrogenase, L-2-hydroxy fatty acid, L-2-hydroxy fatty acid dehydrogenase, and 2-hydroxy fatty acid oxidase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-3-hydroxyacid-ester%20dehydrogenase | In enzymology, a (S)-3-hydroxyacid-ester dehydrogenase () is an enzyme that catalyzes the chemical reaction
ethyl (S)-3-hydroxyhexanoate + NADP ethyl 3-oxohexanoate + NADPH + H
Thus, the two substrates of this enzyme are ethyl (S)-3-hydroxyhexanoate and NADP, whereas its 3 products are ethyl 3-oxohexanoate, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is ethyl-(S)-3-hydroxyhexanoate:NADP 3-oxidoreductase. This enzyme is also called 3-oxo ester (S)-reductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28%2B%29-sabinol%20dehydrogenase | In enzymology, a (+)-sabinol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(+)-cis-sabinol + NAD (+)-sabinone + NADH + H
Thus, the two substrates of this enzyme are (+)-cis-sabinol and NAD, whereas its 3 products are (+)-sabinone, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (+)-cis-sabinol:NAD oxidoreductase. This enzyme is also called (+)-cis-sabinol dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-oxoacyl-%28acyl-carrier-protein%29%20reductase | In enzymology, a 3-oxoacyl-[acyl-carrier-protein] reductase () is an enzyme that catalyzes the chemical reaction
3-oxoacyl-[acyl-carrier-protein](ACP) + NADPH + H+ (3R)-3-hydroxyacyl-[acyl-carrier-protein](ACP) + NADP+
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group as hydride donor with NAD+ or NADP+ as hydride acceptor. The systematic name of this enzyme class is (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase. Other names in common use include beta-ketoacyl-[acyl-carrier protein](ACP) reductase, beta-ketoacyl acyl carrier protein (ACP) reductase, beta-ketoacyl reductase, beta-ketoacyl thioester reductase, beta-ketoacyl-ACP reductase, beta-ketoacyl-acyl carrier protein reductase, 3-ketoacyl acyl carrier protein reductase, 3-ketoacyl ACP reductase, NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase, and 3-oxoacyl-[ACP]reductase. This enzyme participates in fatty acid biosynthesis and polyunsaturated fatty acid biosynthesis.
Structural studies
As of late 2007, 21 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/%28S%29-carnitine%203-dehydrogenase | In enzymology, a (S)-carnitine 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-carnitine + NAD 3-dehydrocarnitine + NADH + H
Thus, the two substrates of this enzyme are (S)-carnitine and NAD, whereas its 3 products are 3-dehydrocarnitine, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (S)-carnitine:NAD oxidoreductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%2CS%29-butanediol%20dehydrogenase | In enzymology, a (S,S)-butanediol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S,S)-butane-2,3-diol + NAD acetoin + NADH + H
Thus, the two substrates of this enzyme are (S,S)-butane-2,3-diol and NAD, whereas its 3 products are acetoin, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (S,S)-butane-2,3-diol:NAD oxidoreductase. Other names in common use include L-butanediol dehydrogenase, L-BDH, and L()-2,3-butanediol dehydrogenase (L-acetoin forming). This enzyme participates in butanoic acid metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-usnate%20reductase | In enzymology, a (S)-usnate reductase () is an enzyme that catalyzes the chemical reaction
(6R)-2-acetyl-6-(3-acetyl-2,4,6-trihydroxy-5-methylphenyl)-3-hydroxy-6- methyl-2,4-cyclohexadien-1-one + NAD (S)-usnic acid + NADH + H
In the reverse direction, (S)-usnate is reduced by NADH with cleavage of the ether bond to form a 7-hydroxy group.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is reduced-(S)-usnate:NAD oxidoreductase (ether-bond-forming). This enzyme is also called L-usnic acid dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-oxoacyl-%28acyl-carrier-protein%29%20reductase%20%28NADH%29 | In enzymology, a 3-oxoacyl-[acyl-carrier-protein] reductase (NADH) () is an enzyme that catalyzes the chemical reaction
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NAD+ 3-oxoacyl-[acyl-carrier-protein] + NADH + H+
Thus, the two substrates of this enzyme are [[(3R)-3-hydroxyacyl-[acyl-carrier-protein]]] and NAD+, whereas its 3 products are [[3-oxoacyl-[acyl-carrier-protein]]], NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NAD+ oxidoreductase. Other names in common use include 3-oxoacyl-[acyl carrier protein] (reduced nicotinamide adenine, dinucleotide) reductase, and 3-oxoacyl-[acyl-carrier-protein] reductase (NADH).
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28%2B%29-trans-carveol%20dehydrogenase | In enzymology, a (+)-trans-carveol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(+)-trans-carveol + NAD (+)-(S)-carvone + NADH + H
Thus, the two substrates of this enzyme are (+)-trans-carveol and NAD, whereas its 3 products are (+)-(S)-carvone, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (+)-trans-carveol:NAD oxidoreductase. This enzyme is also called carveol dehydrogenase. This enzyme participates in monoterpenoid biosynthesis and the degradation of the terpenes limonene and pinene.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/O%C4%BE%C5%A1avka%2C%20Stropkov%20District | Oľšavka (; ) is a village and municipality in Stropkov District in the Prešov Region of north-eastern Slovakia.
References
External links
http://www.statistics.sk/mosmis/eng/run.html
Villages and municipalities in Stropkov District
Šariš |
https://en.wikipedia.org/wiki/Czenakowski%20distance | The Czenakowski distance (sometimes shortened as CZD) is a per-pixel quality metric that estimates quality or similarity by measuring differences between pixels. Because it compares vectors with strictly non-negative elements, it is often used to compare colored images, as color values cannot be negative. This different approach has a better correlation with subjective quality assessment than PSNR.
Definition
Androutsos et al. give the Czenakowski coefficient as follows:
Where a pixel is being compared to a pixel on the k-th band of color – usually one for each of red, green and blue.
