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https://en.wikipedia.org/wiki/Methylisocitrate%20lyase | The enzyme methylisocitrate lyase () catalyzes the chemical reaction
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate + succinate
The reaction is similar to that of isocitrate lyase, except that an additional methyl group (marked with an asterisk in the above scheme) is present, meaning that citrate is replaced by methylcitrate and glyoxylate by pyruvate. In fact, in some bacteria such as Mycobacterium tuberculosis, isocitrate lyase actually plays the role of methylisocitrate lyase.
This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase (succinate-forming). Other names in common use include 2-methylisocitrate lyase, MICL, and (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase. This enzyme participates in propanoate metabolism.
Methylisocitrate lyase was discovered in 1976.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and . The structure is very similar to that of phosphoenolpyruvate mutase. A homotetrameric biological unit is composed of beta barrels with the active site at one end. A magnesium ion is present in the active site, and an active-site "gating loop" moves inward toward it when substrate binds and away with no substrate bound, thus shielding the reaction from solvent. Helices are present all around |
https://en.wikipedia.org/wiki/Methylmalonyl-CoA%20decarboxylase | In enzymology, a methylmalonyl-CoA decarboxylase () is an enzyme that catalyzes the chemical reaction
(S)-methylmalonyl-CoA propanoyl-CoA + CO2
Hence, this enzyme has one substrate, (S)-methylmalonyl-CoA, and two products, propanoyl-CoA and CO2. Along with this reaction, this enzyme transports sodium cations across the membrane, creating a gradient which can be used for synthesis of ATP, hence its classification as a translocase.
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming). Other names in common use include propionyl-CoA carboxylase, propionyl coenzyme A carboxylase, methylmalonyl-coenzyme A decarboxylase, (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase [incorrect], and (S)-methylmalonyl-CoA carboxy-lyase. This enzyme participates in propanoate metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 4.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-acetylneuraminate%20lyase | The enzyme N-acetylneuraminate lyase () catalyzes the chemical reaction
N-acetylneuraminate N-acetyl-D-mannosamine + pyruvate
This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is N-acetylneuraminate pyruvate-lyase (N-acetyl-D-mannosamine-forming). Other names in common use include N-acetylneuraminic acid aldolase, acetylneuraminate lyase, sialic aldolase, sialic acid aldolase, sialate lyase, N-acetylneuraminic aldolase, neuraminic aldolase, N-acetylneuraminate aldolase, neuraminic acid aldolase, N-acetylneuraminic acid aldolase, neuraminate aldolase, N-acetylneuraminic lyase, N-acetylneuraminic acid lyase, NPL, NALase, NANA lyase, acetylneuraminate pyruvate-lyase, and N-acetylneuraminate pyruvate-lyase. This enzyme participates in aminosugars metabolism.
Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , and .
References
EC 4.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Naphthoate%20synthase | The enzyme 1,4-dihydroxy-2-naphthoyl-CoA synthase () catalyzes the sixth step in the biosynthesis of phylloquinone and menaquinone, the two forms of vitamin K. In E. coli, 1,4-dihydroxy-2-naphthoyl-CoA synthase, formerly known as naphthoate synthase, is encoded by menB and uses O-succinylbenzoyl-CoA as a substrate and converts it to 1,4-dihydroxy-2-naphthoyl-CoA.
Nomenclature
MenB is part of the crotonase fold super family, named after the crotonase fold in their structure. The systematic name for MenB is 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA dehydratase (cyclizing). Other common names include:
Naphthoate synthase
1,4-dihydroxy-2-naphthoate synthase
Dihydroxynaphthoate synthase
DHNA-CoA synthase
Reaction
It was originally thought that the product of this reaction had an oxygen where the SCoA currently resides, however; new research has shown that MenB only catalyzes the above reaction. There is a different enzyme that cleaves the SCoA and attaches the oxygen.
Structure
MenB is composed of two hexamers in an asymmetric unit, these hexamers are each composed of two trimers in an eclipsed arrangement. Each sub unit of the hexamers has three C terminal alpha helices, and a N terminal spiral core. These sub units come together to form the active site of the enzyme.
The channel formed by alpha helices that can be seen in the middle of the enzyme leads to the active site. This opening exists on both top and bottom of the enzyme, allowing substrates different entry points |
https://en.wikipedia.org/wiki/GP1BA | Platelet glycoprotein Ib alpha chain also known as glycoprotein Ib (platelet), alpha polypeptide or CD42b (Cluster of Differentiation 42b), is a protein that in humans is encoded by the GP1BA gene.
Function
Glycoprotein Ib (GP Ib) is a platelet surface membrane glycoprotein receptor composed of a heterodimer, an alpha chain and a beta chain, that are linked by disulfide bonds. The Gp Ib functions as a receptor for von Willebrand factor (VWF). The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX and platelet glycoprotein V to form the glycoprotein Ib-IX-V complex. Binding of the GP Ib-IX-V complex to VWF facilitates initial platelet adhesion to vascular subendothelium after vascular injury, and also initiates signaling events within the platelet that lead to enhanced platelet activation, thrombosis, and hemostasis. This gene encodes the alpha subunit. Several polymorphisms and mutations have been described in this gene, some of which are the cause of Bernard–Soulier syndromes and platelet-type von Willebrand disease.
Interactions
GP1BA has been shown to interact with YWHAZ and FLNB.
See also
Cluster of differentiation
References
Further reading
External links
Clusters of differentiation |
https://en.wikipedia.org/wiki/Octadecanal%20decarbonylase | The enzyme octadecanal decarbonylase () catalyzes the chemical reaction
octadecanal heptadecane + CO
This enzyme belongs to the family of lyases, specifically in the "catch-all" class of carbon-carbon lyases. The systematic name of this enzyme class is octadecanal alkane-lyase. Other names in common use include decarbonylase, and aldehyde decarbonylase. At least one compound, EDTA is known to inhibit this enzyme.
References
EC 4.1.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/O-pyrocatechuate%20decarboxylase | The enzyme o-pyrocatechuate decarboxylase () catalyzes the chemical reaction
2,3-dihydroxybenzoate catechol + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 2,3-dihydroxybenzoate carboxy-lyase (catechol-forming). This enzyme is also called 2,3-dihydroxybenzoate carboxy-lyase. This enzyme participates in benzoate degradation via hydroxylation and carbazole degradation.
References
EC 4.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Leptin%20receptor | Leptin receptor, also known as LEP-R or OB-R, is a type I cytokine receptor, a protein that in humans is encoded by the LEPR gene. LEP-R functions as a receptor for the fat cell-specific hormone leptin. LEP-R has also been designated as CD295 (cluster of differentiation 295). Its location is the cell membrane, and it has extracellular, trans-membrane and intracellular sections (protein regions).
History
The Leptin Receptor was discovered in 1995 by Louis Tartaglia and his colleagues at Millennium Pharmaceuticals. This same team demonstrated the leptin receptor was expressed by the mouse db gene. Furthermore, in 1996, after co-discovering the Leptin gene with Jeffrey Friedman et al. in 1994, (which involved a reverse genetic/positional cloning strategy to clone ob and db), Rudolph Leibel, working with collaborators also at Millennium Pharmaceuticals and colleague Streamson Chua, confirmed cloning of the leptin receptor by demonstrating that an apparent leptin receptor cloned from a choroid plexus library using leptin as ligand, mapped to a physical map that included db and fa.
Structure
Like other cytokine receptors, Leptin receptor protein has three different regions: i) extracellular, ii) trans-membrane, and iii) intracellular. The extracellular part has 5 functional domains: i) membrane distal 1st cytokine receptor homology (CRH1), ii) Immunoglobulin like (Ig), iii) 2nd cytokine receptor homology (CRH2) and iv) two membrane proximal fibronectine type-III (FNIII) domains |
https://en.wikipedia.org/wiki/Orsellinate%20decarboxylase | The enzyme orsellinate decarboxylase () catalyzes the chemical reaction
2,4-dihydroxy-6-methylbenzoate orcinol + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 2,4-dihydroxy-6-methylbenzoate carboxy-lyase (orcinol-forming). This enzyme is also called orsellinate carboxy-lyase.
References
EC 4.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/VAV1 | Proto-oncogene vav is a protein that in humans is encoded by the VAV1 gene.
Function
The protein encoded by this proto-oncogene is a member of the Dbl family of guanine nucleotide exchange factors (GEF) for the Rho family of GTP binding proteins. The protein is important in hematopoiesis, playing a role in T-cell and B-cell development and activation. This particular GEF has been identified as the specific binding partner of Nef proteins from HIV-1. Coexpression and binding of these partners initiates profound morphological changes, cytoskeletal rearrangements and the JNK/SAPK signaling cascade, leading to increased levels of viral transcription and replication.
Interactions
VAV1 has been shown to interact with:
ARHGDIB,
Abl gene,
Cbl gene
EZH2,
Grb2,
JAK2,
Ku70,
LAT,
LCP2,
MAPK1,
PIK3R1,
PLCG1,
PRKCQ,
S100B,
SHB,
SIAH2, and
Syk.
References
Further reading |
https://en.wikipedia.org/wiki/Oxalate%20decarboxylase | In enzymology, an oxalate decarboxylase () is an oxalate degrading enzyme that catalyzes the chemical reaction
oxalate + H+ formate + CO2
Thus, the two substrates of this enzyme are oxalate and H+, whereas its two products are formate and CO2.
