Enzyme

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     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.3 Oxo-acid-lyases
ID:4.1.3.39
Description:4-hydroxy-2-oxovalerate aldolase.
Alternative Name: HOA.
4-hydroxy-2-oxovalerate pyruvate-lyase.
4-hydroxy-2-oxopentanoate pyruvate-lyase.
4-hydroxy-2-ketovalerate aldolase.
Prosite: PDOC50991;
PDB:
PDBScop
Cath: 1.10.8.60; 3.20.20.70; 3.30.360.10; 3.40.50.720; 3.40.605.10; 3.40.309.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.3.39
BRENDA Enzyme Link: BRENDA 4.1.3.39
KEGG Enzyme Link: KEGG4.1.3.39
BioCyc Enzyme Link: BioCyc 4.1.3.39
ExPASy Enzyme Link: ExPASy4.1.3.39
EC2PDB Enzyme Link: EC2PDB 4.1.3.39
ExplorEnz Enzyme Link: ExplorEnz 4.1.3.39
PRIAM enzyme-specific profiles Link: PRIAM 4.1.3.39
IntEnz Enzyme Link: IntEnz 4.1.3.39
MEDLINE Enzyme Link: MEDLINE 4.1.3.39
MSA:

4.1.3.39;

Phylogenetic Tree:

4.1.3.39;

Uniprot:
M-CSA:
RHEA:22624 (S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
RULE(radius=1) [*:1]-[CH2;+0:2]-[CH;+0:3](-[*:4])-[OH;+0:5]>>[*:1]-[CH3;+0:2].[*:4]-[CH;+0:3]=[O;H0;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12.Ferrández A, Garciá JL, Díaz E1997 Apr9098055
Characterization of an aldolase-dehydrogenase complex from the cholesterol degradation pathway of Mycobacterium tuberculosis.Carere J, McKenna SE, Kimber MS, Seah SY2013 May 2123614353
Rational design of stereoselectivity in the class II pyruvate aldolase BphI.Baker P, Seah SY2012 Jan 1122081904