For a pixel matrix of size , the Czenakowski coefficient can be used in an arithmetic mean spanning all pixels to calculate the Czenakowski distance as follows:
Where is the (i, j)-th pixel of the k-th band of a color image and, similarly, is the pixel that it is being compared to.
Uses
In the context of image forensics – for example, detecting if an image has been manipulated –, Rocha et al. report the Czenakowski distance is a popular choice for Color Filter Array (CFA) identification.
References
Computer graphics |
https://en.wikipedia.org/wiki/Acetoxyketobemidone | Acetoxyketobemidone (O-Acetylketobemidone) is an opioid analgesic that is an acetylated derivative of ketobemidone. It was developed in the 1950s during research into analogues of pethidine and was assessed by the United Nations Office on Drugs and Crime but was not included on the list of drugs under international control, probably because it was not used in medicine or widely available. Nevertheless, acetoxyketobemidone is controlled as an ester of ketobemidone, which is included in Schedule I of the Single Convention on Narcotic Drugs of 1961.
Presumably acetoxyketobemidone produces similar effects to ketobemidone and other opioids, such as analgesia and sedation, along with side effects such as nausea, itching, vomiting and respiratory depression which may be harmful or fatal.
References
UNODC Bulletin on Narcotics 1954
Synthetic opioids
4-Phenylpiperidines
Ketones
Phenol esters
Acetate esters
Mu-opioid receptor agonists |
https://en.wikipedia.org/wiki/List%20of%20R-7%20launches | This is a list of launches made by the R-7 Semyorka ICBM, and its derivatives. All launches are orbital satellite launches, unless stated otherwise.
Due to the size of the list, it has been split into several smaller articles:
List of R-7 launches (1957–1959)
List of R-7 launches (1960–1964)
List of R-7 launches (1965–1969)
List of R-7 launches (1970–1974)
List of R-7 launches (1975–1979)
List of R-7 launches (1980–1984)
List of R-7 launches (1985–1989)
List of R-7 launches (1990–1994)
List of R-7 launches (1995–1999)
List of R-7 launches (2000–2004)
List of R-7 launches (2005–2009)
List of R-7 launches (2010–2014)
List of R-7 launches (2015–2019)
List of R-7 launches (2020–2024)
Statistics are up-to-date .
References |
https://en.wikipedia.org/wiki/Thomas%20de%20Melsonby | Thomas de Melsonby (died after 1244) was a medieval Bishop of Durham-elect and Prior of Durham.
Melsonby was the son of the rector of Melsonby. He was prior of a cell at Coldingham before being elected prior of Durham Cathedral in about 1233. He was elected to the see of Durham on 1 June 1237 but King Henry III of England objected. After lawsuits, Melsonby resigned the bishopric. He remained prior until 1244 when he resigned that office. He died sometime after 1244.
Citations
References
Bishops of Durham
Priors of Durham
13th-century English Roman Catholic bishops |
https://en.wikipedia.org/wiki/Katz%27s%20back-off%20model | Katz back-off is a generative n-gram language model that estimates the conditional probability of a word given its history in the n-gram. It accomplishes this estimation by backing off through progressively shorter history models under certain conditions. By doing so, the model with the most reliable information about a given history is used to provide the better results.
The model was introduced in 1987 by Slava M. Katz. Prior to that, n-gram language models were constructed by training individual models for different n-gram orders using maximum likelihood estimation and then interpolating them together.
Method
The equation for Katz's back-off model is:
where
C(x) = number of times x appears in training
wi = ith word in the given context
Essentially, this means that if the n-gram has been seen more than k times in training, the conditional probability of a word given its history is proportional to the maximum likelihood estimate of that n-gram. Otherwise, the conditional probability is equal to the back-off conditional probability of the (n − 1)-gram.
The more difficult part is determining the values for k, d and α.
is the least important of the parameters. It is usually chosen to be 0. However, empirical testing may find better values for k.
is typically the amount of discounting found by Good–Turing estimation. In other words, if Good–Turing estimates as , then
To compute , it is useful to first define a quantity β, which is the left-over probability mass fo |
https://en.wikipedia.org/wiki/MK8 | MK8 may refer to:
Mario Kart 8, a 2014 Wii U kart racing video game in the Mario Kart series
Kallikrein 8, an enzyme
Mitsubishi Kinsei (also MK8), a 14-cylinder, air-cooled, twin-row radial aircraft engine
Volkswagen Golf Mk8, the eighth generation of the Volkswagen Golf vehicle |
https://en.wikipedia.org/wiki/Ruskovce%2C%20Sobrance%20District | Ruskovce () is a village and municipality in the Sobrance District in the Košice Region of east Slovakia.
References
External links
http://www.statistics.sk/mosmis/eng/run.html
Villages and municipalities in Sobrance District |
https://en.wikipedia.org/wiki/David%20Provan%20%28footballer%2C%20born%201941%29 | David Provan (11 March 1941 – 26 November 2016) was a Scottish professional footballer, who played for Rangers, Crystal Palace, Plymouth Argyle and St Mirren. Provan also played for Scotland and the Scottish League XI.
Career
Provan was a product of the Rangers youth team and played as a full back. He made his debut on 27 December 1958, in a league match away to Third Lanark which Rangers won 3–2. He helped the club win a domestic treble in 1963–64 and played in the 1967 European Cup Winners' Cup Final, which Rangers lost 1–0 to Bayern Munich. Provan is one of the players elected to Rangers' Hall of Fame.
He left the club in June 1970 and joined English club Crystal Palace, although he was not there for long, making only two senior appearances in total, before moving on in March 1971, to Plymouth Argyle. He stayed at Plymouth for five seasons and made over 100 appearances.
Provan subsequently played for St Mirren where he finished his senior career in 1975, and began his coaching career under then-manager Alex Ferguson. He later went on to manage Albion Rovers from 1987 to 1991, leading the club to the Scottish Football League Second Division title in 1988–9.
Rangers FC announced on 26 November 2016 that Provan had died, following a long illness.
