ID: | 4.1.3.39 | ||
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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: |
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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; |
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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 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 |
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 |
Title | Authors | Date | PubMed ID |
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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 E | 1997 Apr | 9098055 |
Characterization of an aldolase-dehydrogenase complex from the cholesterol degradation pathway of Mycobacterium tuberculosis. | Carere J, McKenna SE, Kimber MS, Seah SY | 2013 May 21 | 23614353 |
Rational design of stereoselectivity in the class II pyruvate aldolase BphI. | Baker P, Seah SY | 2012 Jan 11 | 22081904 |