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https://en.wikipedia.org/wiki/Siegfried%20K.%20Wiedmann | Siegfried K. Wiedmann (born in 1938) is a German electrical engineer noted for his contributions to semiconductor technologies for integrated circuits.
Wiedmann was born in Plochingen, Germany. He received the Diplom-Ingenieur (1963) and Doctor-Ingenieur (1967) degrees in electrical engineering from the University of Applied Sciences Stuttgart, then worked at the IBM Laboratories in Böblingen, Germany and in the United States, ultimately becoming an IBM Fellow. Together with Horst H. Berger, Wiedmann received the 1977 IEEE Morris N. Liebmann Memorial Award "for the invention and exploration of the Merged Transistor Logic, MTL".
Selected works
H. H. Berger and S. K. Wiedmann, "Merged-Transistor Logic (MTL) - A Low-Cost Bipolar Logic Concept", IEEE Journal of Solid-State Circuits, vol. SC-7, No. 5, Oct. 1972, pp. 340–346.
References
High-Speed Split-Emitter 12L/MTL Memory Cell
1938 births
Living people
People from Esslingen (district)
German electrical engineers
IBM Fellows
Engineers from Baden-Württemberg
Academic staff of the Technical University of Berlin |
https://en.wikipedia.org/wiki/Biogenesis%20of%20lysosome-related%20organelles%20complex%201 | BLOC-1 or biogenesis of lysosome-related organelles complex 1 is a ubiquitously expressed multisubunit protein complex in a group of complexes that also includes BLOC-2 and BLOC-3. BLOC-1 is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules. These organelles are called LROs (lysosome-related organelles) which are apparent in specific cell-types, such as melanocytes. The importance of BLOC-1 in membrane trafficking appears to extend beyond such LROs, as it has demonstrated roles in normal protein-sorting, normal membrane biogenesis, as well as vesicular trafficking. Thus, BLOC-1 is multi-purposed, with adaptable function depending on both organism and cell-type.
Mutations in all BLOC complexes lead to diseased states characterized by Hermansky-Pudlak Syndrome (HPS), a pigmentation disorder subdivided into multiple types depending on the mutation, highlighting the role of BLOC-1 in proper LRO-function. BLOC-1 mutations also are thought to be linked to schizophrenia, and BLOC-1 dysfunction in the brain has important ramifications in neurotransmission. Much effort has been given to uncovering the molecular mechanisms of BLOC-1 function to understand its role in these diseases.
Ultracentrifugation coupled with electron microscopy demonstrated that BLOC-1 has 8 subunits (pallidin, cappuccino, dysbindin, Snapin, Muted, BLOS1, BLOS2, and BLOS3) that are linked linearly to form a complex of rou |
https://en.wikipedia.org/wiki/Goldbach%E2%80%93Euler%20theorem | In mathematics, the Goldbach–Euler theorem (also known as Goldbach's theorem), states that the sum of 1/(p − 1) over the set of perfect powers p, excluding 1 and omitting repetitions, converges to 1:
This result was first published in Euler's 1737 paper "Variæ observationes circa series infinitas". Euler attributed the result to a letter (now lost) from Goldbach.
Proof
Goldbach's original proof to Euler involved assigning a constant to the harmonic series:
, which is divergent. Such a proof is not considered rigorous by modern standards. There is a strong resemblance between the method of sieving out powers employed in his proof and the method of factorization used to derive Euler's product formula for the Riemann zeta function.
Let x be given by
Since the sum of the reciprocal of every power of two is , subtracting the terms with powers of two from x gives
Repeat the process with the terms with the powers of three:
Absent from the above sum are now all terms with powers of two and three. Continue by removing terms with powers of 5, 6 and so on until the right side is exhausted to the value of 1. Eventually, we obtain the equation
which we rearrange into
where the denominators consist of all positive integers that are the non-powers minus one. By subtracting the previous equation from the definition of x given above, we obtain
where the denominators now consist only of perfect powers minus one.
While lacking mathematical rigor, Goldbach's proof provides a reasonab |
https://en.wikipedia.org/wiki/2-deoxyglucosidase | The enzyme 2-deoxyglucosidase () catalyzes the following chemical reaction
a 2-deoxy-α-D-glucoside + H2O 2-deoxy-D-glucose + an alcohol
It belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name is 2-deoxy-α-D-glucoside deoxyglucohydrolase. Other names in common use include 2-deoxy-α-glucosidase, and 2-deoxy-α-D-glucosidase.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-deoxyoctulosonase | In enzymology, a 3-deoxyoctulosonase () is an enzyme that catalyzes the chemical reaction
3-deoxyoctulosonyl-lipopolysaccharide + H2O 3-deoxyoctulosonic acid + lipopolysaccharide
Thus, the two substrates of this enzyme are 3-deoxyoctulosonyl-lipopolysaccharide and H2O, whereas its two products are 3-deoxyoctulosonic acid and lipopolysaccharide.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is 3-deoxyoctulosonyl-lipopolysaccharide hydrolase. This enzyme is also called alpha-Kdo-ase.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/6-phospho-%CE%B2-galactosidase | The enzyme 6-phospho-β-galactosidase () catalyzes the following reaction:
a 6-phospho-β-D-galactoside + H2O 6-phospho-D-galactose + an alcohol
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name is 6-phospho-β-D-galactoside 6-phosphogalactohydrolase. Other names in common use include phospho-β-galactosidase, β-D-phosphogalactoside galactohydrolase, phospho-β-D-galactosidase, and 6-phospho-β-D-galactosidase. This enzyme participates in galactose metabolism.
Structural studies
, four structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 3.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/6-Phospho-%CE%B2-glucosidase | The enzyme 6-phospho-β-glucosidase () catalyzes the following reaction:
6-phospho-β-D-glucosyl-(1,4)-D-glucose + H2O D-glucose + D-glucose 6-phosphate
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is 6-phospho-β-D-glucosyl-(1,4)-D-glucose glucohydrolase. Other names in common use include phospho-β-glucosidase A, phospho-β-glucosidase, and phosphocellobiase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 3.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Adenosine%20nucleosidase | In enzymology, an adenosine nucleosidase () is an enzyme that catalyzes the chemical reaction
adenosine + H2O D-ribose + adenine
Thus, the two substrates of this enzyme are adenosine and H2O, whereas its two products are D-ribose and adenine.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is adenosine ribohydrolase. Other names in common use include adenosinase, N-ribosyladenine ribohydrolase, adenosine hydrolase, and ANase. This enzyme participates in purine metabolism.
References
EC 3.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Adenosylhomocysteine%20nucleosidase | In enzymology, an adenosylhomocysteine nucleosidase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-homocysteine + H2O S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
Thus, the two substrates of this enzyme are S-adenosyl-L-homocysteine and H2O, whereas its two products are S-(5-deoxy-D-ribos-5-yl)-L-homocysteine and adenine.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is S-adenosyl-L-homocysteine homocysteinylribohydrolase. Other names in common use include S-adenosylhomocysteine hydrolase (ambiguous), S-adenosylhomocysteine nucleosidase, 5'-methyladenosine nucleosidase, S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase, and AdoHcy/MTA nucleosidase. This enzyme participates in methionine metabolism.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
References
EC 3.2.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/ADP-ribosyl-%28dinitrogen%20reductase%29%20hydrolase | In enzymology, an ADP-ribosyl-[dinitrogen reductase] hydrolase () is an enzyme that catalyzes the chemical reaction
ADP-D-ribosyl-[dinitrogen reductase] ADP-D-ribose + [dinitrogen reductase]
Hence, this enzyme has one substrate, [[ADP-D-ribosyl-[dinitrogen reductase]]], and two products, ADP-D-ribose and dinitrogen reductase.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is ADP-D-ribosyl-[dinitrogen reductase] ADP-ribosylhydrolase. Other names in common use include azoferredoxin glycosidase, azoferredoxin-activating enzymes, dinitrogenase reductase-activating glycohydrolase, and ADP-ribosyl glycohydrolase.
