EC Tree |
2. Transferases |
2.3 Acyltransferases |
2.3.1 Transferring groups other than aminoacyl groups |
ID: | 2.3.1.263 |
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Description: | 2-amino-4-oxopentanoate thiolase. |
Alternative Name: |
AKP thiolase. 2-amino-4-ketopentanoate thiolase. |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 2.3.1.263 |
BRENDA Enzyme Link: | BRENDA 2.3.1.263 |
KEGG Enzyme Link: | KEGG2.3.1.263 |
BioCyc Enzyme Link: | BioCyc 2.3.1.263 |
ExPASy Enzyme Link: | ExPASy2.3.1.263 |
EC2PDB Enzyme Link: | EC2PDB 2.3.1.263 |
ExplorEnz Enzyme Link: | ExplorEnz 2.3.1.263 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.3.1.263 |
IntEnz Enzyme Link: | IntEnz 2.3.1.263 |
MEDLINE Enzyme Link: | MEDLINE 2.3.1.263 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:51436 | acetyl-CoA + D-alanine = (2R)-2-amino-4-oxopentanoate + CoA |
RULE(radius=1) | [*:1]-[CH3;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[S;H0;+0:6]-[*:7]>>[*:7]-[SH;+0:6].[*:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:2]-[*:1] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Ornithine degradation in Clostridium sticklandii; pyridoxal phosphate and coenzyme A dependent thiolytic cleavage of 2-amino-4-ketopentanoate to alanine and acetyl coenzyme A. | Jeng IM, Somack R, Barker HA | 1974 Jul 2 | 4407783 |
A conserved gene cluster rules anaerobic oxidative degradation of L-ornithine. | Fonknechten N, Perret A, Perchat N, Tricot S, Lechaplais C, Vallenet D, Vergne C, Zaparucha A, Le Paslier D, Weissenbach J, Salanoubat M | 2009 May | 19251850 |