References
External links
1941 births
2016 deaths
Footballers from Falkirk
Men's association football fullbacks
Scottish men's footballers
Scotland men's international footballers
Rangers F.C. players
Crystal Palace F.C. play |
https://en.wikipedia.org/wiki/Wolf%20summation | The Wolf summation is a method for computing the electrostatic interactions of systems (e.g. crystals). This method is generally more computationally efficient than the Ewald summation. It was proposed by Dieter Wolf.
References
See also
Wolf method on SklogWiki
Potential theory
Computational physics |
https://en.wikipedia.org/wiki/Gotta%20Lotta%20That | "Gotta Lotta That" is a song written by Bernice Bedwell in 1958 and published by Song Productions, BMI. It was first recorded by Gene Summers and His Rebels in 1958 and issued by Jan/Jane Records. The "Gotta Lotta That" recording session took place at the Liberty Records Studios in Hollywood, California and featured Rene Hall and James McClung on guitar, Plas Johnson on saxophone, Earl Palmer on drums, and George "Red" Callendar on bass. The flipside of "Gotta Lotta That" was "Nervous".
Reviews
Billboard - June 1958 - 'Reviews of New Pop Records' by Gene Summers - "Gotta Lotta That" - "A swinging, blues effort that really moves and rocks. Good sound and solid performance by Summers with fine guitar support".
"Gotta Lotta That" cover versions
Johnny Devlin - New Zealand
Andy Lee & Tennessee Rain - Germany
Rudy Lacrioux & The All-Stars - UK
References
Gene Summers discography from Rocky Productions, France
Gene Summers discography from Wangdangdula Finland
Gene Summers session data from Tapio's Fin-A-Billy, Finland
Sources
Billboard Magazine- June 1958 Reviews of New Pop Records United States
Liner notes "The Ultimate School Of Rock & Roll" 1997 United States
Johnny Devlin, "How Would Ya Be" LP, Prestige Records PLP 1201 New Zealand, 1958
Andy Lee & Tennessee Rain, "I Don't Wanna Be Lonely Tonight" CD, Grunwald Records Germany, 2004
Rudy LaCrioux & The All-Stars, "Let's Have A Ball" CD, Spendrift Records CD 107 UK 2001
"Cover Versions Of The Songs Made Famous By Gene Summer |
https://en.wikipedia.org/wiki/I%27ll%20Never%20Be%20Lonely | I'll Never Be Lonely is a song written by Mary Tarver in 1958 and published by Ted Music, BMI. It was first recorded by Gene Summers and His Rebels in 1958 and issued by Jan/Jane Records that same year. "I'll Never Be Lonely" was recorded at Master Recorders in Los Angeles, California in 1958 during the "School of Rock 'n Roll"/"Straight Skirt" sessions. Musicians featured were the original Rebels: Gene Summers on vocals and guitar, James McClung on lead guitar, Gary Moon on drums, and Benny Williams on slap bass. The flipside of "I'll Never Be Lonely" was "Twixteen".
Reviews
BILLBOARD MAGAZINE - January 26, 1959 Reviews of New Pop Records, page 48
GENE SUMMERS
I'll Never Be Lonely ***
JANE 106 - Gene Summers sells this rockaballad with warmth, helped by a chorus and a big beat from the combo. It's in the current groove and has a chance. (Ted, BMI)
References
Gene Summers discography from Rocky Productions, France
Gene Summers discography from Wangdangdula Finland
Gene Summers session data from Tapio's Fin-A-Billy, Finland
Sources
Billboard (magazine) - January 26, 1959 Reviews of New Pop Records, page 48 United States
Liner notes "The Ultimate School Of Rock & Roll" 1997 United States
"Cover Versions Of The Songs Made Famous By Gene Summers" 2007 United States
Article and sessionography in issue 15 (1977) of New Kommotion Magazine UK
Article and sessionography in issue 23 (1980) of New Kommotion Magazine UK
Feature article and sessionography in issue 74 (1999) of Rockin |
https://en.wikipedia.org/wiki/1996%E2%80%9397%20Mexican%20Primera%20Divisi%C3%B3n%20season | The following are statistics of Mexico's Primera División for the 1996–97 season.
Overview
Teams
Torneo Invierno 1996
Primera División de México (Mexican First Division) Invierno 1996 is a Mexican football tournament - one of two short tournaments that take up the entire year to determine the champion(s) of Mexican football. It began on Friday, August 9, 1996, and ran until November 24, when the regular season ended. In the final Santos defeated Necaxa and became champions for the 1st time.
Final standings (groups)
League table
Results
Top goalscorers
Players sorted first by goals scored, then by last name. Only regular season goals listed.
Source: MedioTiempo
Playoffs
Repechage
Toros Neza won 4–2 on aggregate.
Atlas won 6–3 on aggregate.
Bracket
Quarterfinals
Toros Neza won 9–2 on aggregate.
Santos Laguna won 4–2 on aggregate.
Necaxa won 3–2 on aggregate.
Puebla won 2–1 on aggregate.
Semifinals
Santos Laguna won 5–2 on aggregate.
Necaxa won 7–3 on aggregate.
Finals
First leg
Second leg
Santos Laguna won 4–3 on aggregate.
Torneo Verano 1997
Primera División de México (Mexican First Division) Verano 1997 is a Mexican football tournament - one of two short tournaments that take up the entire year to determine the champion(s) of Mexican football. It began on Saturday, January 11, 1997, and ran until May 4, when the regular season ended. In the final Guadalajara defeated Toros Neza and became champions for the 10th time.
Final standings (groups)
League |
https://en.wikipedia.org/wiki/Parser%20%28programming%20language%29 | Parser is a scripting language developed by Art. Lebedev Studio used for web development and server-side scripting.
The reference compiler for the language was developed in C++ by studio employees Konstantin Morshnev and Alexander Petrosyan to automate often repeated tasks, especially maintenance of already existing websites. It was used in many web projects of the studio. In March 2006, revision three was released as free software under a GPL license and it is now used in other websites, mostly in Russia (according to a partial list at the language website).
Originally, Parser was merely a simple macro processing language but revision three introduced object-oriented programming features.
