Methanol dehydrogenase

Methanol dehydrogenase
methanol dehydrogenase
Identifiers
EC number 1.1.1.244
CAS number 74506-37-9
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

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(EC 1.1.1.244) was first reported in a Gram-positive methylotroph[1] 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.[2]

References

  1. ^ Arfman N, Watling EM, Clement W, van Oosterwijk RJ, de Vries GE, Harder W, Attwood MM, Dijkhuizen L (1989). "Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD-dependent methanol dehydrogenase as a key enzyme". Arch. Microbiol. 152 (3): 280–8. doi:10.1007/BF00409664. PMID 2673121. 
  2. ^ Anthony, C. (1982). The Biochemistry of Methylotrophs. Boston: Academic Press. pp. 167–182. ISBN 0-12-058820-X. 

Further reading

  • Harder W, Attwood MM, Dijkhuizen L (1989). "Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD-dependent methanol dehydrogenase as a key enzyme". Arch. Microbiol. 152 (3): 280–8. doi:10.1007/BF00409664. PMID 2673121. 


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