Entry |
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Name |
methylamine dehydrogenase (amicyanin);
amine dehydrogenase;
primary-amine dehydrogenase;
amine: (acceptor) oxidoreductase (deaminating);
primary-amine:(acceptor) oxidoreductase (deaminating)
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Class |
Oxidoreductases;
Acting on the CH-NH2 group of donors;
With a copper protein as acceptor
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Sysname |
methylamine:amicyanin oxidoreductase (deaminating)
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Reaction(IUBMB) |
methylamine + H2O + 2 amicyanin = formaldehyde + NH3 + 2 reduced amicyanin [RN: R00606]
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Reaction(KEGG) |
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Substrate |
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Product |
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Comment |
Contains tryptophan tryptophylquinone (TTQ) cofactor. The enzyme oxidizes aliphatic monoamines and diamines, histamine and ethanolamine, but not secondary and tertiary amines, quaternary ammonium salts or aromatic amines.
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History |
EC 1.4.9.1 created 1978 as EC 1.4.99.3, modified 1986, transferred 2011 to EC 1.4.98.1, transferred 2011 to EC 1.4.9.1
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Pathway |
ec01120 | Microbial metabolism in diverse environments |
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Orthology |
K08685 | quinohemoprotein amine dehydrogenase |
K15228 | methylamine dehydrogenase light chain |
K15229 | methylamine dehydrogenase heavy chain |
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Genes |
» show all
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Reference |
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Authors |
de Beer R, Duine JA, Frank J, Large PJ. |
Title |
The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1: evidence for a quinone structure. |
Journal |
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Reference |
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Authors |
Eady RR, Large PJ. |
Title |
Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine. |
Journal |
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Reference |
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Authors |
Eady RR, Large PJ. |
Title |
Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM1. |
Journal |
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Reference |
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Authors |
Cavalieri C, Biermann N, Vlasie MD, Einsle O, Merli A, Ferrari D, Rossi GL, Ubbink M |
Title |
Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus. |
Journal |
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Reference |
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Authors |
Meschi F, Wiertz F, Klauss L, Cavalieri C, Blok A, Ludwig B, Heering HA, Merli A, Rossi GL, Ubbink M |
Title |
Amicyanin transfers electrons from methylamine dehydrogenase to cytochrome c-551i via a ping-pong mechanism, not a ternary complex. |
Journal |
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Other DBs |
ExplorEnz - The Enzyme Database: | 1.4.9.1 |
ExPASy - ENZYME nomenclature database: | 1.4.9.1 |
UM-BBD (Biocatalysis/Biodegradation Database): | 1.4.9.1 |
BRENDA, the Enzyme Database: | 1.4.9.1 |
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