The language supports technologies needed for common web design tasks: XML, Document Object Model (DOM), Perl Compatible Regular Expressions (PCRE) and others.
Parser supports web server integration via:
Common Gateway Interface (CGI)
Internet Server Application Programming Interface (ISAPI)
Apache module (mod_parser3)
See also
Parsing
References
External links
Free compilers and interpreters
Procedural programming languages
Macro programming languages
Scripting languages
Programming languages created in 1997 |
https://en.wikipedia.org/wiki/Allylprodine | Allylprodine is an opioid analgesic that is an analog of prodine. It was discovered by Hoffman-La Roche in 1957 during research into the related drug pethidine. Derivatives were tested to prove the theory that phenolic and non-phenolic opioids bind at different sites of the opiate receptor.
Allylprodine is more potent as an analgesic than similar drugs such as α-prodine, and the 3R,4S-isomer is 23 times more potent than morphine, due to the allyl group binding to an additional amino acid target in the binding site on the μ-opioid receptor. It is also stereoselective, with one isomer being much more active.
When modeled in three dimensions, the alkene overlays the alkenes found in 14-cinnamoyloxycodeinone and in 14-allyloxycodeinone, re-enforcing the presence of an interaction of the alkene.
Allylprodine produces similar effects to other opioids, such as analgesia and sedation, along with side effects such as nausea, itching, vomiting and respiratory depression which may be harmful or fatal.
Legal status
Allylprodine is regulated in most countries as is morphine, including being in Schedule I of the US Controlled Substances Act 1970 as a Narcotic with ACSCN 9602 and a 2014 annual aggregate manufacturing quota of 2 grammes.
Australia
Allylprodine is considered a Schedule 9 prohibited substance in Australia under the Poisons Standard (February 2017). A Schedule 9 substance is a substance which may be abused or misused, the manufacture, possession, sale or use of which sho |
https://en.wikipedia.org/wiki/Heteromer | A heteromer is something that consists of different parts; the antonym of homomeric. Examples are:
Biology
Spinal neurons that pass over to the opposite side of the spinal cord.
A protein complex that contains two or more different polypeptides.
Pharmacology
Ligand-gated ion channels such as the nicotinic acetylcholine receptor and GABAA receptor are composed of five subunits arranged around a central pore that opens to allow ions to pass through. There are many different subunits available that can come together in a wide variety of combinations to form different subtypes of the ion channel. Sometimes the channel can be made from only one type of subunit, such as the α7 nicotinic receptor, which is made up from five α7 subunits, and so is a homomer rather than a heteromer, but more commonly several different types of subunit will come together to form a heteromeric complex (e.g., the α4β2 nicotinic receptor, which is made up from two α4 subunits and three β2 subunits). Because the different ion channel subtypes are expressed to different extents in different tissues, this allows selective modulation of ion transport and means that a single neurotransmitter can produce varying effects depending on where in the body it is released.
G protein-coupled receptors are composed of seven membrane-spanning alpha-helical segments that are usually linked together into a single folded chain to form the receptor complex. However, research has demonstrated that a number of GPCRs are |
https://en.wikipedia.org/wiki/Spinal%20neuron | A spinal neuron is a neuron in the spinal cord.
Some spinal neurons are heteromeric, i.e. they have processes pass over to the opposite side of the spinal cord
References
Spinal cord
Neurons |
https://en.wikipedia.org/wiki/Indium%20gallium%20aluminium%20nitride | Indium gallium aluminium nitride (InGaAlN, AlInGaN) is a GaN-based compound semiconductor. It is usually prepared by epitaxial growth, such as metalorganic chemical vapour deposition (MOCVD), molecular-beam epitaxy (MBE), pulsed laser deposition (PLD), etc. This material is used for specialist opto-electronics applications, often in blue laser diodes and LEDs.
See also
Indium aluminium nitride
References
III-V semiconductors
Indium compounds
Gallium compounds
Aluminium compounds
Nitrides |
https://en.wikipedia.org/wiki/NEC%20SX-9 | The SX-9 is a NEC SX supercomputer built by NEC Corporation. The SX-9 Series implements an SMP system in a compact node module and uses an enhanced version of the single chip vector processor that was introduced with the SX-6. The NEC SX-9 processors run at 3.2 GHz, with eight-way replicated vector pipes, each having two multiply units and two addition units; this results in a peak vector performance of 102.4 gigaFLOPS. For non-vectorized code, there is a scalar processor that runs at half the speed of the vector unit, i.e. 1.6 GHz. Up to 16 CPUs and 1 terabyte of memory may be used in a single node. Each node is packaged in an air-cooled cabinet, similar in size to a standard 42U computer rack. The SX-9 series ranges from the single-node SX-9/B system with 4 CPUs to the maximum expansion stage with 512 nodes, 8,192 CPUs, and 970 TFLOPS peak performance. There is up to 4 TB/s shared memory bandwidth per node and 2×128 GB/s node interconnect bandwidth. The operating system is NEC's SUPER-UX, a Unix-like OS.
The SX-9 had the world's fastest vector CPU core. A fully equipped system with 512 nodes would have been the world's fastest supercomputer at the time of release in the first quarter of 2008, with a performance of 819 TFLOPS. The SX-9 was discontinued in 2015.
The German national meteorological service (DWD) operated two independent SX-9 clusters, with 976 processors, 31,232 GB of RAM and 98 TFLOPS performance in total.
NEC Published Product Highlights
1.6 TFLOPS max |
https://en.wikipedia.org/wiki/Petroleum%20transport | Petroleum transport is the transportation of petroleum and derivatives such as gasoline (petrol). Petroleum products are transported via rail cars, trucks, tanker vessels, and pipeline networks. The method used to move the petroleum products depends on the volume that is being moved and its destination. Even the modes of transportation on land such as pipeline or rail have their own strengths and weaknesses. One of the key differences are the costs associated with transporting petroleum though pipeline or rail. The biggest problems with moving petroleum products are pollution related and the chance of spillage. Petroleum oil is very hard to clean up and is very toxic to living animals and their surroundings.