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is oxalate carboxy-lyase (formate-forming). This enzyme is also called oxalate carboxy-lyase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 4.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Oxalomalate%20lyase | The enzyme oxalomalate lyase () catalyzes the chemical reaction
3-oxalomalate oxaloacetate + glyoxylate
This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 3-oxalomalate glyoxylate-lyase (oxaloacetate-forming). This enzyme is also called 3-oxalomalate glyoxylate-lyase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
EC 4.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Coagulation%20factor%20II%20receptor | Proteinase-activated receptor 1 (PAR1) also known as protease-activated receptor 1 or coagulation factor II (thrombin) receptor is a protein that in humans is encoded by the F2R gene. PAR1 is a G protein-coupled receptor and one of four protease-activated receptors involved in the regulation of thrombotic response. Highly expressed in platelets and endothelial cells, PAR1 plays a key role in mediating the interplay between coagulation and inflammation, which is important in the pathogenesis of inflammatory and fibrotic lung diseases. It is also involved both in disruption and maintenance of endothelial barrier integrity, through interaction with either thrombin or activated protein C, respectively.
Structure
PAR1 is a transmembrane G-protein-coupled receptor (GPCR) that shares much of its structure with the other protease-activated receptors. These characteristics include having seven transmembrane alpha helices, four extracellular loops and three intracellular loops. PAR1 specifically contains 425 amino acid residues arranged for optimal binding of thrombin at its extracellular N-terminus. The C-terminus of PAR1 is located on the intracellular side of the cell membrane as part of its cytoplasmic tail.
Signal transduction pathway
Activation
PAR1 is activated when the terminal 41 amino acids of its N-terminus are cleaved by thrombin, a serine protease. Thrombin recognizes PAR1 by a Lysine-Aspartate-Proline-Arginine-Serine sequence at the N-terminal, where it cuts the pept |
https://en.wikipedia.org/wiki/Oxalyl-CoA%20decarboxylase | The enzyme oxalyl-CoA decarboxylase (OXC) (), primarily produced by the gastrointestinal bacterium Oxalobacter formigenes, catalyzes the chemical reaction
oxalyl-CoA formyl-CoA + CO2
OXC belongs to the family of lyases, specifically the carboxy-lyases (decarboxylases), which cleave carbon-carbon bonds. The systematic name of this enzyme class is oxalyl-CoA carboxy-lyase (formyl-CoA-forming). Other names in common use include oxalyl coenzyme A decarboxylase, and oxalyl-CoA carboxy-lyase. This enzyme participates in glyoxylate and dicarboxylate metabolism. It employs one cofactor, thiamin diphosphate (TPP), and plays a key role in catabolism of oxalate, a highly toxic compound that is a product of the oxidation of carbohydrates in many bacteria and plants. Oxalyl-CoA decarboxylase is extremely important for the elimination of ingested oxalates found in human foodstuffs like coffee, tea, and chocolate, and the ingestion of such foods in the absence of Oxalobacter formigenes in the gut can result in kidney disease or even death as a result of oxalate poisoning.
Evolution
Oxalyl-CoA decarboxylase is hypothesized to be evolutionarily related to acetolactate synthase, a TPP-dependent enzyme responsible for the biosynthesis of branched chain amino acids in certain organisms. Sequence alignments between the two enzymes support this claim, as do the presence of vestigial FAD-binding pockets that play no role in either enzyme's catalytic activity. The binding of FAD at this s |
https://en.wikipedia.org/wiki/Pantothenoylcysteine%20decarboxylase | The enzyme pantothenoylcysteine decarboxylase () catalyzes the chemical reaction
N-[(R)-pantothenoyl]-L-cysteine pantetheine + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is N-[(R)-pantothenoyl]-L-cysteine carboxy-lyase (pantetheine-forming). Other names in common use include pantothenylcysteine decarboxylase, and N-[(R)-pantothenoyl]-L-cysteine carboxy-lyase. This enzyme participates in pantothenate and coa biosynthesis.
References
EC 4.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phenylalanine%20decarboxylase | The enzyme phenylalanine decarboxylase () catalyzes the chemical reaction
L-phenylalanine phenethylamine + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-phenylalanine carboxy-lyase (phenylethylamine-forming). Other names in common use include L-phenylalanine decarboxylase, aromatic L-amino acid decarboxylase, and L-phenylalanine carboxy-lyase. This enzyme participates in phenylalanine metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 4.1.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phenylpyruvate%20decarboxylase | The enzyme phenylpyruvate decarboxylase () catalyzes the chemical reaction
phenylpyruvate phenylacetaldehyde + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is phenylpyruvate carboxy-lyase (phenylacetaldehyde-forming). This enzyme is also called phenylpyruvate carboxy-lyase. This enzyme participates in phenylalanine and tryptophan 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 4.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phenylserine%20aldolase | The enzyme phenylserine aldolase () catalyzes the chemical reaction
L-threo-3-phenylserine glycine + benzaldehyde
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-threo-3-phenylserine benzaldehyde-lyase (glycine-forming). This enzyme is also called L-threo-3-phenylserine benzaldehyde-lyase. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 4.1.2
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phosphatidylserine%20decarboxylase | The enzyme phosphatidylserine decarboxylase () catalyzes the chemical reaction
phosphatidyl-L-serine phosphatidylethanolamine + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is phosphatidyl-L-serine carboxy-lyase (phosphatidylethanolamine-forming). Other names in common use include PS decarboxylase, and phosphatidyl-L-serine carboxy-lyase. This enzyme participates in glycine, serine and threonine metabolism, and glycerophospholipid metabolism. It has two cofactors: pyridoxal phosphate, and Pyruvate.
References
EC 4.1.1
Pyridoxal phosphate enzymes
Pyruvate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoketolase | The enzyme phosphoketolase() catalyzes the chemical reactions
D-xylulose 5-phosphate + phosphate acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O ()
D-fructose 6-phosphate + phosphate acetyl phosphate + D-erythrose 4-phosphate + H2O (EC 4.1.2.22)
D-sedoheptulose 7-phosphate + phosphate acetyl phosphate + D-ribose 5-phosphate + H2O
Phosphoketolase is considered a promiscuous enzyme because it was demonstrated to use 3 different sugar phosphates as substrates. In a recent genetic study, more than 150 putative phosphoketolase genes exhibiting varying catalytic properties were found in 650 analyzed bacterial genomes.
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. It participates in 3 metabolic pathways: pentose phosphate pathway, methane metabolism, and carbon fixation. It employs one cofactor, thiamin diphosphate. Phosphoketolase was previously used for biotechnological purposes as it enables the construction of synthetic pathways that allow complete carbon conservation without the generation of reducing power.
References
EC 4.1.2
Thiamine enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphonopyruvate%20decarboxylase | The enzyme phosphonopyruvate decarboxylase () catalyzes the chemical reaction
3-phosphonopyruvate 2-phosphonoacetaldehyde + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 3-phosphonopyruvate carboxy-lyase (2-phosphonoacetaldehyde-forming). This enzyme is also called 3-phosphonopyruvate carboxy-lyase. This enzyme participates in aminophosphonate metabolism.
References
EC 4.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphopantothenoylcysteine%20decarboxylase | The enzyme phosphopantothenoylcysteine decarboxylase () catalyzes the chemical reaction
N-[(R)-4'-phosphopantothenoyl]-L-cysteine pantotheine 4'-phosphate + CO2
This enzyme belongs to the family of lyases, to be specific the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is N-[(R)-4'-phosphopantothenoyl]-L-cysteine carboxy-lyase (pantotheine-4'-phosphate-forming). This enzyme participates in coenzyme A (CoA) biosynthesis from pantothenic acid.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 4.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Propioin%20synthase | The enzyme propioin synthase () catalyzes the chemical reaction
4-hydroxy-3-hexanone 2 propanal
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 4-hydroxy-3-hexanone propanal-lyase (propanal-forming). Other names in common use include 4-hydroxy-3-hexanone aldolase, and 4-hydroxy-3-hexanone propanal-lyase.
References
EC 4.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Protocatechuate%20decarboxylase | The enzyme protocatechuate decarboxylase () catalyzes the chemical reaction
3,4-dihydroxybenzoate catechol + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 3,4-dihydroxybenzoate carboxy-lyase (catechol-forming). Other names in common use include 3,4-dihydroxybenzoate decarboxylase, and protocatechuate carboxy-lyase. This enzyme participates in benzoate degradation via hydroxylation.
References
EC 4.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Rhamnulose-1-phosphate%20aldolase | The enzyme rhamnulose-1-phosphate aldolase () catalyzes the chemical reaction
L-rhamnulose 1-phosphate glycerone phosphate + (S)-lactaldehyde
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-rhamnulose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming). Other names in common use include rhamnulose phosphate aldolase, L-rhamnulose 1-phosphate aldolase, L-rhamnulose-phosphate aldolase, and L-rhamnulose-1-phosphate lactaldehyde-lyase. This enzyme participates in pentose and glucuronate interconversions and fructose and mannose metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 4.1.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Sphinganine-1-phosphate%20aldolase | The enzyme sphinganine-1-phosphate aldolase () catalyzes the chemical reaction
sphinganine 1-phosphate phosphoethanolamine + palmitaldehyde
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is sphinganine-1-phosphate palmitaldehyde-lyase (phosphoethanolamine-forming). Other names in common use include dihydrosphingosine 1-phosphate aldolase, sphinganine-1-phosphate alkanal-lyase, sphinganine-1-phosphate lyase, and sphinganine-1-phosphate palmitaldehyde-lyase. This enzyme participates in sphingolipid metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 4.1.2
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Stipitatonate%20decarboxylase | The enzyme stipitatonate decarboxylase () catalyzes the chemical reaction
stipitatonate stipitatate + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is stipitatonate carboxy-lyase (decyclizing, stipitatate-forming). This enzyme is also called stipitatonate carboxy-lyase (decyclizing).
