EC number:4.1.3.43
| ID: | 4.1.3.43 |
|---|---|
| Description: | 4-hydroxy-2-oxohexanoate aldolase. |
| Cath: | 1.10.8.60; 3.20.20.70; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 4.1.3.43 |
| BRENDA Enzyme Link: | BRENDA 4.1.3.43 |
| KEGG Enzyme Link: | KEGG4.1.3.43 |
| BioCyc Enzyme Link: | BioCyc 4.1.3.43 |
| ExPASy Enzyme Link: | ExPASy4.1.3.43 |
| EC2PDB Enzyme Link: | EC2PDB 4.1.3.43 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.1.3.43 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.1.3.43 |
| IntEnz Enzyme Link: | IntEnz 4.1.3.43 |
| MEDLINE Enzyme Link: | MEDLINE 4.1.3.43 |
| RHEA:36003 | (S)-4-hydroxy-2-oxohexanoate = 1-propanal + 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
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Characterization of an aldolase-dehydrogenase complex that exhibits substrate channeling in the polychlorinated biphenyls degradation pathway. | Baker P, Pan D, Carere J, Rossi A, Wang W, Seah SY | 2009 Jul 14 | 19476337 |
| 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 |