| EC |
2.6.1.62 |
| Accepted name: |
adenosylmethionine—8-amino-7-oxononanoate transaminase |
| Reaction: |
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate |
| Other name(s): |
7,8-diaminonanoate transaminase; 7,8-diaminononanoate transaminase; DAPA transaminase (ambiguous); 7,8-diaminopelargonic acid aminotransferase; DAPA aminotransferase (ambiguous); 7-keto-8-aminopelargonic acid; diaminopelargonate synthase; 7-keto-8-aminopelargonic acid aminotransferase |
| Systematic name: |
S-adenosyl-L-methionine:8-amino-7-oxononanoate aminotransferase |
| Comments: |
A pyridoxal 5′-phosphate enzyme. S-adenosylhomocysteine can also act as donor. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37259-71-5 |
| References: |
| 1. |
Izumi, Y., Sato, K., Tani, Y. and Ogata, K. Purification of 7-keto-8-aminopelargonic acid-7,8-diaminopelargonic acid aminotransferase, an enzyme involved in biotin synthesis, from Brevibacterium divaricatum. Agric. Biol. Chem. 37 (1973) 2683–2684. |
| 2. |
Izumi, Y., Sato, K., Tani, Y. and Ogata, K. 7,8-Diaminopelargonic acid aminotransferase, an enzyme involved in biotin synthesis by microorganisms. Agric. Biol. Chem. 39 (1975) 175–181. |
| 3. |
Stoner, G.L. and Eisenberg, M.A. Purification and properties of 7,8-diaminopelargonic acid aminotransferase. An enzyme in the biotin biosynthetic pathway. J. Biol. Chem. 250 (1973) 4029–4036. [PMID: 1092681] |
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| [EC 2.6.1.62 created 1983] |
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