EC 1.5.1.17 - Alanopine dehydrogenase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 1.5.1.17

Names

Accepted name:
alanopine dehydrogenase
Other names:
meso-N-(1-carboxyethyl)-alanine:NAD+ oxidoreductase
ADH
ALPDH
alanopine: NAD oxidoreductase
alanopine:NAD oxidoreductase
alanopine[meso-N-(1-carboxyethyl)-alanine]dehydrogenase
Systematic name:
2,2'-iminodipropanoate:NAD+ oxidoreductase (L-alanine-forming)

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047636
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: 297-298 (1981).
  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: 110-114 (1980). [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: 615-621 (1981). [PMID: 7238503]

[EC 1.5.1.17 created 1983, modified 1986]