Methods
Marine Vessels
Marine Vessels and barges can transport this petroleum all around the world. Because these vessels can carry a lot of fuel, the amount it costs per barrel to move this oil is very cheap. These tankers are also the only practical way to move crude oil across the oceans. Usually the larger tankers are used to transport this fuel on a global scale, taking fuel from one continent to the other. Barges are more like tankers, but smaller and do not have any method of propulsion to move them. They are often pushed or towed by tugs. This makes barges very ineffective for transporting this oil for long distances. Barges are also not applicable for traveling across rough seas, so they are used in calmer waters. However, these barges are usually used for t |
https://en.wikipedia.org/wiki/DnaE | DnaE, the gene product of dnaE, is the catalytic α subunit of DNA polymerase III, acting as a DNA polymerase. This enzyme is only found in prokaryotes.
References
Bacterial proteins
DNA replication |
https://en.wikipedia.org/wiki/DnaH | dnaH is a gene involved in DNA replication.
References
DNA replication |
https://en.wikipedia.org/wiki/DnaI | DnaI is a protein that is part of the primosome involved in prokaryotic DNA replication. In Bacillus subtilis, genetic analysis has revealed three primosomal proteins, DnaB, DnaD, and DnaI, that have no obvious homologues in E. coli. They are involved in primosome function both at arrested replication forks and at the chromosomal origin.
Bacterial proteins
DNA replication |
https://en.wikipedia.org/wiki/DnaS | dnaS or dut is a gene involved in DNA replication in Escherichia coli. It encodes dUTP nucleotidohydrolase, an enzyme responsible for catalyzing the conversion of dUTP to dUMP, thereby ensuring that the organism's DNA contains the nucleobase thymine instead of uracil.
See also
DUT, the human version of this gene
dnaA
dnaB
dnaC
dnaE
dnaG
dnaH
dnaI
dnaN
dnaP
dnaQ
dnaX
dnaZ
References
DNA replication |
https://en.wikipedia.org/wiki/Stream%20Processors%2C%20Inc. | Stream Processors, Inc. (SPI), was a Silicon Valley-based fabless semiconductor company specializing in the design and manufacture of high-performance digital signal processors for applications including video surveillance, multi-function printers and video conferencing. The company ceased operations in 2009.
Company history
Foundational work in stream processing was initiated in
1995 by a research team led by MIT professor Bill Dally. In 1996, he moved to Stanford University where he continued this work, receiving a multimillion-dollar
grant from DARPA with additional resources from Intel and
Texas Instruments to fund the development of a project called "Imagine"
- the first stream processor chip and accompanying compiler tools.
The Imagine Project
The goal of the Imagine project was to develop a
C programmable signal and image processor intended to provide both the performance density and efficiency of a
special-purpose processor (such as a hard-wired ASIC). The project successfully demonstrated the advantages of stream processing. Details on the Imagine project and its results are posted
on the Stanford Imagine project page. The work also showed that a number of applications
ranging from wireless baseband processing, 3D graphics, encryption, IP
forwarding to video processing could take advantage of the efficiency of stream processing. This research inspired other
designs such as GPUs from ATI Technologies as well as the Cell microprocessor from Sony, Toshiba, and IB |
https://en.wikipedia.org/wiki/Secondary%20cell%20wall | The secondary cell wall is a structure found in many plant cells, located between the primary cell wall and the plasma membrane. The cell starts producing the secondary cell wall after the primary cell wall is complete and the cell has stopped expanding.
Secondary cell walls provide additional protection to cells and rigidity and strength to the larger plant. These walls are constructed of layered sheaths of cellulose microfibrils, wherein the fibers are in parallel within each layer. The inclusion of lignin makes the secondary cell wall less flexible and less permeable to water than the primary cell wall. In addition to making the walls more resistant to degradation, the hydrophobic nature of lignin within these tissues is essential for containing water within the vascular tissues that carry it throughout the plant.
The secondary cell wall consists primarily of cellulose, along with other polysaccharides, lignin, and glycoprotein. It sometimes consists of three distinct layers - S1, S2 and S3 - where the direction of the cellulose microfibrils differs between the layers. The direction of the microfibrils is called microfibril angle (MFA). In the secondary cell wall of fibres of trees a low microfibril angle is found in the S2-layer, while S1 and S3-layers show a higher MFA . However, the MFA can also change depending on the loads on the tissue. It has been shown that in reaction wood the MFA in S2-layer can vary. Tension wood has a low MFA, meaning that the microfibril |
https://en.wikipedia.org/wiki/KJIB-LP | KJIB-LP, VHF analog channel 6, was a low-powered television station licensed to Houston, Texas, United States. The station was owned by Roy Henderson. The station has minimal video modulation, with an offset of its audio modulation to 87.89 MHz. This allows individuals to listen to the TV channel at the lower end of the FM radio dial.
History
In 2013, New Beginnings Fellowship Church applied for a license to operate an LPFM radio station on 106.1 in Houston, Texas. This application thwarted the plans of broadcaster Don Werlinger, who at the time was leasing a translator on 106.7 in Simonton, Texas. He wanted to move his translator into Houston on 106.1. As a solution, Werlinger promised that if the LPFM application was withdrawn, he would get the church permission to build and operate two analog LPTV stations. In 2008, facilities for KJIB-LP and KVDO-LP (channel 25) were destroyed by Hurricane Ike, but the licenses remained valid. Werlinger represented to church officials that the license for channel 5 could easily be modified to Channel 6, and operate as a Franken FM station.
Ben Perez, an attorney claiming to represent licensee Roy Henderson, granted church officials permission to build and operate the LPTV stations at their own cost. In 2014, channel 5
(along with KVDO-LP) resumed operations programming classic music videos.
Subsequently, Abundant Life Christian Center in LaMarque, Texas, sought to purchase the license. Roy Henderson claimed that Ben Perez was no l |
https://en.wikipedia.org/wiki/Co-amilofruse | Co-amilofruse (BAN) is a nonproprietary name used to denote a combination of amiloride and furosemide, which are both diuretics. Co-amilofruse is a treatment for fluid retention (oedema), either in the legs (peripheral edema) or on the lungs (pulmonary oedema). Furosemide is a loop diuretic and is more effective than amiloride, but has a tendency to cause low potassium levels (hypokalaemia); the potassium-sparing effects of amiloride may balance this.
