Literature summary for 1.1.99.36 extracted from

Norin, A.; Piersma, S.R.; Duine, J.A.; Jornvall, H.
Nicotinoprotein (NAD+ -containing) alcohol dehydrogenase: structural relationships and functional interpretations (2003), Cell. Mol. Life Sci., 60, 999-1006.

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Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
38970	-	x * 38970, calculated	Amycolatopsis methanolica

Organism

Organism	UniProt	Comment	Textmining
Amycolatopsis methanolica	P80175	-	-

Subunits

Subunits	Comment	Organism
?	x * 38970, calculated	Amycolatopsis methanolica

Cofactor

Cofactor	Comment	Organism	Structure
NADH	comparison of NADH binding in nicotinoprotein alcohol dehydrogenase and in the conventional alcohol dehydrogenase. Considerable parts of the coenzyme binding in the conventional enzyme are also present in the nicotinoprotein. Alterations in two loop structures affect coenzyme binding and appear to tighten it in the nicotinoprotein model. The positions of residues in a sphere of 3.8 A around the coenzyme template of the nicotinoprotein model reveal the presence of coenzyme interactions additional to those in the conventional structure	Amycolatopsis methanolica

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Release 2023.1 (January 2023)