| EC |
2.2.1.5 |
| Accepted name: |
2-hydroxy-3-oxoadipate synthase |
| Reaction: |
2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO2 |
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For diagram of reaction mechanism, click here |
| Glossary: |
thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium |
| Other name(s): |
2-hydroxy-3-oxoadipate glyoxylate-lyase (carboxylating); α-ketoglutaric-glyoxylic carboligase; oxoglutarate: glyoxylate carboligase |
| Systematic name: |
2-oxoglutarate:glyoxylate succinaldehydetransferase (decarboxylating) |
| Comments: |
The bacterial enzyme requires thiamine diphosphate. The product decarboxylates to 5-hydroxy-4-oxopentanoate. The enzyme can decarboxylate 2-oxoglutarate. Acetaldehyde can replace glyoxylate. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-72-2 |
| References: |
| 1. |
Schlossberg, M.A., Bloom, R.J., Richert, D.A. and Westerfield, W.W. Carboligase activity of α-ketoglutarate dehydrogenase. Biochemistry 9 (1970) 1148–1153. [PMID: 5418712] |
| 2. |
Schlossberg, M.A., Richert, D.A., Bloom, R.J. and Westerfield, W.W. Isolation and identification of 5-hydroxy-4-ketovaleric acid as a product of α-ketoglutarate: glyoxylate carboligase. Biochemistry 7 (1968) 333–337. [PMID: 4320439] |
| 3. |
Stewart, P.R. and Quayle, J.R. The synergistic decarboxylation of glyoxalate and 2-oxoglutarate by an enzyme system from pig-liver mitochondria. Biochem. J. 102 (1967) 885–897. [PMID: 16742506] |
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| [EC 2.2.1.5 created 1972 as EC 4.1.3.15, transferred 2002 to EC 2.2.1.5] |
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