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Methanol dehydrogenase : ウィキペディア英語版
Methanol dehydrogenase

In enzymology, a methanol dehydrogenase is an enzyme that catalyses the chemical reaction:
:methanol \rightleftharpoons formaldehyde + 2 electrons + 2H+
How the electrons are captured and transported depends upon the kind of methanol dehydrogenase and there are two main types. A common electron acceptor in biological systems is nicotinamide adenine dinucleotide (NAD+) and some enzymes use a related molecule called nicotinamide adenine dinucleotide phosphate (NADP+). An NAD+-dependent methanol dehydrogenase() was first reported in a Gram-positive methylotroph and is an enzyme that catalyzes the chemical reaction
:methanol + NAD+ \rightleftharpoons formaldehyde + NADH + H+
Thus, the two substrates of this enzyme are methanol and NAD+, whereas its 3 products are formaldehyde, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is methanol:NAD+ oxidoreductase. This enzyme participates in methane metabolism.
Prior to the discovery of this enzyme, methanol oxidation in Gram-negative bacteria had been shown to be by way of an (NAD+) independent alcohol dehydrogenase found originally in ''Pseudomonas'' M27. This enzyme (EC. 1.1.99.8) contains a prosthetic group called Pyrrolo Quinoline Quinone (PQQ) that accepts the electrons generated from methanol oxidation and passes these electrons to cytochrome c.
==References==


抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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