KEGG   ENZYME: 1.5.1.17Help
Entry
EC 1.5.1.17                 Enzyme                                 

Name
alanopine dehydrogenase;
ALPDH ;
alanopine[meso-N-(1-carboxyethyl)-alanine]dehydrogenase;
meso-N-(1-carboxyethyl)-alanine:NAD+ oxidoreductase;
alanopine: NAD+ oxidoreductase;
ADH;
alanopine:NAD+ oxidoreductase
Class
Oxidoreductases;
Acting on the CH-NH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
2,2'-iminodipropanoate:NAD+ oxidoreductase (L-alanine-forming)
Reaction(IUBMB)
2,2'-iminodipropanoate + NAD+ + H2O = L-alanine + pyruvate + NADH + H+ [RN:R00398]
Reaction(KEGG)
Substrate
2,2'-iminodipropanoate [CPD:C03210];
NAD+ [CPD:C00003];
H2O [CPD:C00001]
Product
L-alanine [CPD:C00041];
pyruvate [CPD:C00022];
NADH [CPD:C00004];
H+ [CPD:C00080]
Comment
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).
History
EC 1.5.1.17 created 1983, modified 1986
Reference
1
  Authors
Dando, P.R.
  Title
Strombine [N-(carboxymethyl)-D-alanine] dehydrogenase and alanopine [meso-N-(1-carboxyethyl)-alanine dehydrogenase from the mussel Mytilus edulis L.
  Journal
Biochem Soc Trans 9:297-298 (1981)
Reference
2  [PMID:6156653]
  Authors
Fields JH, Eng AK, Ramsden WD, Hochachka PW, Weinstein B.
  Title
Alanopine and strombine are novel imino acids produced by a dehydrogenase found in the adductor muscle of the oyster, Crassostrea gigas.
  Journal
Arch Biochem Biophys 201:110-4 (1980)
DOI:10.1016/0003-9861(80)90493-2
Reference
3  [PMID:7238503]
  Authors
Fields JH, Hochachka PW.
  Title
Purification and properties of alanopine dehydrogenase from the adductor muscle of the oyster, Crassostrea gigas (Mollusca, Bivalvia).
  Journal
Eur J Biochem 114:615-21 (1981)
DOI:10.1111/j.1432-1033.1981.tb05188.x
Other DBs
ExplorEnz - The Enzyme Database: 1.5.1.17
IUBMB Enzyme Nomenclature: 1.5.1.17
ExPASy - ENZYME nomenclature database: 1.5.1.17
BRENDA, the Enzyme Database: 1.5.1.17
CAS: 71343-07-2

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