See also
ADP-ribosylhydrolase
References
EC 3.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%CE%91%2C%CE%B1-phosphotrehalase | The enzyme α,α-phosphotrehalase () catalyzes the following chemical reaction:
α,α-trehalose 6-phosphate + H2O D-glucose + D-glucose 6-phosphate
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is α,α-trehalose-6-phosphate phosphoglucohydrolase. This enzyme is also called phosphotrehalase. This enzyme participates in starch and sucrose metabolism.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%CE%91%2C%CE%B1-Trehalase | An α,α-trehalase () is an enzyme with systematic name α,α-trehalose glucohydrolase. This enzyme catalyzes the chemical reaction
α,α-trehalose + H2O 2 D-glucose
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. It is also called trehalase, and it participates in starch and sucrose metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Alpha-glucuronidase | For beta-glucuronidase, see Beta-glucuronidase
In enzymology, an alpha-glucuronidase () is an enzyme that catalyzes the chemical reaction
an alpha-D-glucuronoside + H2O an alcohol + D-glucuronate
Thus, the two substrates of this enzyme are alpha-D-glucuronoside and H2O, whereas its two products are alcohol and D-glucuronate.
This enzyme belongs to the family of hydrolases, to be specific those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is alpha-D-glucosiduronate glucuronohydrolase. This enzyme is also called alpha-glucosiduronase.
Structural studies
As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , and .
See also
Beta-glucuronidase
Glucuronosyl-disulfoglucosamine glucuronidase
Glycyrrhizinate beta-glucuronidase
References
Visser, J., Kusters van Someren, M.A., Beldman, G. and Voragen, A.G.J. (Eds.), Xylans and Xylanases, Elsevier, Amsterdam, 1992, p. 213-224.
EC 3.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/%CE%91-L-fucosidase | {{DISPLAYTITLE:α-L-fucosidase}}
The enzyme α-L-fucosidase () catalyzes the following chemical reaction: an α-L-fucoside + H2O L-fucose + an alcohol
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is α-L-fucoside fucohydrolase. This enzyme is also called α-fucosidase. It participates in N-glycan degradation and glycan structure degradation.
Deficiency of this enzyme is called Fucosidosis.
In CAZy, α-L-fucosidases are found in glycoside hydrolase family 29 and glycoside hydrolase family 95.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
Human medical studies
It was in a recent study by Endreffy, Bjørklund and collaborators (2017) found an association between the activity of α-L-fucosidase-1 (FUCA-1) and chronic autoimmune disorders in children. This should encourage further research on FUCA-1 as a marker of chronic inflammation and autoimmunity.
See also
1,2-α-L-fucosidase
1,3-α-L-fucosidase
1,6-α-L-fucosidase
FUCA2
References
Further reading
External links
CAZy family GH29
CAZy family GH95
Protein families
EC 3.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/AMP%20nucleosidase | In enzymology, an AMP nucleosidase () is an enzyme that catalyzes the chemical reaction
AMP + H2O D-ribose 5-phosphate + adenine
Thus, the two substrates of this enzyme are AMP and H2O, whereas its two products are D-ribose 5-phosphate and adenine.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is AMP phosphoribohydrolase. Other names in common use include adenylate nucleosidase, and adenosine monophosphate nucleosidase. This enzyme participates in purine metabolism.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 3.2.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Amygdalin%20beta-glucosidase | The enzyme amygdalin β-glucosidase () catalyzes the following chemical reaction:
(R)-amygdalin + H2O (R)-prunasin + D-glucose
Thus, the two substrates of this enzyme are (R)-amygdalin and H2O, whereas its two products are (R)-prunasin and D-glucose.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is amygdalin beta-D-glucohydrolase. Other names in common use include amygdalase, amygdalinase, amygdalin hydrolase, and amygdalin glucosidase.
It can be completely inhibited by the action of Glucono-δ-lactone at 1 mM concentration.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-apiosyl-beta-glucosidase | In enzymology, a beta-apiosyl-beta-glucosidase () is an enzyme that catalyzes the chemical reaction
7-[beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranosyloxy]isoflavonoid + H2O a 7-hydroxyisoflavonoid + beta-D-apiofuranosyl-(1->6)-D-glucose
The 3 substrates of this enzyme are [[7-[beta-D-apiofuranosyl-(1->6)-beta-D-]], [[glucopyranosyloxy]isoflavonoid]], and H2O, whereas its two products are 7-hydroxyisoflavonoid and [[beta-D-apiofuranosyl-(1->6)-D-glucose]].
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is 7-[beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranosyloxy]isoflavonoid beta-D-apiofuranosyl-(1->6)-D-glucohydrolase. Other names in common use include isoflavonoid-7-O-beta[D-apiosyl-(1->6)-beta-D-glucoside], disaccharidase, isoflavonoid 7-O-beta-apiosyl-glucoside beta-glucosidase, and furcatin hydrolase.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-aspartyl-N-acetylglucosaminidase | In enzymology, a beta-aspartyl-N-acetylglucosaminidase () is an enzyme that catalyzes the chemical reaction
1-beta-aspartyl-N-acetyl-D-glucosaminylamine + H2O L-asparagine + N-acetyl-D-glucosamine
Thus, the two substrates of this enzyme are 1-beta-aspartyl-N-acetyl-D-glucosaminylamine and H2O, whereas its two products are L-asparagine and N-acetyl-D-glucosamine.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is 1-beta-aspartyl-N-acetyl-D-glucosaminylamine L-asparaginohydrolase. This enzyme is also called beta-aspartylacetylglucosaminidase.
References
EC 3.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Non-reducing%20end%20%CE%B2-L-arabinopyranosidadase | {{DISPLAYTITLE:Non-reducing end β-L-arabinopyranosidadase}}
The enzyme β-L-arabinosidase () catalyzes the following chemical reaction
a β-L-arabinoside + H2O L-arabinose + an alcohol
It belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name is β-L-arabinoside arabinohydrolase. It is also called vicianosidase.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-primeverosidase | In enzymology, a beta-primeverosidase () is an enzyme that catalyzes the chemical reaction
a 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranoside + H2O 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranose + an alcohol
Thus, the two substrates of this enzyme are 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranoside and H2O, whereas its two products are 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranose and alcohol.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranoside 6-O-(beta-D-xylosyl)-beta-D-glucohydrolase.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Coniferin%20beta-glucosidase | The enzyme coniferin β-glucosidase () catalyzes the following chemical reaction:
coniferin + H2O D-glucose + coniferol
It belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name is coniferin β-D-glucosidase. It is also called coniferin-hydrolyzing β-glucosidase. It participates in phenylpropanoid biosynthesis.