References
EC 4.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sulfinoalanine%20decarboxylase | The enzyme sulfinoalanine decarboxylase () catalyzes the chemical reaction
3-sulfino-L-alanine hypotaurine + CO2
Hence, this enzyme has one substrate, 3-sulfino-L-alanine (also known as Cysteine sulfinic acid), and two products, hypotaurine and CO2.
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 3-sulfino-L-alanine carboxy-lyase (hypotaurine-forming). Other names in common use include cysteine-sulfinate decarboxylase, L-cysteinesulfinic acid decarboxylase, cysteine-sulfinate decarboxylase, CADCase/CSADCase, CSAD, cysteic decarboxylase, cysteinesulfinic acid decarboxylase, cysteinesulfinate decarboxylase, sulfoalanine decarboxylase, and 3-sulfino-L-alanine carboxy-lyase. This enzyme participates in taurine metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 4.1.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Sulfopyruvate%20decarboxylase | The enzyme sulfopyruvate decarboxylase () catalyzes the chemical reaction
3-sulfopyruvate 2-sulfoacetaldehyde + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 3-sulfopyruvate carboxy-lyase (2-sulfoacetaldehyde-forming). This enzyme is also called sulfopyruvate carboxy-lyase.
References
EC 4.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tagatose-bisphosphate%20aldolase | The enzyme tagatose-bisphosphate aldolase () catalyzes the chemical reaction
D-tagatose 1,6-bisphosphate glycerone phosphate + Dglyceraldehyde 3-phosphate
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is D-tagatose 1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase (glycerone-phosphate-forming). This enzyme is also called D-tagatose-1,6-bisphosphate triosephosphate lyase. This enzyme participates in galactose 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 4.1.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Tartrate%20decarboxylase | The enzyme tartrate decarboxylase () catalyzes the chemical reaction
(R,R)-tartrate D-glycerate + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (R,R)-tartrate carboxy-lyase (D-glycerate-forming). This enzyme is also called (R,R)-tartrate carboxy-lyase.
References
EC 4.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tartronate-semialdehyde%20synthase | The enzyme tartronate-semialdehyde synthase () catalyzes the chemical reaction
2 glyoxylate tartronate semialdehyde + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is glyoxylate carboxy-lyase (dimerizing tartronate-semialdehyde-forming). Other names in common use include tartronate semialdehyde carboxylase, glyoxylate carbo-ligase, glyoxylic carbo-ligase, hydroxymalonic semialdehyde carboxylase, tartronic semialdehyde carboxylase, glyoxalate carboligase, and glyoxylate carboxy-lyase (dimerizing). This enzyme participates in glyoxylate and dicarboxylate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.
References
EC 4.1.1
Flavoproteins
Thiamin diphosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Threonine%20aldolase | The enzyme threonine aldolase () is an enzyme that catalyzes the chemical reaction
L-threonine glycine + acetaldehyde
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-threonine acetaldehyde-lyase (glycine-forming). This enzyme is also called L-threonine acetaldehyde-lyase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
Presence in human and mouse
The enzyme is synthesized and functional in mice.
Humans also have the remnants of the gene, coding this enzyme (GLY1), however it is damaged by past mutations and inactive. Human gene contains two single nucleotide deletions causing frameshifts and premature stop codons. Also, the encoded protein would not be active anyway due mutations in other highly conserved regions. Human gene is no longer transcribed into RNA.
References
EC 4.1.2
Pyridoxal phosphate enzymes
Enzymes of known structure
Pseudogenes |
https://en.wikipedia.org/wiki/Threonine-phosphate%20decarboxylase | The enzyme threonine-phosphate decarboxylase () catalyzes the chemical reaction
L-threonine O-3-phosphate (R)-1-aminopropan-2-yl phosphate + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-threonine-O-3-phosphate carboxy-lyase [(R)-1-aminopropan-2-yl-phosphate-forming]. Other names in common use include L-threonine-O-3-phosphate decarboxylase, CobD and L-threonine-O-3-phosphate carboxy-lyase. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in anaerobic bacteria such as Salmonella typhimurium and Bacillus megaterium. In the next step, (R)-1-aminopropan-2-ol is attached to adenosylcobyric acid, forming adenosylcobinamide phosphate.
See also
Cobalamin biosynthesis
References
EC 4.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trimethylamine-oxide%20aldolase | The enzyme trimethylamine-oxide aldolase () catalyzes the chemical reaction
trimethylamine N-oxide dimethylamine + formaldehyde
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is trimethylamine-N-oxide formaldehyde-lyase (dimethylamine-forming). Other names in common use include trimethylamine N-oxide formaldehyde-lyase, trimethylamine N-oxide aldolase, trimethylamine N-oxide demethylase, and trimethylamine-N-oxide formaldehyde-lyase. This enzyme participates in methane metabolism.
References
EC 4.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tryptophanase | The enzyme tryptophanase () catalyzes the chemical reaction
L-tryptophan + H2O indole + pyruvate + NH3
This enzyme belongs to the family of lyases, specifically in the "catch-all" class of carbon-carbon lyases. The systematic name of this enzyme class is L-tryptophan indole-lyase (deaminating; pyruvate-forming). Other names in common use include L-tryptophanase, and L-tryptophan indole-lyase (deaminating). This enzyme participates in tryptophan metabolism and nitrogen metabolism. It has 2 cofactors: pyridoxal phosphate, and potassium.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1AX4, 2C44, and 2OQX.
References
External links
EC 4.1.99
Pyridoxal phosphate enzymes
Potassium enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Tyrosine%20decarboxylase | The enzyme tyrosine decarboxylase () catalyzes the chemical reaction
L-tyrosine tyramine + CO2
Hence, this enzyme has one substrate, L-tyrosine, and two products, tyramine and carbon dioxide.
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-tyrosine carboxy-lyase (tyramine-forming). Other names in common use include L-tyrosine decarboxylase, L-(−)-tyrosine apodecarboxylase, and L-tyrosine carboxy-lyase. This enzyme participates in tyrosine metabolism and alkaloid biosynthesis. It employs one cofactor, pyridoxal phosphate.
References
EC 4.1.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tyrosine%20phenol-lyase | The enzyme tyrosine phenol-lyase () catalyzes the chemical reaction
L-tyrosine + H2O phenol + pyruvate + NH3
This enzyme belongs to the family of lyases, specifically in the "catch-all" class of carbon-carbon lyases. The systematic name of this enzyme class is L-tyrosine phenol-lyase (deaminating; pyruvate-forming). Other names in common use include beta-tyrosinase, and L-tyrosine phenol-lyase (deaminating). This enzyme participates in tyrosine metabolism and nitrogen metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, five structures have been solved for this class of enzyme, with PDB accession codes , , , , and .
References
EC 4.1.99
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/UDP-galacturonate%20decarboxylase | The enzyme UDP-galacturonate decarboxylase () catalyzes the chemical reaction
UDP-D-galacturonate UDP-L-arabinose + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is UDP-D-galacturonate carboxy-lyase (UDP-L-arabinose-forming). Other names in common use include UDP-galacturonic acid decarboxylase, UDPGalUA carboxy lyase, and UDP-D-galacturonate carboxy-lyase. This enzyme participates in nucleotide sugars metabolism.
References
EC 4.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-glucuronate%20decarboxylase | The enzyme UDP-glucuronate decarboxylase () catalyzes the chemical reaction
UDP-D-glucuronate UDP-D-xylose + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is UDP-D-glucuronate carboxy-lyase (UDP-D-xylose-forming). Other names in common use include uridine-diphosphoglucuronate decarboxylase, and UDP-D-glucuronate carboxy-lyase. This enzyme participates in starch and sucrose metabolism and nucleotide sugars metabolism. It employs one cofactor, NAD+.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 4.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Uracil-5-carboxylate%20decarboxylase | The enzyme uracil-5-carboxylate decarboxylase () catalyzes the chemical reaction
uracil 5-carboxylate uracil + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is uracil-5-carboxylate carboxy-lyase (uracil-forming). Other names in common use include uracil-5-carboxylic acid decarboxylase, and uracil-5-carboxylate carboxy-lyase.
References
EC 4.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Valine%20decarboxylase | In enzymology, a valine decarboxylase () is an enzyme that catalyzes the chemical reaction
L-valine 2-methylpropanamine + CO2
Hence, this enzyme has one substrate, L-valine, and two products, 2-methylpropanamine and CO2.
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-valine carboxy-lyase (2-methylpropanamine-forming). Other names in common use include leucine decarboxylase and L-valine carboxy-lyase. It employs one cofactor, pyridoxal phosphate.
References
EC 4.1.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Vanillin%20synthase | In enzymology, a vanillin synthase () is an enzyme that catalyzes the chemical reaction
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA vanillin + acetyl-CoA
Hence, this enzyme has one substrate, 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA, and two products, vanillin and acetyl-CoA.
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA vanillin-lyase (acetyl-CoA-forming). Other names in common use include 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA:vanillin lyase, and (acetyl-CoA-forming).
