Enzyme

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EC Tree
     2. Transferases
        2.3 Acyltransferases
            2.3.1 Transferring groups other than aminoacyl groups
ID:2.3.1.263
Description:2-amino-4-oxopentanoate thiolase.
Alternative Name: AKP thiolase.
2-amino-4-ketopentanoate thiolase.

3D structure

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References

External Links

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:

2.3.1.263;

Phylogenetic Tree:

2.3.1.263;

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

References

TitleAuthorsDatePubMed 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 HA1974 Jul 24407783
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 M2009 May19251850