EC |
2.6.1.23 |
Accepted name: |
4-hydroxyglutamate transaminase |
Reaction: |
erythro-4-hydroxy-L-glutamate + 2-oxoglutarate = (4R)-4-hydroxy-2-oxoglutarate + L-glutamate |
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For diagram of reaction, click here and for mechanism, click here |
Glossary: |
erythro-4-hydroxy-L-glutamate = (2S,4R)-2-amino-4-hydroxypentanedioate |
Other name(s): |
4-hydroxyglutamate aminotransferase; 4-hydroxy-L-glutamate:2-oxoglutarate aminotransferase |
Systematic name: |
erythro-4-hydroxy-L-glutamate:2-oxoglutarate aminotransferase |
Comments: |
The enzyme participates in a degradation pathway of trans-4-hydroxy-L-proline, a compound that contributes to the stability of the collagen triple helix. Oxaloacetate can replace 2-oxoglutarate. This enzyme may be identical with EC 2.6.1.1 aspartate transaminase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-86-4 |
References: |
1. |
Goldstone, A. and Adams, E. Metabolism of γ-hydroxyglutamic acid. I. Conversion to α-hydroxy-γ-ketoglutarate by purified glutamic-aspartic transaminase to rat liver. J. Biol. Chem. 237 (1962) 3476–3485. [PMID: 13948827] |
2. |
Kuratomi, K., Fukunaga, K. and Kobayashi, Y. The metabolism of γ-hydroxyglutamate in rat liver. II. A transaminase concerned in γ-hydroxyglutamate metabolism. Biochim. Biophys. Acta 78 (1963) 629–636. [DOI] [PMID: 14089443] |
3. |
Maitra U, Deekker E Purification of rat-liver γ-hydroxyglutamate transaminase and its probable identity with glutamate-aspartate transaminase. Biochim. Biophys. Acta 81 (1964) 517–532. [PMID: 14170323] |
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[EC 2.6.1.23 created 1972, modified 1982, modified 2020] |
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