References
EC 4.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2%2C3-dihydroxybenzoate%E2%80%94serine%20ligase | In enzymology, an enterobactin synthase (2,3-dihydroxybenzoate—serine ligase, ) is an enzyme that catalyzes the chemical reaction
ATP + 2,3-dihydroxybenzoate + L-serine products of ATP breakdown + N-(2,3-dihydroxybenzoyl)-L-serine
The 3 substrates of this enzyme are ATP, 2,3-dihydroxybenzoate, and L-serine, whereas its two products are products of ATP breakdown and N-(2,3-dihydroxybenzoyl)-L-serine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is 2,3-dihydroxybenzoate:L-serine ligase. Other names in common use include N-(2,3-dihydroxybenzoyl)-serine synthetase, and 2,3-dihydroxybenzoylserine synthetase.
References
EC 6.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-furoate%E2%80%94CoA%20ligase | In enzymology, a 2-furoate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + 2-furoate + CoA AMP + diphosphate + 2-furoyl-CoA
The 3 substrates of this enzyme are ATP, 2-furoate, and CoA, whereas its 3 products are AMP, diphosphate, and 2-furoyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is 2-furoate:CoA ligase (AMP-forming). This enzyme is also called 2-furoyl coenzyme A synthetase.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-oxoglutarate%20carboxylase | In enzymology, a 2-oxoglutarate carboxylase () is an enzyme that catalyzes the chemical reaction
ATP + 2-oxoglutarate + HCO3- ADP + phosphate + oxalosuccinate
The 3 substrates of this enzyme are ATP, 2-oxoglutarate, and HCO3-, whereas its 3 products are ADP, phosphate, and oxalosuccinate.
This enzyme belongs to the family of ligases, specifically those forming carbon-carbon bonds. The systematic name of this enzyme class is '''. Other names in common use include oxalosuccinate synthetase, carboxylating factor for ICDH (incorrect), CFI, and OGC'''.
References
EC 6.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-alpha%2C7-alpha-dihydroxy-5-beta-cholestanate%E2%80%94CoA%20ligase | In enzymology, a 3α,7α-dihydroxy-5β-cholestanate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + (25R)-3alpha,7alpha-dihydroxy-5beta-cholestan-26-oate + CoA AMP + diphosphate + (25R)-3alpha,7alpha-dihydroxy-5beta-cholestanoyl-CoA
The 3 substrates of this enzyme are ATP, (25R)-3alpha,7alpha-dihydroxy-5beta-cholestan-26-oate, and CoA, whereas its 3 products are AMP, diphosphate, and (25R)-3alpha,7alpha-dihydroxy-5beta-cholestanoyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is (25R)-3alpha,7alpha-dihydroxy-5beta-cholestan-26-oate:CoA ligase (AMP-forming). Other names in common use include 3alpha,7alpha-dihydroxy-5beta-cholestanoyl coenzyme A synthetase, DHCA-CoA ligase, and 3alpha,7alpha-dihydroxy-5beta-cholestanate:CoA ligase (AMP-forming). This enzyme participates in bile acid biosynthesis.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-chlorobenzoate%E2%80%94CoA%20ligase | In enzymology, a 4-chlorobenzoate—CoA ligase () is an enzyme that catalyzes the chemical reaction
4-chlorobenzoate + CoA + ATP 4-chlorobenzoyl-CoA + AMP + diphosphate
The 3 substrates of this enzyme are 4-chlorobenzoate, CoA, and ATP, whereas its 3 products are 4-chlorobenzoyl-CoA, AMP, and diphosphate.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is 4-chlorobenzoate:CoA ligase. This enzyme participates in 2,4-dichlorobenzoate degradation. It employs one cofactor, magnesium.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 6.2.1
Magnesium enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/4-Coumarate-CoA%20ligase | In enzymology, a 4-coumarate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + 4-coumarate + CoA AMP + diphosphate + 4-coumaroyl-CoA
The 3 substrates of this enzyme are ATP, 4-coumarate, and CoA, whereas its 3 products are AMP, diphosphate, and 4-coumaroyl-CoA.
This enzyme belongs to the family of ligases, to be specific those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is 4-coumarate:CoA ligase (AMP-forming). Other names in common use include 4-coumaroyl-CoA synthetase, p-coumaroyl CoA ligase, p-coumaryl coenzyme A synthetase, p-coumaryl-CoA synthetase, p-coumaryl-CoA ligase, feruloyl CoA ligase, hydroxycinnamoyl CoA synthetase, 4-coumarate:coenzyme A ligase, caffeoyl coenzyme A synthetase, p-hydroxycinnamoyl coenzyme A synthetase, feruloyl coenzyme A synthetase, sinapoyl coenzyme A synthetase, 4-coumaryl-CoA synthetase, hydroxycinnamate:CoA ligase, p-coumaryl-CoA ligase, p-hydroxycinnamic acid:CoA ligase, and 4CL. This enzyme participates in phenylpropanoid biosynthesis.
References
EC 6.2.1
Enzymes of unknown structure
Hydroxycinnamic acids metabolism |
https://en.wikipedia.org/wiki/4-hydroxybenzoate%E2%80%94CoA%20ligase | In enzymology, a 4-hydroxybenzoate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + 4-hydroxybenzoate + CoA AMP + diphosphate + 4-hydroxybenzoyl-CoA
The 3 substrates of this enzyme are ATP, 4-hydroxybenzoate, and CoA, whereas its 3 products are AMP, diphosphate, and 4-hydroxybenzoyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is 4-hydroxybenzoate:CoA ligase (AMP-forming). Other names in common use include 4-hydroxybenzoate-CoA synthetase, 4-hydroxybenzoate-coenzyme A ligase (AMP-forming), 4-hydroxybenzoyl coenzyme A synthetase, and 4-hydroxybenzoyl-CoA ligase. This enzyme participates in benzoate degradation via coa ligation.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-methyleneglutamate%E2%80%94ammonia%20ligase | In enzymology, a 4-methyleneglutamate—ammonia ligase () is an enzyme that catalyzes the chemical reaction
ATP + 4-methylene-L-glutamate + NH3 AMP + diphosphate + 4-methylene-L-glutamine
The 3 substrates of this enzyme are ATP, 4-methylene-L-glutamate, and NH3, whereas its 3 products are AMP, diphosphate, and 4-methylene-L-glutamine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The systematic name of this enzyme class is 4-methylene-L-glutamate:ammonia ligase (AMP-forming). This enzyme is also called 4-methyleneglutamine synthetase. This enzyme participates in c5-branched dibasic acid metabolism.
References
EC 6.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-%28carboxyamino%29imidazole%20ribonucleotide%20synthase | In enzymology, a 5-(carboxyamino)imidazole ribonucleotide synthase () is an enzyme that catalyzes the chemical reaction
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole + HCO3− ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
The 3 substrates of this enzyme are ATP, 5-amino-1-(5-phospho-D-ribosyl)imidazole ("AIR"), and HCO3−, whereas its 3 products are ADP, phosphate, and 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is 5-amino-1-(5-phospho-D-ribosyl)imidazole:carbon-dioxide ligase (ADP-forming).
References
EC 6.3.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-formyltetrahydrofolate%20cyclo-ligase | In enzymology, a 5-formyltetrahydrofolate cyclo-ligase () is an enzyme that catalyzes the chemical reaction
ATP + 5-formyltetrahydrofolate (folinic acid) ADP + phosphate + 5,10-methenyltetrahydrofolate
Thus, the two substrates of this enzyme are ATP and 5-formyltetrahydrofolate, whereas its 3 products are ADP, phosphate, and 5,10-methenyltetrahydrofolate.
This enzyme belongs to the family of ligases, specifically the cyclo-ligases, which form carbon-nitrogen bonds. The systematic name of this enzyme class is 5-formyltetrahydrofolate cyclo-ligase (ADP-forming). Other names in common use include 5,10-methenyltetrahydrofolate synthetase (MTHFS), formyltetrahydrofolic cyclodehydrase, and 5-formyltetrahydrofolate cyclodehydrase. This enzyme participates in one carbon pool by folate.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
Role in pathology
Mutations of the MTHFS gene cause the disease 5,10-methenyltetrahydrofolate synthetase deficiency.
References
EC 6.3.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/6-carboxyhexanoate%E2%80%94CoA%20ligase | In enzymology, a 6-carboxyhexanoate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + 6-carboxyhexanoate + CoA AMP + diphosphate + 6-carboxyhexanoyl-CoA
The 3 substrates of this enzyme are ATP, 6-carboxyhexanoate, and CoA, whereas its 3 products are AMP, diphosphate, and 6-carboxyhexanoyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is 6-carboxyhexanoate:CoA ligase (AMP-forming). Other names in common use include 6-carboxyhexanoyl-CoA synthetase, and pimelyl-CoA synthetase. This enzyme participates in biotin metabolism.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetate%E2%80%94CoA%20ligase%20%28ADP-forming%29 | In enzymology, an acetate—CoA ligase (ADP-forming) () is an enzyme that catalyzes the chemical reaction
ATP + acetate + CoA ADP + phosphate + acetyl-CoA
The 3 substrates of this enzyme are ATP, acetate, and CoA, whereas its 3 products are ADP, phosphate, and acetyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is acetate:CoA ligase (ADP-forming). Other names in common use include acetyl-CoA synthetase (ADP-forming), acetyl coenzyme A synthetase (adenosine diphosphate-forming), and acetate thiokinase. This enzyme participates in pyruvate metabolism and propanoate metabolism.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetoacetate%E2%80%94CoA%20ligase | In enzymology, an acetoacetate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + acetoacetate + CoA AMP + diphosphate + acetoacetyl-CoA
The 3 substrates of this enzyme are ATP, acetoacetate, and CoA, whereas its 3 products are AMP, diphosphate, and acetoacetyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is acetoacetate:CoA ligase (AMP-forming). This enzyme is also called acetoacetyl-CoA synthetase. This enzyme participates in butanoate metabolism.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetone%20carboxylase | In enzymology, an acetone carboxylase () is an enzyme that catalyzes the chemical reaction
acetone + CO2 + ATP + 2 H2O acetoacetate + AMP + 2 phosphate
The 4 substrates of this enzyme are acetone, CO2, ATP, and H2O, whereas its 3 products are acetoacetate, AMP, and phosphate.