References
EC 3.2.1
Enzymes of unknown structure
Phenylpropanoids metabolism |
https://en.wikipedia.org/wiki/Cyclomaltodextrinase | The enzyme cyclomaltodextrinase () catalyzes the chemical reaction
cyclomaltodextrin + H2O linear maltodextrin
It belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is cyclomaltodextrin dextrin-hydrolase (decyclizing). Other names in common use include cycloheptaglucanase, cyclohexaglucanase, and cyclodextrinase. The enzyme participates in starch and sucrose metabolism and acarbose degradation. The cyclomaltodextrinase is capable of degradation of acarbose to glucose and acarviosine-glucose.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
Further reading
EC 3.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Difructose-anhydride%20synthase | In enzymology, a difructose-anhydride synthase () is an enzyme that catalyzes the chemical reaction
bis-D-fructose 2',1:2,1'-dianhydride + H2O inulobiose
Thus, the two substrates of this enzyme are bis-D-fructose 2',1:2,1'-dianhydride and H2O, whereas its product is inulobiose.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is bis-D-fructose 2',1:2,1'-dianhydride fructohydrolase. This enzyme is also called inulobiose hydrolase.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Endoglycosylceramidase | The enzyme endoglycosylceramidase () catalyzes the following chemical reaction:
oligoglycosylglucosylceramide + H2O ceramide + oligoglycosylglucose
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name is oligoglycosylglucosylceramide glycohydrolase. Other names in common use include endoglycoceramidase, EGCase, and glycosyl-N-acetyl-sphingosine 1,1-β-D-glucanohydrolase.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 3.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Galacturan%201%2C4-%CE%B1-galacturonidase | The enzyme galacturan 1,4-α-galacturonidase () catalyzes the following chemical reaction:
(1,4-α-D-galacturonide)n + H2O (1,4-α-D-galacturonide)n-1 + D-galacturonate
It belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name is poly(1,4-α-D-galacturonide) galacturonohydrolase. Other names in common use include exopolygalacturonase, poly(galacturonate) hydrolase, exo-D-galacturonase, exo-D-galacturonanase, and exopoly-D-galacturonase. This enzyme participates in pentose and glucuronate interconversions and starch and sucrose metabolism.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/GDP-glucosidase | The enzyme GDP-glucosidase () catalyzes the chemical reaction
GDP-glucose + H2O D-glucose + GDP
Thus, the two substrates of this enzyme are GDP-glucose and H2O, whereas its two products are D-glucose and GDP.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is GDP-glucose glucohydrolase. Other names in common use include guanosine diphosphoglucosidase, and guanosine diphosphate D-glucose glucohydrolase.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucosylceramidase | In enzymology, a glucosylceramidase () is an enzyme that catalyzes the chemical reaction
D-glucosyl-N-acylsphingosine + H2O D-glucose + N-acylsphingosine
Thus, the two substrates of this enzyme are D-glucosyl-N-acylsphingosine and H2O, whereas its two products are D-glucose and N-acylsphingosine.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is D-glucosyl-N-acylsphingosine glucohydrolase. Other names in common use include:
psychosine hydrolase,
glucosphingosine glucosylhydrolase,
GlcCer-beta-glucosidase,
beta-D-glucocerebrosidase,
glucosylcerebrosidase,
beta-glucosylceramidase,
ceramide glucosidase,
glucocerebrosidase,
glucosylsphingosine beta-glucosidase,
and glucosylsphingosine beta-D-glucosidase.
This enzyme participates in sphingolipid metabolism and degradation of glycan structures.
Human proteins containing this domain
GBA belongs to Glycoside hydrolase family 30, GBA2 belongs to Glycoside hydrolase family 116.
References
Further reading
EC 3.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glucuronosyl-disulfoglucosamine%20glucuronidase | The enzyme glucuronosyl-disulfoglucosamine glucuronidase () catalyzes the following chemical reaction:
3-D-glucuronosyl-N2,6-disulfo-β-D-glucosamine + H2O D-glucuronate + N2,6-disulfo-D-glucosamine
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is 3-D-glucuronsyl-N2,6-disulfo-β-D-glucosamine glucuronohydrolase. Other names in common use include glycuronidase, and 3-D-glucuronsyl-2-N,6-disulfo-β-D-glucosamine glucuronohydrolase.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycosylceramidase | The enzyme glycosylceramidase () catalyzes the following chemical reaction:
glycosyl-N-acylsphingosine + H2O N-acylsphingosine + a sugar
It belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is glycosyl-N-acylsphingosine glycohydrolase. Other names in common use include phlorizin hydrolase, phloretin-glucosidase, glycosyl ceramide glycosylhydrolase, cerebrosidase, phloridzin β-glucosidase, lactase-phlorizin hydrolase, and phloridzin glucosidase.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycyrrhizinate%20beta-glucuronidase | In enzymology, a glycyrrhizinate β-glucuronidase () is an enzyme that catalyzes the chemical reaction
glycyrrhizinate + H2O 1,2-β-D-glucuronosyl-D-glucuronate + glycyrrhetinate
It belongs to the family of hydrolases, to be specific those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name is glycyrrhizinate glucuronosylhydrolase. Other names in common use include glycyrrhizin β-hydrolase, glycyrrhizin hydrolase, and glycyrrhizinic acid hydrolase.
See also
α-Glucuronidase
β-Glucuronidase
Glucuronosyl-disulfoglucosamine glucuronidase
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Inosinate%20nucleosidase | In enzymology, an inosinate nucleosidase () is an enzyme that catalyzes the chemical reaction
5'-inosinate + H2O D-ribose 5-phosphate + hypoxanthine
Thus, the two substrates of this enzyme are 5'-inosinate and H2O, whereas its two products are D-ribose 5-phosphate and hypoxanthine.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is 5'-inosinate phosphoribohydrolase. This enzyme participates in purine metabolism.
References
EC 3.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Inosine%20nucleosidase | In enzymology, an inosine nucleosidase () is an enzyme that catalyzes the chemical reaction
inosine + H2O D-ribose + hypoxanthine
Thus, the two substrates of this enzyme are inosine and H2O, whereas its two products are D-ribose and hypoxanthine.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is inosine ribohydrolase. Other names in common use include inosinase, and inosine-guanosine nucleosidase. This enzyme participates in purine metabolism.
References
EC 3.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Maltose-6%27-phosphate%20glucosidase | The enzyme maltose-6′-phosphate glucosidase () catalyzes the following chemical reaction:
maltose 6′-phosphate + H2O D-glucose + D-glucose 6-phosphate
It belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. It participates in starch and sucrose metabolism.
Nomenclature
The systematic name of this enzyme class is maltose-6′-phosphate 6-phosphoglucohydrolase. This enzyme is also called phospho-α-glucosidase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 3.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Methylthioadenosine%20nucleosidase | In enzymology, a methylthioadenosine nucleosidase () is an enzyme that catalyzes the chemical reaction
S-methyl-5'-thioadenosine + H2O S-methyl-5-thio-D-ribose + adenine
Thus, the two substrates of this enzyme are S-methyl-5'-thioadenosine and H2O, whereas its two products are S-methyl-5-thio-D-ribose and adenine.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is S-methyl-5'-thioadenosine adeninehyrolase. Other names in common use include 5'-methylthioadenosine nucleosidase, MTA nucleosidase, MeSAdo nucleosidase, and methylthioadenosine methylthioribohydrolase. This enzyme participates in urea cycle and metabolism of amino groups and methionine metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 3.2.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Mucinaminylserine%20mucinaminidase | In enzymology, a mucinaminylserine mucinaminidase () is an enzyme that catalyzes the chemical reaction
D-galactosyl-3-(N-acetyl-beta-D-galactosaminyl)-L-serine + H2O D-galactosyl-3-N-acetyl-beta-D-galactosamine + L-serine
Thus, the two substrates of this enzyme are D-galactosyl-3-(N-acetyl-beta-D-galactosaminyl)-L-serine and H2O, whereas its two products are D-galactosyl-3-N-acetyl-beta-D-galactosamine and L-serine.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is D-galactosyl-3-(N-acetyl-beta-D-galactosaminyl)-L-serine mucinaminohydrolase. Other names in common use include endo-alpha-N-acetylgalactosaminidase, and endo-alpha-N-acetyl-D-galactosaminidase.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/NAD%2B%20glycohydrolase | {{DISPLAYTITLE:NAD+ glycohydrolase}}
In enzymology, a NAD+ glycohydrolase () is an enzyme that catalyzes the chemical reaction
NAD+ + H2O ADP-ribose + nicotinamide
Thus, the two substrates of this enzyme are NAD+ and H2O, whereas its two products are ADP-ribose and nicotinamide. Unlike ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase (EC 3.2.2.6), which catalyzes the same reaction, this reaction does not proceed through a cyclic ADP-ribose.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is NAD+ glycohydrolase. Other names in common use include NAD+ nucleosidase, NADase, DPNase, DPN hydrolase, NAD hydrolase, diphosphopyridine nucleosidase, nicotinamide adenine dinucleotide nucleosidase, NAD glycohydrolase, NAD nucleosidase, and nicotinamide adenine dinucleotide glycohydrolase. This enzyme participates in nicotinate and nicotinamide metabolism and calcium signaling pathway. Calcium metabolism involves the regulation of the levels of calcium in the body. The role this calcium plays also includes providing enough calcium for bone mineralization. It serves as the basis for the structure and rigidity of bones. Calcium metabolism can lead to a variety of diseases which can involve renal function. High concentrations of calcium can lead to cell death or apoptosis.