Formulation
Two strengths of co-amilofruse are available:
2.5 mg amiloride with 20 mg furosemide, BAN of Co-amilofruse 2.5/20 (brand name Frumil LS)
5 mg amiloride with 40 mg furosemide, BAN of Co-amilofruse 5/4-0 (brand name Frumil)
References
British National Formulary 2004
Loop diuretics
Potassium-sparing diuretics
Combination drugs |
https://en.wikipedia.org/wiki/Load%20line%20%28electronics%29 | In graphical analysis of nonlinear electronic circuits, a load line is a line drawn on the current–voltage characteristic graph for a nonlinear device like a diode or transistor. It represents the constraint put on the voltage and current in the nonlinear device by the external circuit. The load line, usually a straight line, represents the response of the linear part of the circuit, connected to the nonlinear device in question. The points where the characteristic curve and the load line intersect are the possible operating point(s) (Q points) of the circuit; at these points the current and voltage parameters of both parts of the circuit match.
The example at right shows how a load line is used to determine the current and voltage in a simple diode circuit. The diode, a nonlinear device, is in series with a linear circuit consisting of a resistor, R and a voltage source, VDD. The characteristic curve (curved line), representing the current I through the diode for any given voltage across the diode VD, is an exponential curve. The load line (diagonal line), representing the relationship between current and voltage due to Kirchhoff's voltage law applied to the resistor and voltage source, is
Since the same current flows through each of the three elements in series, and the voltage produced by the voltage source and resistor is the voltage across the terminals of the diode, the operating point of the circuit will be at the intersection of the curve with the load line.
In a c |
https://en.wikipedia.org/wiki/Aminoacetone | Aminoacetone is the simplest monopeptide with the formula CH3C(O)CH2NH2. Although stable in the gaseous form, once condensed it reacts with itself. The protonated derivative forms stable salts, e.g. aminoacetone hydrochloride ([CH3C(O)CH2NH3]Cl)). The semicarbazone of the hydrochloride is another bench-stable precursor. Aminoacetone is a metabolite that is implicated in the biosynthesis of methylglyoxal.
See also
Propanolamines
Aminoaldehydes and aminoketones
References
Amines
Ketones |
https://en.wikipedia.org/wiki/Docosanoid | In biochemistry, docosanoids are signaling molecules made by the metabolism of twenty-two-carbon fatty acids (EFAs), especially the omega-3 fatty acid, Docosahexaenoic acid (DHA) (i.e. 4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoic acid) by lipoxygenase, cyclooxygenase, and cytochrome P450 enzymes. Other docosanoids are metabolites of n-3 docosapentaenoic acid (i.e. 7Z,10Z,13Z,16Z,19Z-docosahexaenoic acid), n-6 DHA (i.e. 4Z,7Z,10Z,13Z,16Z-docosahexaenoic acid, and docosatetraenoic acid (i.e. 7Z,10Z,13Z,16Z-docosatetraenoic acid, DTA, or adrenic acid). Prominent docosanoid metabolites of DHA and n-3 DHA are members of the specialized proresolving mediator class of polyunsaturated fatty acid metabolites that possess potent anti-inflammation, tissue healing, and other activities (see specialized proresolving mediators).
Prominent docosanoids
Specialized proresolving mediator docosanoids
Potently bioactive agents of the specialized proresolving mediator class include:
DHA-derived Resolvins (Rv's) of the D series: RvD1, RvD2, RvD3, RvD4, RvD5, RvD6, AT-RvD1, AT-RvD2, AT-RvD3, AT-RvD4, AT-RvD5, and AT-RvD6 (see specialized proresolving mediators#DHA-derived Resolvins).
n-3 DPA-derived Rvs of the D series (RvD1n-3, RvD2n-3, and RvDD1n-3) and the T series (RvT1, TvT2, RvT3, and RvT4) (see specialized proresolving mediators#n-3 DPA-derived resolvins).
DHA-derived Neuroprotectins, also termed protectins: PD1, PDX, 17-epi PD1, and 10-epi-DHA1 (see specialized proresolving mediators#DHA-derived |
https://en.wikipedia.org/wiki/ERB1 | Erb1 also known as the eukaryotic ribosome biogenesis protein 1 is a yeast protein required for maturation of the 25S and 5.8S ribosomal RNAs. It is a component of 66S pre-ribosomal particles and is homologous to the human protein BOP1.
References
External links
Proteins |
https://en.wikipedia.org/wiki/Silver%20zinc%20battery | A silver zinc battery is a secondary cell that utilizes silver(I,III) oxide and zinc.
Overview
Silver zinc cells share most of the characteristics of the silver-oxide battery, and in addition, is able to deliver one of the highest specific energies of all presently known electrochemical power sources. Long used in specialized applications, it is now being developed for more mainstream markets, for example, batteries in laptops and hearing aids.
Silver–zinc batteries, in particular, are being developed to power flexible electronic applications, where the reactants are integrated directly into flexible substrates, such as polymers or paper, using printing or chemical deposition methods.
Experimental new silver–zinc technology (different to silver-oxide) may provide up to 40% more run time than lithium-ion batteries and also features a water-based chemistry that is free from the thermal runaway and flammability problems that have plagued the lithium-ion alternatives.
Chemistry
The silver–zinc battery is manufactured in a fully discharged condition and has the opposite electrode composition, the cathode being of metallic silver, while the anode is a mixture of zinc oxide and pure zinc powders. The electrolyte used is a potassium hydroxide solution in water.
During the charging process, silver is first oxidized to silver(I) oxide
2 Ag(s) + 2 OH− → Ag2O + H2O + 2 e−
and then to silver(II) oxide
Ag2O + 2 OH− → 2 AgO + H2O + 2 e−,
while the zinc oxide is reduced to metallic |
https://en.wikipedia.org/wiki/Poikilohydry | Poikilohydry is the lack of ability (structural or functional mechanism) to maintain and/or regulate water content to achieve homeostasis of cells and tissue connected with quick equilibration of cell/tissue water content to that of the environment. The term is derived from Ancient Greek ποικίλος (poikílos, “spotted or variegate”).
