Alanopine dehydrogenase

Alanopine dehydrogenase (EC 1.5.1.17) is an enzyme that catalyzes the chemical reaction

2,2'-iminodipropanoate + NAD⁺ + H₂O ${\displaystyle \rightleftharpoons }$ L-alanine + pyruvate + NADH + H⁺

The 2 substrates of this enzyme are 2,2'-iminodipropanoate, and nicotinamide adenine dinucleotide+. water is excluded since water is 55M and does not change. Its 4 products are L-alanine, pyruvate, nicotinamide adenine dinucleotide, and hydrogen ion.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2,2'-iminodipropanoate:NAD+ oxidoreductase (L-alanine-forming). Other names in common use include ALPDH, alanopine[meso-N-(1-carboxyethyl)-alanine]dehydrogenase, meso-N-(1-carboxyethyl)-alanine:NAD+ oxidoreductase, alanopine: NAD+ oxidoreductase, ADH, and alanopine:NAD+ oxidoreductase.

References

• Dando PR (1981). "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.
• Fields JH, Eng AK, Ramsden WD, Hochachka PW, Weinstein B (1980). "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 (1): 110–4. doi:10.1016/0003-9861(80)90493-2. PMID 6156653.
• Fields JH, Hochachka PW (1981). "Purification and properties of alanopine dehydrogenase from the adductor muscle of the oyster, Crassostrea gigas (Mollusca, Bivalvia)". Eur. J. Biochem. 114 (3): 615–21. doi:10.1111/j.1432-1033.1981.tb05188.x. PMID 7238503.

This page was last edited on 26 August 2023, at 13:01