This enzyme belongs to the family of ligases, specifically those forming carbon-carbon bonds. The systematic name of this enzyme class is acetone:carbon-dioxide ligase (AMP-forming).
References
EC 6.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acid%E2%80%94CoA%20ligase%20%28GDP-forming%29 | In enzymology, an acid—CoA ligase (GDP-forming) () is an enzyme that catalyzes the chemical reaction
GTP + an acid + CoA GDP + phosphate + acyl-CoA
The 3 substrates of this enzyme are GTP, acid, and CoA, whereas its 3 products are GDP, phosphate, and acyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is acid:CoA ligase (GDP-forming). Other names in common use include acyl-CoA synthetase (GDP-forming), and acyl coenzyme A synthetase (guanosine diphosphate forming).
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Adenosylcobyric%20acid%20synthase%20%28glutamine-hydrolysing%29 | In enzymology, an adenosylcobyric acid synthase (glutamine-hydrolysing) () is an enzyme that catalyzes the chemical reaction
4 ATP + adenosylcobyrinic acid a,c-diamide + 4 L-glutamine + 4 H2O 4 ADP + 4 phosphate + adenosylcobyric acid + 4 L-glutamate
The four substrates of this enzyme are ATP, adenosylcobyrinic acid a,c-diamide, L-glutamine, and H2O; its four products are ADP, phosphate, adenosylcobyric acid, and L-glutamate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor (Glutamine amidotransferases). The systematic name of this enzyme class is adenosylcobyrinic-acid-a,c-diamide:L-glutamine amido-ligase (ADP-forming). This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria.
See also
Cobalamin biosynthesis
References
EC 6.3.5
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aerobactin%20synthase | In enzymology, an aerobactin synthase () is an enzyme that catalyzes the chemical reaction
4 ATP + citrate + 2 N6-acetyl-N6-hydroxy-L-lysine + 2 H2O 4 ADP + 4 phosphate + aerobactin
The 4 substrates of this enzyme are ATP, citrate, N6-acetyl-N6-hydroxy-L-lysine, and H2O, whereas its 3 products are ADP, phosphate, and aerobactin.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is citrate:N6-acetyl-N6-hydroxy-L-lysine ligase (ADP-forming). This enzyme is also called citrate:6-N-acetyl-6-N-hydroxy-L-lysine ligase (ADP-forming). This enzyme participates in lysine degradation.
References
EC 6.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alanine%E2%80%94tRNA%20ligase | In enzymology, an alanine—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-alanine + tRNAAla AMP + diphosphate + L-alanyl-tRNAAla
The 3 substrates of this enzyme are ATP, L-alanine, and tRNA(Ala), whereas its 3 products are AMP, diphosphate, and L-alanyl-tRNA(Ala).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-alanine:tRNAAla ligase (AMP-forming). Other names in common use include alanyl-tRNA synthetase, alanyl-transfer ribonucleate synthetase, alanyl-transfer RNA synthetase, alanyl-transfer ribonucleic acid synthetase, alanine-transfer RNA ligase, alanine transfer RNA synthetase, alanine tRNA synthetase, alanine translase, alanyl-transfer ribonucleate synthase, AlaRS, and Ala-tRNA synthetase. This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis.
See also
Sticky mouse - mutation in the gene
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Aminodeoxychorismate%20synthase | In enzymology, an aminodeoxychorismate synthase (EC 2.6.1.85) is an enzyme that catalyzes the chemical reaction
chorismate + L-glutamine 4-amino-4-deoxychorismate + L-glutamate
Thus, the two substrates of this enzyme are chorismate and L-glutamine, whereas its two products are 4-amino-4-deoxychorismate and L-glutamate.
It is part of a pathway for the biosynthesis of para-aminobenzoic acid (PABA); a precursor for the production of folates. Folates are family of cofactors that are essential for living organisms. Folate cofactors are used in several one-carbon transfer reactions required during the synthesis of essential metabolites, including methionine and thymidylate.
Aminodeoxychorismate synthase (PabB), a 51 kDa protein in E. coli, is encoded by the gene pabB. 4-amino-4-deoxychorismate, the product of PabB, can be converted to para-aminobenzoic acid by the enzyme 4-amino-4-deoxychorismate lyase (PabC).
Nonmenclature
This enzyme belongs to the class of transferases. This means that aminodeoxychorismate synthase catalyzes the transfer of one functional group from a molecule to another. Specifically, aminodeoxychorismate synthase is a transaminase that transfers an amino group to a keto acid. The systematic name is Chorismate:L-glutamine aminotransferase. Formerly aminodeoxychorismate synthase was referred to as PABA synthase; however this name is no longer recommended as it is understood that the formation of PABA requires the action of a further enzyme (4-amino-4-deo |
https://en.wikipedia.org/wiki/Anthranilate%E2%80%94CoA%20ligase | In enzymology, an anthranilate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + anthranilate + CoA AMP + diphosphate + anthranilyl-CoA
The 3 substrates of this enzyme are ATP, anthranilate, and CoA, whereas its 3 products are AMP, diphosphate, and anthranilyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is anthranilate:CoA ligase (AMP-forming). Other names in common use include anthraniloyl coenzyme A synthetase, 2-aminobenzoate-CoA ligase, 2-aminobenzoate-coenzyme A ligase, and 2-aminobenzoate coenzyme A ligase. This enzyme participates in 3 metabolic pathways: carbazole degradation, benzoate degradation via coa ligation, and acridone alkaloid biosynthesis.
References
EC 6.2.1
Enzymes of unknown structure
Anthranilates |
https://en.wikipedia.org/wiki/Arachidonate%E2%80%94CoA%20ligase | In enzymology, an arachidonate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + arachidonate + CoA AMP + diphosphate + arachidonoyl-CoA
The 3 substrates of this enzyme are ATP, arachidonate, and CoA, whereas its 3 products are AMP, diphosphate, and arachidonoyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is arachidonate:CoA ligase (AMP-forming). This enzyme is also called arachidonoyl-CoA synthetase.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Arginine%E2%80%94tRNA%20ligase | In enzymology, an arginine—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-arginine + tRNAArg AMP + diphosphate + L-arginyl-tRNAArg
The 3 substrates of this enzyme are ATP, L-arginine, and tRNA(Arg), whereas its 3 products are AMP, diphosphate, and L-arginyl-tRNA(Arg).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-arginine:tRNAArg ligase (AMP-forming). Other names in common use include arginyl-tRNA synthetase, arginyl-transfer ribonucleate synthetase, arginyl-transfer RNA synthetase, arginyl transfer ribonucleic acid synthetase, arginine-tRNA synthetase, and arginine translase. This enzyme participates in arginine and proline metabolism and aminoacyl-trna biosynthesis.
It contains a conserved domain at the N terminus called arginyl tRNA synthetase N terminal domain or additional domain 1 (Add-1). This domain is about 140 residues long and it has been suggested that it is involved in tRNA recognition.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
Further reading
Protein domains
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Asparagine%E2%80%94tRNA%20ligase | In enzymology, an asparagine-tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-asparagine + tRNAAsn AMP + diphosphate + L-asparaginyl-tRNAAsn
The 3 substrates of this enzyme are ATP, L-asparagine, and tRNA(Asn), whereas its 3 products are AMP, diphosphate, and L-asparaginyl-tRNA(Asn).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-asparagine:tRNAAsn ligase (AMP-forming). Other names in common use include asparaginyl-tRNA synthetase, asparaginyl-transfer ribonucleate synthetase, asparaginyl transfer RNA synthetase, asparaginyl transfer ribonucleic acid synthetase, asparagyl-transfer RNA synthetase, and asparagine translase. This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Asparaginyl-tRNA%20synthase%20%28glutamine-hydrolysing%29 | In enzymology, an asparaginyl-tRNA synthase (glutamine-hydrolysing) () is an enzyme that catalyzes the chemical reaction
ATP + aspartyl-tRNAAsn + L-glutamine ADP + phosphate + asparaginyl-tRNAAsn + L-glutamate
The 3 substrates of this enzyme are ATP, aspartyl-tRNA(Asn), and L-glutamine, whereas its 4 products are ADP, phosphate, asparaginyl-tRNA(Asn), and L-glutamate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. The systematic name of this enzyme class is aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming). This enzyme participates in glutamate metabolism and alanine and aspartate metabolism.