Tolerance to desiccation has been utilized in the Archaea, Bacteria, and Eukaryote kingdoms to take advantage of ecological niches. The tolerance to desiccation is often combined with other abiotic stress factors such as temperature extremes, malnutrition, vitamin imbalances, salinity content, and ultraviolet radiation. Many plants control desiccation tolerance through non-specialized structures such as vegetative tissues or specialized structures such as spores, seeds, and tubers. Desiccation tolerance is distributed among Bryophytes that have no cuticle or stomata, nine Pteridophyte families and ten Angiosperm families, vascular plants that do have a cuticle and stomata.
Selaginella lepidophylla is a vascular lycophyte native to the Chihuahuan Desert in New Mexico, Texas and Mexico. It occurs in north-facing rock crevices and in open habitats. The notable leaf curling attributed to S. lepidophylla, tested by Lebkeucher and Eickmeier in 1991, occurs to prevent photoinhibition in the microphylls in response to UV radiation and gradual leaf uncurling when rehydrated, protects the plant from the same photoinhibition until photon fluxes are fully |
https://en.wikipedia.org/wiki/Apelin%20receptor | The Apelin Receptor (APLNR, also known as APJ) is a G protein-coupled receptor. APLNR possesses two endogenous ligands which are APELIN and ELABELA. The structure of APLNR was resolved in 2017
References
Further reading
External links |
https://en.wikipedia.org/wiki/Tunicamycin | Tunicamycin is a mixture of homologous nucleoside antibiotics that inhibits the UDP-HexNAc: polyprenol-P HexNAc-1-P family of enzymes. In eukaryotes, this includes the enzyme GlcNAc phosphotransferase (GPT), which catalyzes the transfer of N-acetylglucosamine-1-phosphate from UDP-N-acetylglucosamine to dolichol phosphate in the first step of glycoprotein synthesis. Tunicamycin blocks N-linked glycosylation (N-glycans) and treatment of cultured human cells with tunicamycin causes cell cycle arrest in G1 phase. It is used as an experimental tool in biology, e.g. to induce unfolded protein response. Tunicamycin is produced by several bacteria, including Streptomyces clavuligerus and Streptomyces lysosuperificus.
Tunicamycin homologues have varying molecular weights owing to the variability in fatty acid side chain conjugates.
Biosynthesis
The biosynthesis of tunicamycins was studied in Streptomyces chartreusis and a proposed biosynthetic pathway was characterized. The bacteria utilize the enzymes in the tun gene cluster (TunA-N) to make tunicamycins.
TunA uses the starter unit uridine diphosphate-N-acetyl-glucosamine (UDP-GlcNAc) and catalyzes the dehydration of the 6’ hydroxyl group. First, a Tyr residue in TunA abstracts a proton from the 4’ hydroxyl group, forming a ketone at that position. A hydride is subsequently abstracted from the 4’ carbon by NAD+, forming NADH. The ketone is stabilized by hydrogen bonding from the Tyr residue, and a nearby Thr residue. A glut |
https://en.wikipedia.org/wiki/Uridine%20diphosphate%20N-acetylglucosamine | Uridine diphosphate N-acetylglucosamine or UDP-GlcNAc is a nucleotide sugar and a coenzyme in metabolism. It is used by glycosyltransferases to transfer N-acetylglucosamine residues to substrates. D-Glucosamine is made naturally in the form of glucosamine-6-phosphate, and is the biochemical precursor of all nitrogen-containing sugars. To be specific, glucosamine-6-phosphate is synthesized from fructose 6-phosphate and glutamine as the first step of the hexosamine biosynthesis pathway. The end-product of this pathway is UDP-GlcNAc, which is then used for making glycosaminoglycans, proteoglycans, and glycolipids.
UDP-GlcNAc is extensively involved in intracellular signaling as a substrate for O-linked N-acetylglucosamine transferases (OGTs) to install the O-GlcNAc post-translational modification in a wide range of species. It is also involved in nuclear pore formation and nuclear signalling. OGTs and OG-ases play an important role in the structure of the cytoskeleton. In mammals, there is enrichment of OGT transcripts in the pancreas beta-cells, and UDP-GlcNAc is thought to be part of the glucose sensing mechanism. There is also evidence that it plays a part in insulin sensitivity in other cells. In plants, it is involved in the control of gibberellin production.
Clostridium novyi type A alpha-toxin is an O-linked N-actetylglucosamine transferase acting on Rho proteins and causing the collapse of the cytoskeleton.
References
Metabolism
Coenzymes |
https://en.wikipedia.org/wiki/Japanese%20theorem%20for%20cyclic%20quadrilaterals | In geometry, the Japanese theorem states that the centers of the incircles of certain triangles inside a cyclic quadrilateral are vertices of a rectangle.
Triangulating an arbitrary cyclic quadrilateral by its diagonals yields four overlapping triangles (each diagonal creates two triangles). The centers of the incircles of those triangles form a rectangle.
Specifically, let be an arbitrary cyclic quadrilateral and let , , , be the incenters of the triangles , , , . Then the quadrilateral formed by , , , is a rectangle.
Note that this theorem is easily extended to prove the Japanese theorem for cyclic polygons. To prove the quadrilateral case, simply construct the parallelogram tangent to the corners of the constructed rectangle, with sides parallel to the diagonals of the quadrilateral. The construction shows that the parallelogram is a rhombus, which is equivalent to showing that the sums of the radii of the incircles tangent to each diagonal are equal.
The quadrilateral case immediately proves the general case by induction on the set of triangulating partitions of a general polygon.
