Methylamine dehydrogenase (amicyanin)
| Methylamine dehydrogenase (amicyanin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.4.9.1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Methylamine dehydrogenase (amicyanin) (EC 1.4.9.1, amine dehydrogenase, primary-amine dehydrogenase) is an enzyme with systematic name methylamine:amicyanin oxidoreductase (deaminating).[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- methylamine + H2O + amicyanin formaldehyde + ammonia + reduced amicyanin
This enzyme contains tryptophan tryptophylquinone (TTQ) cofactor.
References
- ↑ De Beer, R.; Duine, J.A.; Frank, J.; Jr.; Large, P.J. (1980). "The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1: evidence for a quinone structure". Biochim. Biophys. Acta. 622 (2): 370–374. doi:10.1016/0005-2795(80)90050-1. PMID 6246962.
- ↑ Eady, R.R.; Large, P.J. (1968). "Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine". Biochem. J. 106 (1): 245–255. PMC 1198491
. PMID 4388687. - ↑ Eady, R.R.; Large, P.J. (1971). "Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM1". Biochem. J. 123 (5): 757–771. PMC 1177077. PMID 5124384.
- ↑ Cavalieri, C.; Biermann, N.; Vlasie, M.D.; Einsle, O.; Merli, A.; Ferrari, D.; Rossi, G.L.; Ubbink, M. (2008). "Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus". Biochemistry. 47 (25): 6560–6570. doi:10.1021/bi7023749. PMID 18512962.
- ↑ Meschi, F.; Wiertz, F.; Klauss, L.; Cavalieri, C.; Blok, A.; Ludwig, B.; Heering, H.A.; Merli, A.; Rossi, G.L.; Ubbink, M. (2010). "Amicyanin transfers electrons from methylamine dehydrogenase to cytochrome c-551i via a ping-pong mechanism, not a ternary complex". J. Am. Chem. Soc. 132 (41): 14537–14545. doi:10.1021/ja105498m. PMID 20873742.
External links
- Methylamine dehydrogenase (amicyanin) at the US National Library of Medicine Medical Subject Headings (MeSH)
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