References
EC 6.3.5
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aspartate%E2%80%94ammonia%20ligase | In enzymology, an aspartate—ammonia ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-aspartate + NH3 AMP + diphosphate + L-asparagine
The 3 substrates of this enzyme are ATP, L-aspartate, and NH3, whereas its 3 products are AMP, diphosphate, and L-asparagine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The systematic name of this enzyme class is L-aspartate:ammonia ligase (AMP-forming). Other names in common use include asparagine synthetase, and L-asparagine synthetase. This enzyme participates in 3 metabolic pathways: alanine and aspartate metabolism, cyanoamino acid metabolism, and nitrogen metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 6.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Aspartate%E2%80%94ammonia%20ligase%20%28ADP-forming%29 | In enzymology, an aspartate—ammonia ligase (ADP-forming) () is an enzyme that catalyzes the chemical reaction
ATP + L-aspartate + NH3 ADP + phosphate + L-asparagine
The 3 substrates of this enzyme are ATP, L-aspartate, and NH3, whereas its 3 products are ADP, phosphate, and L-asparagine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The systematic name of this enzyme class is L-aspartate:ammonia ligase (ADP-forming). Other names in common use include asparagine synthetase (ADP-forming), and asparagine synthetase (adenosine diphosphate-forming). This enzyme participates in nitrogen metabolism.
References
EC 6.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aspartate%E2%80%94tRNA%28Asn%29%20ligase | Aspartate—tRNAAsn ligase (, nondiscriminating aspartyl-tRNA synthetase) is an enzyme with systematic name L-aspartate:tRNAAsx ligase (AMP-forming). This enzyme catalyses the following chemical reaction
ATP + L-aspartate + tRNAAsx AMP + diphosphate + aspartyl-tRNAAsx
The 3 substrates of this enzyme are ATP, L-asparagine, and tRNAAsx, whereas its 3 products are AMP, diphosphate, and asparaginyl-tRNAAsx.
When this enzyme acts on tRNAAsp, it catalyses the same reaction as EC 6.1.1.12, aspartate---tRNA ligase. It has, however, diminished discrimination, so that it can also form aspartyl-tRNAAsn. This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon [1]. This accounts for the ability of this enzyme in, for example, Thermus thermophilus, to recognize both tRNAAsp (GUC anticodon) and tRNAAsn (GUU anticodon). The aspartyl-tRNAAsn is not used in protein synthesis until it is converted by EC 6.3.5.6, asparaginyl-tRNA synthase (glutamine-hydrolysing), into asparaginyl-tRNAAsn.
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-asparaginyl:tRNAAsx ligase (AMP-forming). This enzyme is also called nondiscriminating asparaginyl-tRNA synthetase. This enzyme participates in alanine and asparagine metabolism.
References
EC 6.1.1
Enzymes of unknown str |
https://en.wikipedia.org/wiki/Aspartate%E2%80%94tRNA%20ligase | In enzymology, an aspartate—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-aspartate + tRNAAsp AMP + diphosphate + L-aspartyl-tRNAAsp
The 3 substrates of this enzyme are ATP, L-aspartate, and tRNA(Asp), whereas its 3 products are AMP, diphosphate, and L-aspartyl-tRNA(Asp).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-aspartate:tRNAAsp ligase (AMP-forming). Other names in common use include aspartyl-tRNA synthetase, aspartyl ribonucleic synthetase, aspartyl-transfer RNA synthetase, aspartic acid translase, aspartyl-transfer ribonucleic acid synthetase, and aspartyl ribonucleate synthetase. This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , and .
See also
DARS (gene)
References
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Benzoate%E2%80%94CoA%20ligase | In enzymology, a benzoate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + benzoate + CoA AMP + diphosphate + benzoyl-CoA
The 3 substrates of this enzyme are ATP, benzoate, and CoA, whereas its 3 products are AMP, diphosphate, and benzoyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is benzoate:CoA ligase (AMP-forming). Other names in common use include benzoate-coenzyme A ligase, benzoyl-coenzyme A synthetase, and benzoyl CoA synthetase (AMP forming). This enzyme participates in benzoate degradation via coa ligation.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 6.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Immobilized%20whole%20cell | The immobilized whole cell system is an alternative to enzyme immobilization. Unlike enzyme immobilization, where the enzyme is attached to a solid support (such as calcium alginate or activated PVA or activated PEI), in immobilized whole cell systems, the target cell is immobilized. Such methods may be implemented when the enzymes required are difficult or expensive to extract, an example being intracellular enzymes. Also, if a series of enzymes are required in the reaction; whole cell immobilization may be used for convenience. This is only done on a commercial basis when the need for the product is more justified.
Multiple enzymes may be introduced into the reaction, thus eliminating the need for immobilization of multiple enzymes. Furthermore, intracellular enzymes need not be extracted prior to the reaction; they may be used directly. However, some enzymes may be used for the metabolic needs of the cell, leading to reduced yield of the cell.
References
See also
Immobilized enzyme
Biochemistry methods |
https://en.wikipedia.org/wiki/Biotin%E2%80%94%28acetyl-CoA-carboxylase%29%20ligase | In enzymology, a biotin—[acetyl-CoA-carboxylase] ligase () is an enzyme that catalyzes the chemical reaction
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
The 3 substrates of this enzyme are ATP, biotin, and apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)], whereas its 3 products are AMP, diphosphate, and acetyl-CoA:carbon-dioxide ligase (ADP-forming).
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds.
This enzyme participates in biotin metabolism. This protein may use the morpheein model of allosteric regulation.
Nomenclature
The systematic name of this enzyme class is biotin:apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] ligase (AMP-forming). Other names in common use include:
biotin-[acetyl-CoA carboxylase] synthetase,
biotin-[acetyl coenzyme A carboxylase] synthetase,
acetyl coenzyme A holocarboxylase synthetase,
acetyl CoA holocarboxylase synthetase,
biotin:apocarboxylase ligase,
biotin holoenzyme synthetase,
and HCS.
References
Further reading
EC 6.3.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Biotin%20carboxylase | In enzymology, a biotin carboxylase () is an enzyme that catalyzes the chemical reaction
ATP + biotin-carboxyl-carrier protein + CO2 ADP + phosphate + carboxybiotin-carboxyl-carrier protein
The three substrates of this enzyme are ATP, biotin-carboxyl-carrier protein (BCCP), and CO2, whereas its three products are ADP, phosphate, and carboxybiotin-carboxyl-carrier protein.
The systematic name of this enzyme class is biotin-carboxyl-carrier-protein:carbon-dioxide ligase (ADP-forming). This enzyme is also called biotin carboxylase (component of acetyl CoA carboxylase). This enzyme participates in fatty acid biosynthesis. This enzyme participates in fatty acid biosynthesis by providing one of the catalytic functions of the Acetyl-CoA carboxylase complex. As previously mentioned, after the carboxybiotin product is formed, the carboxyltransferase unit of the complex will transfer the activated carboxy group from BCCP to Acetyl-CoA, forming a malonate analog known as malonyl-CoA. Malonyl-CoA serves as the primary carbon donor in fatty acid biosynthesis, followed by a series of reduction and dehydration reactions to remove the acyl group.
Reaction pathway
Biotin carboxylases are a conserved enzyme present within biotin-dependent carboxylase complexes such as acetyl-CoA carboxylase. How biotin carboxylase functions is, within the relevant carboxylase complex, there is a biotin carboxyl-carrier protein which is covalently linked to biotin via a Lys-residue. Both biotin carboxyl |
https://en.wikipedia.org/wiki/Biotin%E2%80%94CoA%20ligase | In enzymology, a biotin—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + biotin + CoA AMP + diphosphate + biotinyl-CoA
The 3 substrates of this enzyme are ATP, biotin, and CoA, whereas its 3 products are AMP, diphosphate, and biotinyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is biotin:CoA ligase (AMP-forming). Other names in common use include biotinyl-CoA synthetase, biotin CoA synthetase, and biotinyl coenzyme A synthetase. This enzyme participates in biotin metabolism.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Biotin%E2%80%94%28methylcrotonoyl-CoA-carboxylase%29%20ligase | In enzymology, a biotin-[methylcrotonoyl-CoA-carboxylase] ligase () is an enzyme that catalyzes the chemical reaction
ATP + biotin + apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] AMP + diphosphate + [3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]
The 3 substrates of this enzyme are ATP, biotin, and [[apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]]], whereas its 3 products are AMP, diphosphate, and 3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming).
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is biotin:apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] ligase (AMP-forming). Other names in common use include biotin-[methylcrotonoyl-CoA-carboxylase] synthetase, biotin-beta-methylcrotonyl coenzyme A carboxylase synthetase, beta-methylcrotonyl coenzyme A holocarboxylase synthetase, and holocarboxylase-synthetase. This enzyme participates in biotin metabolism.
References
EC 6.3.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Biotin%E2%80%94%28methylmalonyl-CoA-carboxytransferase%29%20ligase | In enzymology, a biotin—[methylmalonyl-CoA-carboxytransferase] ligase () is an enzyme that catalyzes the chemical reaction
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxytransferase] AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxytransferase]
The 3 substrates of this enzyme are ATP, biotin, and [[apo-[methylmalonyl-CoA:pyruvate carboxytransferase]]], whereas its 3 products are AMP, diphosphate, and methylmalonyl-CoA:pyruvate carboxytransferase.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is biotin:apo[methylmalonyl-CoA:pyruvate carboxytransferase] ligase (AMP-forming). This enzyme participates in biotin metabolism.
