EC |
1.5.1.17 |
Accepted name: |
alanopine dehydrogenase |
Reaction: |
2,2′-iminodipropanoate + NAD+ + H2O = L-alanine + pyruvate + NADH + H+ |
Other name(s): |
ALPDH; alanopine[meso-N-(1-carboxyethyl)-alanine]dehydrogenase; meso-N-(1-carboxyethyl)-alanine:NAD+ oxidoreductase; alanopine: NAD+ oxidoreductase; ADH (ambiguous); alanopine:NAD+ oxidoreductase |
Systematic name: |
2,2′-iminodipropanoate:NAD+ oxidoreductase (L-alanine-forming) |
Comments: |
In the reverse reaction, L-alanine can be replaced by L-cysteine, L-serine or L-threonine; glycine acts very slowly (cf. EC 1.5.1.22 strombine dehydrogenase). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 71343-07-2 |
References: |
1. |
Dando, P.R. Strombine [N-(carboxymethyl)-D-alanine] dehydrogenase and alanopine [meso-N-(1-carboxyethyl)-alanine dehydrogenase from the mussel Mytilus edulis L. Biochem. Soc. Trans. 9 (1981) 297–298. |
2. |
Fields, J.H.A., Eng, A.K., Ramsden, W.D., Hochachka, P.W. and Weinstein, B. Alanopine and strombine are novel imino acids produced by a dehydrogenase found in the adductor muscle of the oyster, Crassostrea gigas. Arch. Biochem. Biophys. 201 (1980) 110–114. [DOI] [PMID: 6156653] |
3. |
Fields, J.H.A. and Hochachka, P.W. Purification and properties of alanopine dehydrogenase from the adductor muscle of the oyster, Crassostrea gigas (Mollusca, Bivalvia). Eur. J. Biochem. 114 (1981) 615–621. [DOI] [PMID: 7238503] |
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[EC 1.5.1.17 created 1983, modified 1986] |
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