References
Putney, J. W. P. (2019). Calcium Metabolism. Access Science. https://www.accessscience.com/ |
https://en.wikipedia.org/wiki/ADP-ribosyl%20cyclase | In enzymology, a ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase () is a bifunctional enzyme that catalyzes the chemical reaction
NAD+ + H2O cADPR + H2O + nicotinamide ADP-ribose + nicotinamide
The 3 substrates of this enzyme are NAD+ and H2O, whereas its two products are ADP-ribose and nicotinamide. The reaction proceeds through cyclic ADP-ribose (cADPR) as intermediate, which is then hydrolyzed into ADP-ribose. This makes it different from NAD+ glycohydrolase (EC 3.2.2.5), where the reaction does not proceed through cADPR.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. Other names of this enzyme in common use include nicotinamide adenine dinucleotide (phosphate) nucleosidase, triphosphopyridine nucleotidase, NAD(P) nucleosidase, NAD(P)ase, and nicotinamide adenine dinucleotide (phosphate) glycohydrolase. This enzyme participates in nicotinate and nicotinamide metabolism.
References
EC 3.2.2
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-methyl%20nucleosidase | In enzymology, a N-methyl nucleosidase () is an enzyme that catalyzes the chemical reaction
7-methylxanthosine + H2O 7-methylxanthine + D-ribose
Thus, the two substrates of this enzyme are 7-methylxanthosine and H2O, whereas its two products are 7-methylxanthine and D-ribose.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is 7-methylxanthosine ribohydrolase. Other names in common use include 7-methylxanthosine nucleosidase, N-MeNase, N-methyl nucleoside hydrolase, and methylpurine nucleosidase.
References
EC 3.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/NMN%20nucleosidase | In enzymology, a NMN nucleosidase () is an enzyme that catalyzes the chemical reaction
nicotinamide D-ribonucleotide + H2O D-ribose 5-phosphate + nicotinamide
Thus, the two substrates of this enzyme are nicotinamide D-ribonucleotide and H2O, whereas its two products are D-ribose 5-phosphate and nicotinamide.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is nicotinamide-nucleotide phosphoribohydrolase. Other names in common use include NMNase, nicotinamide mononucleotide nucleosidase, nicotinamide mononucleotidase, NMN glycohydrolase, and NMNGhase. This enzyme participates in nicotinate and nicotinamide metabolism.
References
EC 3.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Protein-glucosylgalactosylhydroxylysine%20glucosidase | The enzyme protein-glucosylgalactosylhydroxylysine glucosidase () catalyzes the following chemical reaction:
[collagen]-(5R)-5-O-[α-D-glucosyl-(1→2)-β-D-galactosyl]-5-hydroxy-L-lysine + H2O = D-glucose + [collagen]-(5R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysine
It belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name is protein-α-D-glucosyl-1,2-β-D-galactosyl-L-hydroxylysine glucohydrolase. Other names in common use include 2-O-α-D-glucopyranosyl-5-O-α-D-galactopyranosylhydroxy-L-lysine glucohydrolase, and lysine glucohydrolase.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Prunasin%20beta-glucosidase | In enzymology, a prunasin β-glucosidase () is an enzyme that catalyzes the chemical reaction
(R)-prunasin + H2O D-glucose + mandelonitrile
It belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name is prunasin β-D-glucohydrolase. It is also called prunasin hydrolase.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Purine%20nucleosidase | In enzymology, a purine nucleosidase () is an enzyme that catalyzes the chemical reaction
a purine nucleoside + H2O D-ribose + a purine base
Thus, the two substrates of this enzyme are purine nucleoside and H2O, whereas its two products are D-ribose and purine base.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is purine-nucleoside ribohydrolase. Other names in common use include nucleosidase, purine beta-ribosidase, purine nucleoside hydrolase, purine ribonucleosidase, ribonucleoside hydrolase, nucleoside hydrolase, N-ribosyl purine ribohydrolase, nucleosidase g, N-D-ribosylpurine ribohydrolase, inosine-adenosine-guanosine preferring nucleoside hydrolase, purine-specific nucleoside N-ribohydrolase, IAG-nucleoside hydrolase, and IAG-NH. This enzyme participates in purine metabolism and nicotinate and nicotinamide metabolism.
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
References
EC 3.2.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Pyrimidine-5%27-nucleotide%20nucleosidase | In enzymology, a pyrimidine-5'-nucleotide nucleosidase () is an enzyme that catalyzes the chemical reaction
a pyrimidine 5'-nucleotide + H2O D-ribose 5-phosphate + a pyrimidine base
Thus, the two substrates of this enzyme are pyrimidine 5'-nucleotide and H2O, whereas its two products are D-ribose 5-phosphate and pyrimidine base.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is pyrimidine-5'-nucleotide phosphoribo(deoxyribo)hydrolase. Other names in common use include pyrimidine nucleotide N-ribosidase, and Pyr5N. This enzyme participates in pyrimidine metabolism.
References
EC 3.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Quercitrinase | The enzyme quercitrinase () catalyzes the following chemical reaction:
quercitrin + H2O L-rhamnose + quercetin
Thus, the two substrates of this enzyme are quercitrin and H2O, whereas its two products are L-rhamnose and quercetin.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is quercitrin 3-L-rhamnohydrolase.
The enzyme can be found in Aspergillus flavus. It is an enzyme in the rutin catabolic pathway.
References
Further reading
EC 3.2.1
Enzymes of unknown structure
Quercetin glycosides |
https://en.wikipedia.org/wiki/Beta-3%20adrenergic%20receptor | The beta-3 adrenergic receptor (β3-adrenoceptor), also known as ADRB3, is a beta-adrenergic receptor, and also denotes the human gene encoding it.
Function
Actions of the β3 receptor include
Enhancement of lipolysis in adipose tissue.
Thermogenesis in skeletal muscle
It is located mainly in adipose tissue and is involved in the regulation of lipolysis and thermogenesis. Some β3 agonists have demonstrated antistress effects in animal studies, suggesting it also has a role in the central nervous system (CNS). β3 receptors are found in the gallbladder, urinary bladder, and in brown adipose tissue. Their role in gallbladder physiology is unknown, but they are thought to play a role in lipolysis and thermogenesis in brown fat. In the urinary bladder it is thought to cause relaxation of the bladder and prevention of urination.
Mechanism of action
Beta adrenergic receptors are involved in the epinephrine- and norepinephrine-induced activation of adenylate cyclase through the action of the G proteins of the type Gs.
Ligands
Agonists
Amibegron (SR-58611A)
BRL-37344
CL-316,243
L-742,791
L-796,568
LY-368,842
Mirabegron (YM-178), approved for treatment of overactive bladder in Japan, United States, UK, Canada, China and India.
Nebivolol selective beta(1)-blocker and beta(3)-agonist.