References
EC 6.3.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Butyrate%E2%80%94CoA%20ligase | Butyrate—CoA ligase, also known as xenobiotic/medium-chain fatty acid-ligase (XM-ligase), is an enzyme () that catalyzes the chemical reaction:
ATP + a carboxylic acid + CoA AMP + diphosphate + an acyl-CoA
The 3 substrates of this enzyme are ATP, carboxylic acid, and CoA, whereas its 3 products are AMP, diphosphate, and acyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. This enzyme participates in the glycine conjugation of xenobiotics and butanoate metabolism.
Nomenclature
The systematic name of this enzyme class is butanoate:CoA ligase (AMP-forming). Other names in common use include:
butyryl-CoA synthetase, fatty acid thiokinase (medium chain),
acyl-activating enzyme, fatty acid elongate,
fatty acid activating enzyme,
fatty acyl coenzyme A synthetase,
medium chain acyl-CoA synthetase,
butyryl-coenzyme A synthetase,
L-(+)-3-hydroxybutyryl CoA ligase,
xenobiotic/medium-chain fatty acid ligase, and
short-chain acyl-CoA synthetase.
Human proteins containing this domain
ACSM1
ACSM2A
ACSM2B
ACSM3
ACSM4
ACSM5
ACSM6
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28carboxyethyl%29arginine%20beta-lactam-synthase | In enzymology, a (carboxyethyl)arginine β-lactam-synthase () is an enzyme that catalyzes the chemical reaction
ATP + L-N-(2-carboxyethyl)arginine AMP + diphosphate + deoxyamidinoproclavaminate
Thus, the two substrates of this enzyme are ATP and L-N2-(2-carboxyethyl)arginine, whereas its 3 products are AMP, diphosphate, and deoxyamidinoproclavaminate.
This enzyme belongs to the family of ligases, specifically the cyclo-ligases, which form carbon-nitrogen bonds. The systematic name of this enzyme class is L-N2-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming). This enzyme is also called L-2-N-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming). This enzyme participates in clavulanic acid biosynthesis.
References
Further reading
EC 6.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Carnosine%20synthase | Carnosine synthase () is an enzyme that catalyzes the chemical reaction
ATP + L-histidine + beta-alanine ADP + phosphate + carnosine
The 3 substrates of this enzyme are ATP, L-histidine, and beta-alanine, whereas its 3 products are ADP (previously thought to form AMP), diphosphate, and carnosine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is 'L-histidine:beta-alanine ligase (AMP-forming)' (incorrect on AMP-forming). Other names in common use include 'carnosine synthetase', 'carnosine-anserine synthetase', 'homocarnosine synthetase', and 'carnosine-homocarnosine synthetase'.
Gene
The gene encoding this enzyme has been identified by Jakub Drozak and coworkers in 2010. The gene encoding the Carnosine synthase is ATPGD1, a member of the “ATP-grasp family” of ligases. Because of its involvement in the formation of carnosine, this gene is now also named 'CARNS1'.
References
EC 6.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Citrate%E2%80%94CoA%20ligase | In enzymology, a citrate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + citrate + CoA ADP + phosphate + (3S)-citryl-CoA
The 3 substrates of this enzyme are ATP, citrate, and CoA, whereas its 3 products are ADP, phosphate, and (3S)-citryl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is citrate:CoA ligase (ADP-forming). Other names in common use include citryl-CoA synthetase, citrate:CoA ligase, and citrate thiokinase. This enzyme participates in citric acid cycle.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28citrate%20%28pro-3S%29-lyase%29%20ligase | In enzymology, a [citrate (pro-3S)-lyase] ligase () is an enzyme that catalyzes the chemical reaction
ATP + acetate + citrate (pro-3S)-lyase(thiol form) AMP + diphosphate + citrate (pro-3S)-lyase(acetyl form)
The 3 substrates of this enzyme are ATP, acetate, and citrate (pro-3S)-lyase(thiol form), whereas its 3 products are AMP, diphosphate, and citrate (pro-3S)-lyase(acetyl form).
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is acetate:citrate (pro-3S)-lyase(thiol-form) ligase (AMP-forming). Other names in common use include citrate lyase ligase, citrate lyase synthetase, acetate: SH-acyl-carrier-protein enzyme ligase (AMP), acetate:HS-citrate lyase ligase, and acetate:citrate-(pro-3S)-lyase(thiol-form) ligase (AMP-forming). This enzyme participates in two-component system - general.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cobalt%20chelatase | Cobalt chelatase () is an enzyme that catalyzes the chemical reaction
ATP + hydrogenobyrinic acid a,c-diamide + Co2+ + H2O ADP + phosphate + cob(II)yrinic acid a,c-diamide + H+
The four substrates of this enzyme are ATP, hydrogenobyrinic acid a,c-diamide, Co2+, and H2O; its four products are ADP, phosphate, cob(II)yrinic acid a,c-diamide, and H+.
The aerobic cobalt chelatase (aerobic cobalamin biosynthesis pathway) consists of three subunits, CobT, CobN () and CobS ().
The macrocycle of vitamin B12 can be complexed with metal via the ATP-dependent reactions in the aerobic pathway (e.g., in Pseudomonas denitrificans) or via ATP-independent reactions of sirohydrochlorin in the anaerobic pathway (e.g., in Salmonella typhimurium). The corresponding cobalt chelatases are not homologous. However, aerobic cobalt chelatase subunits CobN and CobS are homologous to Mg-chelatase subunits BchH and BchI, respectively. CobT, too, has been found to be remotely related to the third subunit of Mg-chelatase, BchD (involved in bacteriochlorophyll synthesis, e.g., in Rhodobacter capsulatus).
This enzyme belongs to the family of ligases, specifically those forming nitrogen-D-metal bonds in coordination complexes. The systematic name of this enzyme class is hydrogenobyrinic-acid-a,c-diamide:cobalt cobalt-ligase (ADP-forming). Other names in common use include hydrogenobyrinic acid a,c-diamide cobaltochelatase, CobNST, and CobNCobST. This enzyme is part of the biosynthetic pathway to cobalam |
https://en.wikipedia.org/wiki/Cysteine%E2%80%94tRNA%20ligase | In enzymology, a cysteine—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-cysteine + tRNACys AMP + diphosphate + L-cysteinyl-tRNACys
The 3 substrates of this enzyme are ATP, L-cysteine, and tRNA(Cys), whereas its 3 products are AMP, diphosphate, and L-cysteinyl-tRNA(Cys).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-cysteine:tRNACys ligase (AMP-forming). Other names in common use include cysteinyl-tRNA synthetase, cysteinyl-transferRNA synthetase, cysteinyl-transfer ribonucleate synthetase, and cysteine translase. This enzyme participates in cysteine metabolism and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/D-alanine%E2%80%94alanyl-poly%28glycerolphosphate%29%20ligase | In enzymology, a D-alanine—alanyl-poly(glycerolphosphate) ligase () is an enzyme that catalyzes the chemical reaction
ATP + D-alanine + alanyl-poly(glycerolphosphate) ADP + phosphate + D-alanyl-alanyl-poly(glycerolphosphate)
The 3 substrates of this enzyme are ATP, D-alanine, and alanyl-poly(glycerolphosphate), whereas its 3 products are ADP, phosphate, and D-alanyl-alanyl-poly(glycerolphosphate).
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is D-alanine:alanyl-poly(glycerolphosphate) ligase (ADP-forming). Other names in common use include D-alanyl-alanyl-poly(glycerolphosphate) synthetase, D-alanine:membrane-acceptor ligase, D-alanylalanylpoly(phosphoglycerol) synthetase, D-alanyl-poly(phosphoglycerol) synthetase, and D-alanine-membrane acceptor-ligase. This enzyme participates in d-alanine metabolism.
References
EC 6.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-alanine%E2%80%94D-alanine%20ligase | In enzymology, a D-alanine—D-alanine ligase () is an enzyme that catalyzes the chemical reaction
ATP + 2 D-alanine ADP + phosphate + D-alanyl-D-alanine
Thus, the two substrates of this enzyme are ATP and D-alanine, whereas its 3 products are ADP, phosphate, and D-alanyl-D-alanine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is D-alanine:D-alanine ligase (ADP-forming). Other names in common use include alanine:alanine ligase (ADP-forming), and alanylalanine synthetase. This enzyme participates in d-alanine metabolism and peptidoglycan biosynthesis. Phosphinate and D-cycloserine are known to inhibit this enzyme.
The N-terminal region of the D-alanine—D-alanine ligase is thought to be involved in substrate binding, while the C-terminus is thought to be a catalytic domain.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
References
Further reading
EC 6.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/D-alanine%E2%80%94poly%28phosphoribitol%29%20ligase | In enzymology, a D-alanine—poly(phosphoribitol) ligase () is an enzyme that catalyzes the chemical reaction
ATP + D-alanine + poly(ribitol phosphate) AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate)
The 3 substrates of this enzyme are ATP, D-alanine, and poly(ribitol phosphate), whereas its 3 products are AMP, diphosphate, and O-D-alanyl-poly(ribitol phosphate).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is D-alanine:poly(phosphoribitol) ligase (AMP-forming). Other names in common use include D-alanyl-poly(phosphoribitol) synthetase, D-alanine: membrane acceptor ligase, D-alanine-D-alanyl carrier protein ligase, D-alanine-membrane acceptor ligase, and D-alanine-activating enzyme. This enzyme participates in d-alanine metabolism.