See also
Carnot's theorem
Sangaku
Japanese mathematics
References
Mangho Ahuja, Wataru Uegaki, Kayo Matsushita: In Search of the Japanese Theorem (postscript file)
Theorem at Cut-the-Knot
Wataru Uegaki: "" (On the Origin and History of the Japanese Theorem). Departmental Bulletin Paper, Mie University Scholarly E-Collections, 2001-03-01
Wilfred Reyes: An Application of Thebault’s Theor |
https://en.wikipedia.org/wiki/Japanese%20theorem | The term Japanese theorem refers to either of the following two geometrical theorems:
Japanese theorem for cyclic polygons
Japanese theorem for cyclic quadrilaterals |
https://en.wikipedia.org/wiki/Albumen%20%28disambiguation%29 | Albumen is the white of an egg. It contains albumin proteins. It is the scientific name for the white of a cooked egg.
Albumin is a class of several hundred proteins.
Albumen or albumin may also refer to:
Serum albumin, a protein, encoded by the ALB gene in humans
Operation Albumen, a series of sabotages against airfields on occupied Crete in 1942
Albumen (album), by the Egg
See also
Human serum albumin, the human variant
Bovine serum albumin, the cow variant
Endosperm, tissue produced in the seeds of most flowering plants
Albumen print, method of producing a print on a paper base from a negative using egg white |
https://en.wikipedia.org/wiki/CLP%20Regulation | The CLP Regulation (for "Classification, Labelling and Packaging") is a European Union regulation from 2008, which aligns the European Union system of classification, labelling and packaging of chemical substances and mixtures to the Globally Harmonised System (GHS). It is expected to facilitate global trade and the harmonised communication of hazard information of chemicals and to promote regulatory efficiency. It complements the 2006 Registration, Evaluation, Authorisation and Restriction of Chemicals (REACH) Regulation (EC No 1907/2006) and replaces an older system contained in the Dangerous Substances Directive (67/548/EEC) and the Dangerous Preparations Directive (1999/45/EC).
Content
The European Union's 2008 Classification, Labelling and Packaging Regulation incorporates the classification criteria and labelling rules agreed at the UN level, the so-called Globally Harmonised System of Classification and Labelling of Chemicals (GHS). It introduced new classification criteria, european hazard symbols (pictograms) and Risk and Safety Statements for labelling, while taking into account elements which were part of the prior EU legislation.
The regulation requires companies to appropriately classify, label and package their substances and mixtures before placing them on the market. It aims to protect workers, consumers and the environment by labelling that reflects a particular chemical's possible hazards. It also addresses the notification of classifications, the establis |
https://en.wikipedia.org/wiki/Kravany%2C%20Trebi%C5%A1ov%20District | Kravany () is a village and municipality in the Trebišov District in the Košice Region of eastern Slovakia.
External links
https://web.archive.org/web/20100202015957/http://www.statistics.sk/mosmis/eng/run.html
Villages and municipalities in Trebišov District
Zemplín (region) |
https://en.wikipedia.org/wiki/DS80C390 | The DS80C390 is a microcontroller, introduced by Dallas Semiconductor (now part of Maxim Integrated Products), whose architecture is derived from that of the Intel 8051 processor series. It contains a code memory address space of twenty-two bits. It also contains two Controller Area Network (CAN) controllers and a 32-bit integer coprocessor. The open-source Small Device C Compiler (SDCC) supports the processor. It was used in the initial version of the Tiny Internet Interface (TINI) processor module where it was superseded by the DS80C400, a processor that also incorporates an Ethernet port.
References
Home page of the SDCC compiler on SourceForge
Summary page on the Maxim website
Microcontrollers |
https://en.wikipedia.org/wiki/Studentized%20range | In statistics, the studentized range, denoted q, is the difference between the largest and smallest data in a sample normalized by the sample standard deviation.
It is named after William Sealy Gosset (who wrote under the pseudonym "Student"), and was introduced by him in 1927.
The concept was later discussed by Newman (1939), Keuls (1952), and John Tukey in some unpublished notes.
Its statistical distribution is the studentized range distribution, which is used for multiple comparison procedures, such as the single step procedure Tukey's range test, the Newman–Keuls method, and the Duncan's step down procedure, and establishing confidence intervals that are still valid after data snooping has occurred.
Description
The value of the studentized range, most often represented by the variable q, can be defined based on a random sample x1, ..., xn from the N(0, 1) distribution of numbers, and another random variable s that is independent of all the xi, and νs2 has a χ2 distribution with ν degrees of freedom. Then
has the Studentized range distribution for n groups and ν degrees of freedom. In applications, the xi are typically the means of samples each of size m, s2 is the pooled variance, and the degrees of freedom are ν = n(m − 1).
The critical value of q is based on three factors:
α (the probability of rejecting a true null hypothesis)
n (the number of observations or groups)
ν (the degrees of freedom used to estimate the sample variance)
Distribution
If X1, ..., Xn |
https://en.wikipedia.org/wiki/Athabasca%20Sand%20Dunes%20Provincial%20Park | The Athabasca Sand Dunes Provincial Park was created to protect the Athabasca sand dunes, a unique boreal shield ecosystem located in the far-north Northern Saskatchewan Administration District. The Athabasca sand dunes are the most northerly active sand dune formations on Earth.
It first came to attention that it should be a protected area in 1969, finally becoming the Athabasca Sand Dunes Provincial Wilderness Park on August 24, 1992.
The park extends for along the southern edge of Lake Athabasca and lies within the Athabasca Basin of the Canadian Shield. The sand dunes are 400 to 1,500 metres long, and their maximum height is approximately 30 metres. The park is accessible by float plane or boat only.
The William River flows through the western section of the park ending in a large river delta. The McFarlane River flows through the far eastern section of the park. The park goes around the Fond du Lac 231 Indian reserve located on the McFarlane River. The First Nations village of Fond du Lac is about by air from the park's eastern boundary.
Geology
The Athabasca Sand Dunes are estimated to be approximately 8,000 years old, formed near the end of the last glacial period. As glaciers receded, meltwater washed enormous quantities of sand, silt and sediment from local sandstone into Lake Athabasca, whose water level was at the time much higher than currently. As the lake level declined to its modern depth, the large sand deposits were revealed. The sand dunes are quite u |
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