Ro40-2148
Solabegron (GW-427,353)
Vibegron (MK-4618)
Antagonists
L-748,328
L-748,337
SR 59230A was thought to be a selective β3 antagonist but later found to also be an antagonist |
https://en.wikipedia.org/wiki/Galactosylgalactosylglucosylceramidase | In enzymology, a galactosylgalactosylglucosylceramidase () is an enzyme that catalyzes the chemical reaction
D-galactosyl-D-galactosyl-D-glucosyl-N-acylsphingosine + H2O D-galactose + lactosyl-N-acylsphingosine
Thus, the two substrates of this enzyme are D-galactosyl-D-galactosyl-D-glucosyl-N-acylsphingosine and H2O, whereas its two products are D-galactose and lactosyl-N-acylsphingosine.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is D-galactosyl-D-galactosyl-D-glucosyl-N-acylsphingosine galactohydrolase. Other names in common use include trihexosyl ceramide galactosidase, ceramide trihexosidase, ceramidetrihexoside alpha-galactosidase, trihexosylceramide alpha-galactosidase, and ceramidetrihexosidase.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Raucaffricine%20beta-glucosidase | The enzyme raucaffricine β-glucosidase () catalyzes the following chemical reaction:
raucaffricine + H2O D-glucose + vomilenine
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is raucaffricine β-D-glucohydrolase. Other names in common use include raucaffricine β-D-glucosidase, and raucaffricine glucosidase. This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ribosylpyrimidine%20nucleosidase | In enzymology, a ribosylpyrimidine nucleosidase () is an enzyme that catalyzes the chemical reaction
a pyrimidine nucleoside + H2O D-ribose + a pyrimidine base
Thus, the two substrates of this enzyme are pyrimidine nucleoside and H2O, whereas its two products are D-ribose and pyrimidine base.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is pyrimidine-nucleoside ribohydrolase. Other names in common use include N-ribosylpyrimidine nucleosidase, pyrimidine nucleosidase, N-ribosylpyrimidine ribohydrolase, pyrimidine nucleoside hydrolase, RihB, YeiK, and nucleoside ribohydrolase. This enzyme participates in purine metabolism and pyrimidine metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.2.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Steryl-beta-glucosidase | The enzyme steryl-β-glucosidase () catalyzes the following chemical reaction:
cholesteryl-β-D-glucoside + H2O D-glucose + cholesterol
It belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name is cholesteryl-β-D-glucoside glucohydrolase.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Uridine%20nucleosidase | In enzymology, an uridine nucleosidase () is an enzyme that catalyzes the chemical reaction
uridine + H2O D-ribose + uracil
Thus, the two substrates of this enzyme are uridine and H2O, whereas its two products are D-ribose and uracil.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is uridine ribohydrolase. This enzyme is also called uridine hydrolase. This enzyme participates in pyrimidine metabolism.
Structural studies
As of late 2007, 23 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , and .
References
EC 3.2.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Vicianin%20beta-glucosidase | The enzyme vicianin β-glucosidase () catalyzes the following chemical reaction:
(R)-vicianin + H2O mandelonitrile + vicianose
It belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name is (R)-vicianin β-D-glucohydrolase. It is also called vicianin hydrolase.
References
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Xyloglucan-specific%20endo-beta-1%2C4-glucanase | In enzymology, a xyloglucan-specific endo-beta-1,4-glucanase () is an enzyme that catalyzes the chemical reaction
xyloglucan + H2O xyloglucan oligosaccharides
Thus, the two substrates of this enzyme are xyloglucan and H2O, whereas its product is xyloglucan oligosaccharides.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is [(1->6)-alpha-D-xylo]-(1->4)-beta-D-glucan glucanohydrolase. Other names in common use include XEG, xyloglucan endo-beta-1,4-glucanase, xyloglucanase, xyloglucanendohydrolase, XH, and 1,4-beta-D-glucan glucanohydrolase.
Family 12 was first identified in plant pathogens by discovery in Phytophthora spp.
Structural studies
As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , and .
References
Further reading
EC 3.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Xyloglucan-specific%20exo-beta-1%2C4-glucanase | In enzymology, a xyloglucan-specific exo-beta-1,4-glucanase () is an enzyme that catalyzes the chemical reaction
xyloglucan + H2O xyloglucan oligosaccharides (exohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan)
Thus, the two substrates of this enzyme are xyloglucan and H2O, and its products are xyloglucan oligosaccharides (exohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan).
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is [(1->6)-alpha-D-xylo]-(1->4)-beta-D-glucan exo-glucohydrolase. This enzyme is also called Cel74A.
References
Further reading
EC 3.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Surface%20diffusion | Surface diffusion is a general process involving the motion of adatoms, molecules, and atomic clusters (adparticles) at solid material surfaces. The process can generally be thought of in terms of particles jumping between adjacent adsorption sites on a surface, as in figure 1. Just as in bulk diffusion, this motion is typically a thermally promoted process with rates increasing with increasing temperature. Many systems display diffusion behavior that deviates from the conventional model of nearest-neighbor jumps. Tunneling diffusion is a particularly interesting example of an unconventional mechanism wherein hydrogen has been shown to diffuse on clean metal surfaces via the quantum tunneling effect.
Various analytical tools may be used to elucidate surface diffusion mechanisms and rates, the most important of which are field ion microscopy and scanning tunneling microscopy. While in principle the process can occur on a variety of materials, most experiments are performed on crystalline metal surfaces. Due to experimental constraints most studies of surface diffusion are limited to well below the melting point of the substrate, and much has yet to be discovered regarding how these processes take place at higher temperatures.
Surface diffusion rates and mechanisms are affected by a variety of factors including the strength of the surface-adparticle bond, orientation of the surface lattice, attraction and repulsion between surface species and chemical potential gradients. It |
https://en.wikipedia.org/wiki/Entosis | Entosis (from Greek ἐντός entos, "within" and -ωσις -osis, "development process") is the invasion of a living cell into another cell's cytoplasm. The process was discovered by Overholtzer et al. as reported in Cell.
Entotic cells, also referred to as cell-in-cell structures, are triggered by loss of attachment to the extracellular matrix (ECM). This internalization of one cell by another is dependent on adherens junctions, and is driven by a Rho-dependent process, involving actin polymerization and myosin II activity in the internalized cell. Adherens junctions bind cells together by linking cadherin transmembrane protein complexes of adjacent cells to the cytoskeleton. When certain cell types are detached from the ECM and have lost adhesion, the compaction force between neighboring cells can cause them to push into their neighbors, forming the trademark cell-in-cell structures. Though cell-in-cell structures commonly refer to the interaction between two neighboring cells, entosis has been observed involving more than two cells. In the case of an entotic structure formed between three cells, the middle cell acts as both an internalizing and an outer host cell simultaneously.
Aneuploidy, a condition in which nondisjunction gives rise to gametes with an abnormal number of chromosomes, is one of the most prevalent phenotypes of human tumors. The underlying cause of aneuploidy remains highly debated; however, entosis is shown to perturb cytokinesis (cytoplasmic division) and tr |
https://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate%20deaminase | In enzymology, a 1-aminocyclopropane-1-carboxylate deaminase () is an enzyme that catalyzes the chemical reaction
1-aminocyclopropane-1-carboxylate + H2O 2-oxobutanoate + NH3
Thus, the two substrates of this enzyme are 1-aminocyclopropane-1-carboxylate and H2O, whereas its two products are 2-oxobutanoate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing). This enzyme is also called 1-aminocyclopropane-1-carboxylate endolyase (deaminating). This enzyme participates in propanoate metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 3.5.99
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/1-pyrroline-4-hydroxy-2-carboxylate%20deaminase | In enzymology, a 1-pyrroline-4-hydroxy-2-carboxylate deaminase () is an enzyme that catalyzes the chemical reaction
1-pyrroline-4-hydroxy-2-carboxylate + H2O 2,5-dioxopentanoate + NH3
Thus, the two substrates of this enzyme are 1-pyrroline-4-hydroxy-2-carboxylate and H2O, whereas its two products are 2,5-dioxopentanoate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 1-pyrroline-4-hydroxy-2-carboxylate aminohydrolase (decyclizing). This enzyme is also called HPC deaminase. This enzyme participates in arginine and proline metabolism.
References
EC 3.5.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2%2C5-dioxopiperazine%20hydrolase | In enzymology, a 2,5-dioxopiperazine hydrolase () is an enzyme that catalyzes the chemical reaction
2,5-dioxopiperazine + H2O glycylglycine
Thus, the two substrates of this enzyme are 2,5-dioxopiperazine and H2O, whereas its product is glycylglycine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is 2,5-dioxopiperazine amidohydrolase. Other names in common use include cyclo(Gly-Gly) hydrolase, and cyclo(glycylglycine) hydrolase.
References
EC 3.5.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-%28acetamidomethylene%29succinate%20hydrolase | In enzymology, a 2-(acetamidomethylene)succinate hydrolase () is an enzyme that catalyzes the chemical reaction
2-(acetamidomethylene)succinate + 2 H2O acetate + succinate semialdehyde + NH3 + CO2
Thus, the two substrates of this enzyme are 2-(acetamidomethylene)succinate and H2O, whereas its 4 products are acetate, succinate semialdehyde, NH3, and CO2.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 2-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating). This enzyme is also called alpha-(N-acetylaminomethylene)succinic acid hydrolase. This enzyme participates in vitamin B6 metabolism.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-Aminomuconate%20deaminase | In enzymology, 2-aminomuconate deaminase () (also known as amnd) is an enzyme that catalyzes the chemical reaction
2-aminomuconate + H2O 4-oxalocrotonate + NH3
Thus, the two substrates of this enzyme are 2-aminomuconate and H2O, whereas its two products are 4-oxalocrotonate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 2-aminomuconate aminohydrolase. This enzyme participates in tryptophan metabolism.