References
EC 6.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-aspartate%20ligase | In enzymology, a D-aspartate ligase () is an enzyme that catalyzes the chemical reaction
ATP + D-aspartate + [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D- Ala)]n [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L- Lys-D-Ala-D-Ala)]n + ADP + phosphate
The 4 substrates of this enzyme are ATP, D-aspartate, [[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-]], and [[Ala)]n]], whereas its 4 products are [[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-]], [[Lys-D-Ala-D-Ala)]n]], ADP, and phosphate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The systematic name of this enzyme class is D-aspartate:[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D -Ala-D-Ala)]n ligase (ADP-forming). Other names in common use include Aslfm, UDP-MurNAc-pentapeptide:D-aspartate ligase, and D-aspartic acid-activating enzyme.
References
EC 6.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dethiobiotin%20synthase | In enzymology, a dethiobiotin synthase () is an enzyme that catalyzes the chemical reaction
ATP + 7,8-diaminononanoate + CO2 ADP + phosphate + dethiobiotin
The 3 substrates of this enzyme are ATP, 7,8-diaminononanoate, and CO2, whereas its 3 products are ADP, phosphate, and dethiobiotin.
This enzyme belongs to the family of ligases, specifically the cyclo-ligases, which form carbon-nitrogen bonds. The systematic name of this enzyme class is 7,8-diaminononanoate:carbon-dioxide cyclo-ligase (ADP-forming). This enzyme is also called desthiobiotin synthase. This enzyme participates in biotin metabolism.
Structural studies
As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , and .
References
EC 6.3.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Dicarboxylate%E2%80%94CoA%20ligase | In enzymology, a dicarboxylate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + an alphaomega-dicarboxylic acid + CoA AMP + diphosphate + an omega-carboxyacyl-CoA
The 3 substrates of this enzyme are ATP, alphaomega-dicarboxylic acid, and CoA, whereas its 3 products are AMP, diphosphate, and omega-carboxyacyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is omega-dicarboxylate:CoA ligase (AMP-forming). Other names in common use include carboxylyl-CoA synthetase, and dicarboxylyl-CoA synthetase.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydrofolate%20synthase | In enzymology, a dihydrofolate synthase () is an enzyme that catalyzes the chemical reaction
ATP + 7,8-dihydropteroate + L-glutamate ADP + phosphate + 7,8-dihydropteroylglutamate
The 3 substrates of this enzyme are ATP, 7,8-dihydropteroate, and L-glutamate, whereas its 3 products are ADP, phosphate, and 7,8-dihydropteroylglutamate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is 7,8-dihydropteroate:L-glutamate ligase (ADP-forming). Other names in common use include dihydrofolate synthetase, 7,8-dihydrofolate synthetase, H2-folate synthetase, 7,8-dihydropteroate:L-glutamate ligase (ADP), dihydrofolate synthetase-folylpolyglutamate synthetase, folylpoly-(gamma-glutamate) synthetase-dihydrofolate synthase, FHFS, FHFS/FPGS, dihydropteroate:L-glutamate ligase (ADP-forming), and DHFS. This enzyme participates in folate biosynthesis.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 6.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Diphthine%E2%80%94ammonia%20ligase | In enzymology, a diphthine—ammonia ligase (, diphthamide synthase, diphthamide synthetase) is an enzyme that catalyzes the chemical reaction
ATP + diphthine + NH3 ADP + phosphate + diphthamide
The 3 substrates of this enzyme are ATP, diphthine, and NH3, whereas its 3 products are ADP, phosphate, and diphthamide.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is diphthine:ammonia ligase (ADP-forming). Other names in common use include diphthamide synthase, and diphthamide synthetase.
References
EC 6.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Formate%E2%80%94dihydrofolate%20ligase | In enzymology, a formate—dihydrofolate ligase () is an enzyme that catalyzes the chemical reaction
ATP + formate + dihydrofolate ADP + phosphate + 10-formyldihydrofolate
The 3 substrates of this enzyme are ATP, formate, and dihydrofolate, whereas its 3 products are ADP, phosphate, and 10-formyldihydrofolate.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is formate:dihydrofolate ligase (ADP-forming).
References
Further reading
EC 6.3.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Formate%E2%80%93tetrahydrofolate%20ligase | In enzymology, a formate—tetrahydrofolate ligase () is an enzyme that catalyzes the chemical reaction
ATP + formate + tetrahydrofolate ADP + phosphate + 10-formyltetrahydrofolate
The 3 substrates of this enzyme are ATP, formate, and tetrahydrofolate, whereas its 3 products are ADP, phosphate, and 10-formyltetrahydrofolate.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. This enzyme participates in glyoxylate and dicarboxylate metabolism and one carbon pool by folate.
In eukaryotes the FTHFS activity is expressed by a multifunctional enzyme, C-1-tetrahydrofolate synthase (C1-THF synthase), which also catalyses the dehydrogenase and cyclohydrolase activities. Two forms of C1-THF syntheses are known, one is located in the mitochondrial matrix, while the second one is cytoplasmic. In both forms the FTHFS domain consists of about 600 amino acid residues and is located in the C-terminal section of C1-THF synthase. In prokaryotes FTHFS activity is expressed by a monofunctional homotetrameric enzyme of about 560 amino acid residues.
Nomenclature
The systematic name of this enzyme class is formate:tetrahydrofolate ligase (ADP-forming). Other names in common use include:
formyltetrahydrofolate synthetase,
10-formyltetrahydrofolate synthetase,
tetrahydrofolic formylase, and
tetrahydrofolate formylase.
Examples
Human genes encoding formate-tetrahydrofolate ligases include:
MTHFD1 – cytoplasmic
MTHFD1L – mitochond |
https://en.wikipedia.org/wiki/Gamma-glutamylhistamine%20synthase | In enzymology, a γ-glutamylhistamine synthase () is an enzyme that catalyzes the chemical reaction
ATP + L-glutamate + histamine products of ATP breakdown + Nα-γ-L-glutamylhistamine
The 3 substrates of this enzyme are ATP, L-glutamate, and histamine, whereas its two products are products of ATP breakdown and Nalpha-gamma-L-glutamylhistamine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is L-glutamate:histamine ligase. Other names in common use include gamma-glutaminylhistamine synthetase, and gamma-GHA synthetase.
References
EC 6.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Geranoyl-CoA%20carboxylase | In enzymology, a geranoyl-CoA carboxylase () is an enzyme that catalyzes the chemical reaction
ATP + geranoyl-CoA + HCO3- ADP + phosphate + 3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA
The 3 substrates of this enzyme are ATP, geranoyl-CoA, and HCO3-, whereas its 3 products are ADP, phosphate, and 3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon–carbon bonds. The systematic name of this enzyme class is geranoyl-CoA:carbon-dioxide ligase (ADP-forming). Other names in common use include geranoyl coenzyme A carboxylase, and geranyl-CoA carboxylase. It employs one cofactor, biotin.
References
EC 6.4.1
Biotin enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutamate%E2%80%93cysteine%20ligase | Glutamate–cysteine ligase (GCL) ), previously known as γ-glutamylcysteine synthetase (GCS), is the first enzyme of the cellular glutathione (GSH) biosynthetic pathway that catalyzes the chemical reaction:
L-glutamate + L-cysteine + ATP γ-glutamyl cysteine + ADP + Pi
GSH, and by extension GCL, is critical to cell survival. Nearly every eukaryotic cell, from plants to yeast to humans, expresses a form of the GCL protein for the purpose of synthesizing GSH. To further highlight the critical nature of this enzyme, genetic knockdown of GCL results in embryonic lethality. Furthermore, dysregulation of GCL enzymatic function and activity is known to be involved in the vast majority of human diseases, such as diabetes, Parkinson's disease, Alzheimer's disease, COPD, HIV/AIDS, and cancer. This typically involves impaired function leading to decreased GSH biosynthesis, reduced cellular antioxidant capacity, and the induction of oxidative stress. However, in cancer, GCL expression and activity is enhanced, which serves to both support the high level of cell proliferation and confer resistance to many chemotherapeutic agents.
Function
Glutamate cysteine ligase (GCL) catalyzes the first and rate-limiting step in the production of the cellular antioxidant glutathione (GSH), involving the ATP-dependent condensation of cysteine and glutamate to form the dipeptide gamma-glutamylcysteine (γ-GC). This peptide coupling is unique in that it occurs between the amino moiety of the cysteine and |
https://en.wikipedia.org/wiki/Glutamate%E2%80%94ethylamine%20ligase | In enzymology, a glutamate—ethylamine ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-glutamate + ethylamine ADP + phosphate + N5-ethyl-L-glutamine
The 3 substrates of this enzyme are ATP, L-glutamate, and ethylamine, whereas its 3 products are ADP, phosphate, and N5-ethyl-L-glutamine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The systematic name of this enzyme class is L-glutamate:ethylamine ligase (ADP-forming). Other names in common use include N5-ethyl-L-glutamine synthetase, theanine synthetase, and N5-ethylglutamine synthetase.
References
EC 6.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutamate%E2%80%94methylamine%20ligase | In enzymology, a glutamate—methylamine ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-glutamate + methylamine ADP + phosphate + N5-methyl-L-glutamine
The 3 substrates of this enzyme are ATP, L-glutamate, and methylamine, whereas its 3 products are ADP, phosphate, and N5-methyl-L-glutamine.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is L-glutamate:methylamine ligase (ADP-forming). This enzyme is also called gamma-glutamylmethylamide synthetase.
References
EC 6.3.4
Enzymes of unknown structure |
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