Methanol dehydrogenase
| methanol dehydrogenase | |||||||||
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| 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 | ||||||||
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In enzymology, a methanol dehydrogenase is an enzyme that catalyses the chemical reaction:
- methanol
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+ 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
- ↑ 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.
- ↑ 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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