References
EC 3.5.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-%28hydroxymethyl%29-3-%28acetamidomethylene%29succinate%20hydrolase | In enzymology, a 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase () is an enzyme that catalyzes the chemical reaction
2-(hydroxymethyl)-3-(acetamidomethylene)succinate + 2 H2O acetate + 2-(hydroxymethyl)-4-oxobutanoate + NH3 + CO2
Thus, the two substrates of this enzyme are 2-(hydroxymethyl)-3-(acetamidomethylene)succinate and H2O, whereas its 4 products are acetate, 2-(hydroxymethyl)-4-oxobutanoate, NH3, and CO2.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 2-(hydroxymethyl)-3-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating). Other names in common use include compound B hydrolase, alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid, and hydrolase. This enzyme participates in vitamin B6 metabolism.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-acetamidobutyrate%20deacetylase | In enzymology, a 4-acetamidobutyrate deacetylase () is an enzyme that catalyzes the chemical reaction
4-acetamidobutanoate + H2O acetate + 4-aminobutanoate
Thus, the two substrates of this enzyme are 4-acetamidobutanoate and H2O, whereas its two products are acetate and 4-aminobutanoate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 4-acetamidobutanoate amidohydrolase. This enzyme participates in urea cycle and metabolism of amino groups and lysine degradation.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-acetamidobutyryl-CoA%20deacetylase | In enzymology, a 4-acetamidobutyryl-CoA deacetylase () is an enzyme that catalyzes the chemical reaction
4-acetamidobutanoyl-CoA + H2O acetate + 4-aminobutanoyl-CoA
Thus, the two substrates of this enzyme are 4-acetamidobutanoyl-CoA and H2O, whereas its two products are acetate and 4-aminobutanoyl-CoA.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 4-acetamidobutanoyl-CoA amidohydrolase. Other names in common use include aminobutyryl-CoA thiolesterase, and deacetylase-thiolesterase.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-methyleneglutaminase | In enzymology, a 4-methyleneglutaminase () is an enzyme that catalyzes the chemical reaction
4-methylene-L-glutamine + H2O 4-methylene-L-glutamate + NH3
Thus, the two substrates of this enzyme are 4-methylene-L-glutamine and H2O, whereas its two products are 4-methylene-L-glutamate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 4-methylene-L-glutamine amidohydrolase. Other names in common use include 4-methyleneglutamine deamidase, and 4-methyleneglutamine amidohydrolase. This enzyme participates in c5-branched dibasic acid metabolism.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-aminopentanamidase | In enzymology, a 5-aminopentanamidase () is an enzyme that catalyzes the chemical reaction
5-aminopentanamide + H2O 5-aminopentanoate + NH3
Thus, the two substrates of this enzyme are 5-aminopentanamide and H2O, whereas its two products are 5-aminopentanoate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 5-aminopentanamide amidohydrolase. Other names in common use include 5-aminovaleramidase, and 5-aminonorvaleramidase. This enzyme participates in lysine degradation.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-oxoprolinase%20%28ATP-hydrolysing%29 | In enzymology, a 5-oxoprolinase (ATP-hydrolysing) () is an enzyme that catalyzes the chemical reaction
ATP + 5-oxo-L-proline + 2 H2O ADP + phosphate + L-glutamate
The 3 substrates of this enzyme are ATP, 5-oxo-L-proline, and H2O, whereas its 3 products are ADP, phosphate, and L-glutamate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is 5-oxo-L-proline amidohydrolase (ATP-hydrolysing). Other names in common use include pyroglutamase (ATP-hydrolysing), oxoprolinase, pyroglutamase, 5-oxoprolinase, pyroglutamate hydrolase, pyroglutamic hydrolase, L-pyroglutamate hydrolase, 5-oxo-L-prolinase, and pyroglutamase. This enzyme participates in glutathione metabolism.
References
EC 3.5.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/6-aminohexanoate-cyclic-dimer%20hydrolase | In enzymology, a 6-aminohexanoate-cyclic-dimer hydrolase () is an enzyme that catalyzes the chemical reaction
1,8-diazacyclotetradecane-2,9-dione + H2O N-(6-aminohexanoyl)-6-aminohexanoate
Thus, the two substrates of this enzyme are 1,8-diazacyclotetradecane-2,9-dione and H2O, whereas its product is N-(6-aminohexanoyl)-6-aminohexanoate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is 1,8-diazacyclotetradecane-2,9-dione lactamhydrolase.
References
External links
EC 3.5.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/6-aminohexanoate-dimer%20hydrolase | In enzymology, a 6-aminohexanoate-dimer hydrolase () is an enzyme that catalyzes the chemical reaction N-(6-aminohexanoyl)-6-aminohexanoate + H2O 2 6-aminohexanoate. Thus, the two substrates of this enzyme are N-(6-aminohexanoyl)-6-aminohexanoate and H2O, whereas its product is two molecules of 6-aminohexanoate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-(6-aminohexanoyl)-6-aminohexanoate amidohydrolase. This enzyme is also called 6-aminohexanoic acid oligomer hydrolase.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
See also
Nylon-eating bacteria
References
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Acetylornithine%20deacetylase | In enzymology, an acetylornithine deacetylase () is an enzyme that catalyzes the chemical reaction
N2-acetyl-L-ornithine + H2O acetate + L-ornithine
Thus, the two substrates of this enzyme are N2-acetyl-L-ornithine and H2O, whereas its two products are acetate and L-ornithine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N2-acetyl-L-ornithine amidohydrolase. Other names in common use include acetylornithinase, N-acetylornithinase, and 2-N-acetyl-L-ornithine amidohydrolase. This enzyme participates in urea cycle and metabolism of amino groups.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Acetylputrescine%20deacetylase | In enzymology, an acetylputrescine deacetylase () is an enzyme that catalyzes the chemical reaction
N-acetylputrescine + H2O acetate + putrescine
Thus, the two substrates of this enzyme are N-acetylputrescine and H2O, whereas its two products are acetate and putrescine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acetylputrescine acetylhydrolase. This enzyme participates in urea cycle and metabolism of amino groups.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetylspermidine%20deacetylase | In enzymology, an acetylspermidine deacetylase () is an enzyme that catalyzes the chemical reaction
N8-acetylspermidine + H2O acetate + spermidine
Thus, the two substrates of this enzyme are N8-acetylspermidine and H2O, whereas its two products are acetate and spermidine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N8-acetylspermidine amidohydrolase. Other names in common use include N8-monoacetylspermidine deacetylase, N8-acetylspermidine deacetylase, N-acetylspermidine deacetylase, N1-acetylspermidine amidohydrolase (incorrect), and 8-N-acetylspermidine amidohydrolase.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acylagmatine%20amidase | In enzymology, an acylagmatine amidase () is an enzyme that catalyzes the chemical reaction
benzoylagmatine + H2O benzoate + agmatine
Thus, the two substrates of this enzyme are benzoylagmatine and H2O, whereas its two products are benzoate and agmatine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is benzoylagmatine amidohydrolase. Other names in common use include acylagmatine amidohydrolase, and acylagmatine deacylase.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acyl-lysine%20deacylase | In enzymology, an acyl-lysine deacylase () is an enzyme that catalyzes the chemical reaction
N6-acyl-L-lysine + H2O a carboxylate + L-lysine
Thus, the two substrates of this enzyme are N6-acyl-L-lysine and H2O, whereas its two products are carboxylate and L-lysine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N6-acyl-L-lysine amidohydrolase. Other names in common use include epsilon-lysine acylase, and 6-N-acyl-L-lysine amidohydrolase. This enzyme participates in lysine degradation.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Adenine%20deaminase | In enzymology, an adenine deaminase () is an enzyme that catalyzes the chemical reaction
adenine + H2O hypoxanthine + NH3
Thus, the two substrates of this enzyme are adenine and H2O, whereas its two products are hypoxanthine and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is adenine aminohydrolase. Other names in common use include adenase, adenine aminase, and ADase. This enzyme participates in purine 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 3.5.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Adenosine-phosphate%20deaminase | In enzymology, an adenosine-phosphate deaminase () is an enzyme that catalyzes the chemical reaction
5'-AMP + H2O 5'-IMP + NH3
Thus, the two substrates of this enzyme are 5'-AMP and H2O, whereas its two products are 5'-IMP and NH3.
Classification
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is adenosine-phosphate aminohydrolase. Other names in common use include adenylate deaminase, adenine nucleotide deaminase, and adenosine (phosphate) deaminase.
The EC number for adenosine-phosphate deaminase is [EC 3.5.4.17]. The class is (EC 3) for hydrolase. Hydrolases are enzymes that catalyze bond cleavage by reaction with water. The sub-class refers to adenosine-phosphate deaminase acting on carbon-nitrogen bonds, other than peptide bonds. The sub-sub-class refers to the type of substrate the enzyme is binding to, in this case, cyclic amidines. The final number (17) indicates that adenosine-phosphate deaminase binds to 5'-adenosine monophosphate.
Reaction mechanism
The pathway for adenosine-phosphate deaminase involves two substrates, 5'-adenosine monophosphate and water. This pathway is referred to as amidine hydrolysis. Adenosine-phosphate deaminase binds to 5'-AMP using water to break the C-N bond and replacing it with a carbonyl group. Ultimately, this produces 5'-IMP (Inosine monophosphate) and NH3 (ammonia). Substrate specificiti |
https://en.wikipedia.org/wiki/Adenosylcobinamide%20hydrolase | In enzymology, an adenosylcobinamide hydrolase () is an enzyme that catalyzes the chemical reaction
adenosylcobinamide + H2O adenosylcobyric acid + (R)-1-aminopropan-2-ol
Thus, the two substrates of this enzyme are adenosylcobinamide and H2O, whereas its two products are adenosylcobyric acid and (R)-1-aminopropan-2-ol.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is adenosylcobinamide amidohydrolase. Other names in common use include CbiZ, and AdoCbi amidohydrolase. This enzyme participates in porphyrin and chlorophyll metabolism.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/ADP%20deaminase | In enzymology, an ADP deaminase () is an enzyme that catalyzes the chemical reaction
ADP + H2O IDP + NH3
Thus, the two substrates of this enzyme are ADP and H2O, whereas its two products are IDP and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is ADP aminohydrolase. Other names in common use include adenosine diphosphate deaminase, and adenosinepyrophosphate deaminase.
References
EC 3.5.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Agmatinase | In enzymology, an agmatinase () is an enzyme that catalyzes the chemical reaction
agmatine + H2O putrescine + urea
Thus, the two substrates of this enzyme are agmatine and H2O, whereas its two products are putrescine and urea.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is agmatine amidinohydrolase. Other names in common use include agmatine ureohydrolase, and SpeB. This enzyme participates in urea cycle and metabolism of amino groups.
Genetics
In humans, the enzyme is encoded by the AGMAT gene.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
Inhibitors
Piperazine-1-carboxamidine
References
External links
EC 3.5.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Agmatine%20deiminase | In enzymology, an agmatine deiminase () is an enzyme that catalyzes the chemical reaction
agmatine + H2O N-carbamoylputrescine + NH3
Thus, the two substrates of this enzyme are agmatine and H2O, whereas its two products are N-carbamoylputrescine and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is agmatine iminohydrolase. This enzyme is also called agmatine amidinohydrolase. This enzyme participates in urea cycle and metabolism of amino groups.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 3.5.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Aliphatic%20nitrilase | In enzymology, an aliphatic nitrilase also known as aliphatic nitrile aminohydrolase () is an enzyme that catalyzes the hydrolysis of nitriles to carboxylic acids:
R-CN + 2 H2O R-COOH + NH3
Thus, the two substrates of this enzyme are an aliphatic nitrile (R-CN) and H2O, whereas its two products are a carboxylic acid (R-COOH) and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in nitriles. This enzyme participates in styrene degradation.
References
*
EC 3.5.5
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alkylamidase | In enzymology, an alkylamidase () is an enzyme that catalyzes the chemical reaction
N-methylhexanamide + H2O hexanoate + methylamine
Thus, the two substrates of this enzyme are N-methylhexanamide and H2O, whereas its two products are hexanoate and methylamine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-methylhexanamide amidohydrolase.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Allantoate%20deiminase | In enzymology, an allantoate deiminase () is an enzyme that catalyzes the chemical reaction
allantoate + H2O ureidoglycine + NH3 + CO2
Thus, the two substrates of this enzyme are allantoate and H2O, whereas its 3 products are ureidoglycine, NH3, and CO2.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is allantoate amidinohydrolase (decarboxylating). This enzyme is also called allantoate amidohydrolase. This enzyme participates in purine metabolism.
References
EC 3.5.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Allantoicase | Allantoicase is an enzyme () that in humans is encoded by the ALLC gene. Allantoicase catalyzes the chemical reaction
allantoate + H2O (S)-ureidoglycolate + urea
Thus, the two substrates of this enzyme are allantoate and H2O, whereas its two products are (S)-ureidoglycolate and urea.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is allantoate amidinohydrolase. This enzyme participates in purine metabolism by facilitating the utilization of purines as secondary nitrogen sources under nitrogen-limiting conditions. While purine degradation converges to uric acid in all vertebrates, its further degradation varies from species to species. Uric acid is excreted by birds, reptiles, and some mammals that do not have a functional uricase gene, whereas other mammals produce allantoin. Amphibians and microorganisms produce ammonia and carbon dioxide using the uricolytic pathway. Allantoicase performs the second step in this pathway catalyzing the conversion of allantoate into ureidoglycolate and urea.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
The structure of allantoicase is best described as being composed of two repeats (the allantoicase repeats: AR1 and AR2), which are connected by a flexible linker. The crystal structure, resolved at 2.4A resolution, r |
https://en.wikipedia.org/wiki/Allantoinase | In enzymology, an allantoinase () is an enzyme that catalyzes the chemical reaction
(S)-allantoin + H2O allantoate
Thus, the two substrates of this enzyme are (S)-allantoin and H2O, whereas its product is allantoate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is (S)-allantoin amidohydrolase. This enzyme participates in purine metabolism.
References
EC 3.5.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Allophanate%20hydrolase | In enzymology, an allophanate hydrolase () is an enzyme that catalyzes the chemical reaction
allophanate + 3 H2O + H+ 2 HCO3− + 2 NH4+
Thus, the two substrates of this enzyme are allophanate (urea-1-carboxylate or N-carbamoylcarbamate) and H2O, whereas its two products are HCO3− and NH4+.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is urea-1-carboxylate amidohydrolase. This enzyme is also called allophanate lyase. This enzyme participates in urea cycle and metabolism of amino groups and atrazine degradation.
See also
Urea carboxylase
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Amidase | In enzymology, an amidase (, acylamidase, acylase (misleading), amidohydrolase (ambiguous), deaminase (ambiguous), fatty acylamidase, N-acetylaminohydrolase (ambiguous)) is an enzyme that catalyzes the hydrolysis of an amide. In this way, the two substrates of this enzyme are an amide and H2O, whereas its two products are monocarboxylate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is acylamide amidohydrolase. Other names in common use include acylamidase, acylase, amidohydrolase, deaminase, fatty acylamidase, and N-acetylaminohydrolase. This enzyme participates in 6 metabolic pathways: urea cycle and metabolism of amino groups, phenylalanine metabolism, tryptophan metabolism, cyanoamino acid metabolism, benzoate degradation via coa ligation, and styrene degradation.
Amidases contain a conserved stretch of approximately 130 amino acids known as the AS sequence. They are widespread, being found in both prokaryotes and eukaryotes. AS enzymes catalyse the hydrolysis of amide bonds (CO-NH2), although the family has diverged widely with regard to substrate specificity and function. Nonetheless, these enzymes maintain a core alpha/beta/alpha structure, where the topologies of the N- and C-terminal halves are similar. AS enzymes characteristically have a highly conserved C-terminal region rich in serine and glycine residues, but de |
https://en.wikipedia.org/wiki/Amidinoaspartase | In enzymology, an amidinoaspartase () is an enzyme that catalyzes the chemical reaction
N-amidino-L-aspartate + H2O L-aspartate + urea
Thus, the two substrates of this enzyme are N-amidino-L-aspartate and H2O, whereas its two products are L-aspartate and urea.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is N-amidino-L-aspartate amidinohydrolase. This enzyme is also called amidinoaspartic amidinohydrolase.
References
EC 3.5.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aminoacylase | In enzymology, an aminoacylase () is an enzyme that catalyzes the chemical reaction
N-acyl-L-amino acid + H2O carboxylate + L-amino acid
Thus, the two substrates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acyl-L-amino acid amidohydrolase. Other names in common use include dehydropeptidase II, histozyme, hippuricase, benzamidase, acylase I, hippurase, amido acid deacylase, L-aminoacylase, acylase, aminoacylase I, L-amino-acid acylase, alpha-N-acylaminoacid hydrolase, long acyl amidoacylase, and short acyl amidoacylase. This enzyme participates in urea cycle and metabolism of amino groups.
Enzyme structure
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and . These structures also correspond to two known primary amino acid sequences for aminoacylases. The associated papers identify two types of domains comprising aminoacylases: Zinc binding domains - which bind Zn2+ ions - and domains that facilitate dimerization of Zinc binding domains. It is this dimerization that allows catalysis to occur, since aminoacylase's active site lies between its two Zinc binding domains.
Bound Zinc facilitates the binding of the N-acyl-L-amino acid substrate, causing a conformati |
https://en.wikipedia.org/wiki/Aminoimidazolase | In enzymology, an aminoimidazolase () is an enzyme that catalyzes the chemical reaction
4-aminoimidazole + H2O unidentified product + NH3
Thus, the two substrates of this enzyme are 4-aminoimidazole and H2O, whereas its two products are unidentified product and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 4-aminoimidazole aminohydrolase. This enzyme is also called 4-aminoimidazole hydrolase. This enzyme participates in purine metabolism. It employs one cofactor, iron.
References
EC 3.5.4
Iron enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Arginine%20deiminase | In enzymology, an arginine deiminase () is an enzyme that catalyzes the chemical reaction
L-arginine + H2O L-citrulline + NH3
Thus, the two substrates of this enzyme are L-arginine and H2O, whereas its two products are L-citrulline and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is L-arginine iminohydrolase. Other names in common use include arginine dihydrolase, citrulline iminase, and L-arginine deiminase. This enzyme participates in arginine and proline metabolism. This enzyme is widely expressed in bacteria, including streptococcus and actinomyces. The bacterial arginine deiminase expression could be regulated by various environmental factors.
Recently, a new enzyme that catalyzes the chemical reaction
L-arginine + 2H2O L-ornithine + 2NH3 + CO2 was identified in cyanobacteria which should be named as arginine dihydrolase.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 3.5.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Arylacetonitrilase | In enzymology, an arylacetonitrilase () is an enzyme that catalyzes the chemical reaction
4-chlorophenylacetonitrile + 2 H2O 4-chlorophenylacetate + NH3
Thus, the two substrates of this enzyme are 4-chlorophenylacetonitrile and H2O, whereas its two products are 4-chlorophenylacetate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in nitriles. The systematic name of this enzyme class is arylacetonitrile aminohydrolase. This enzyme participates in cyanoamino acid metabolism.
References
EC 3.5.5
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aryl-acylamidase | In enzymology, an aryl-acylamidase () is an enzyme that catalyzes the chemical reaction
an anilide + H2O a carboxylate + aniline
Thus, the two substrates of this enzyme are anilide and H2O, whereas its two products are carboxylate and aniline.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is aryl-acylamide amidohydrolase. Other names in common use include AAA-1, AAA-2, brain acetylcholinesterase (is associated with AAA-2), and pseudocholinesterase (associated with arylacylamidase).
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Arylalkyl%20acylamidase | In enzymology, an arylalkyl acylamidase () is an enzyme that catalyzes the chemical reaction
N-acetylarylalkylamine + H2O arylalkylamine + acetate
Thus, the two substrates of this enzyme are N-acetylarylalkylamine and H2O, whereas its two products are arylalkylamine and acetate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acetylarylalkylamine amidohydrolase. This enzyme is also called aralkyl acylamidase.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Arylformamidase | In enzymology, an arylformamidase () is an enzyme that catalyzes the chemical reaction
N-formyl-L-kynurenine + H2O formate + L-kynurenine
Thus, the two substrates of this enzyme are N-formyl-L-kynurenine and H2O, whereas its two products are formate and L-kynurenine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is aryl-formylamine amidohydrolase. Other names in common use include kynurenine formamidase, formylase, formylkynureninase, formylkynurenine formamidase, formamidase I, and formamidase II. This enzyme participates in tryptophan metabolism and glyoxylate and dicarboxylate metabolism.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/ATP%20deaminase | In enzymology, an ATP deaminase () is an enzyme that catalyzes the chemical reaction
ATP + H2O ITP + NH3
Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ITP and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is ATP aminohydrolase. This enzyme is also called adenosine triphosphate deaminase.
References
EC 3.5.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-ureidopropionase | In enzymology, a beta-ureidopropionase () is an enzyme that catalyzes the chemical reaction
N-carbamoyl-beta-alanine + H2O beta-alanine + CO2 + NH3
Thus, the two substrates of this enzyme are N-carbamoyl-beta-alanine and H2O, whereas its 3 products are beta-alanine, CO2, and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-carbamoyl-beta-alanine amidohydrolase. This enzyme participates in 3 metabolic pathways: pyrimidine metabolism, beta-alanine metabolism, and pantothenate and coenzyme A biosynthesis.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Biuret%20amidohydrolase | In enzymology, a biuret amidohydrolase () is an enzyme that catalyzes the chemical reaction
biuret + H2O urea(CH4N2O) + CO2 + NH3
Thus, the two substrates of this enzyme are biuret and H2O, whereas its 3 products are urea, CO2, and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is biuret amidohydrolase. This enzyme participates in atrazine degradation.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Blasticidin-S%20deaminase | In enzymology, a blasticidin-S deaminase () is an enzyme that catalyzes the chemical reaction
blasticidin S + H2O deaminohydroxyblasticidin S + NH3
Thus, the two substrates of this enzyme are blasticidin S and H2O, whereas its two products are deaminohydroxyblasticidin S and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is blasticidin-S aminohydrolase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.5.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Bromoxynil%20nitrilase | In enzymology, a bromoxynil nitrilase () is an enzyme that catalyzes the chemical reaction
3,5-dibromo-4-hydroxybenzonitrile + 2 H2O 3,5-dibromo-4-hydroxy-benzoate + NH3
Thus, the two substrates of this enzyme are 3,5-dibromo-4-hydroxybenzonitrile and H2O, whereas its two products are 3,5-dibromo-4-hydroxy-benzoate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in nitriles. The systematic name of this enzyme class is 3,5-dibromo-4-hydroxybenzonitrile aminohydrolase. This enzyme participates in 1,4-dichlorobenzene degradation.
References
EC 3.5.5
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Carboxymethylhydantoinase | In enzymology, a carboxymethylhydantoinase () is an enzyme that catalyzes the chemical reaction
L-5-carboxymethylhydantoin + H2O N-carbamoyl-L-aspartate
Thus, the two substrates of this enzyme are L-5-carboxymethylhydantoin and H2O, whereas its product is N-carbamoyl-L-aspartate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is L-5-carboxymethylhydantoin amidohydrolase. This enzyme is also called hydantoin hydrolase.
References
EC 3.5.2
Enzymes of unknown structure |
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