1.4.9.1: methylamine dehydrogenase (amicyanin)
This is an abbreviated version!
For detailed information about methylamine dehydrogenase (amicyanin), go to the full flat file.
Word Map on EC 1.4.9.1
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1.4.9.1
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tryptophylquinone
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ttq
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paracoccus
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denitrificans
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maug
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quinoproteins
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diheme
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versutus
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bis-feiv
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protein-derived
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methylobacterium
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premadh
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thiobacillus
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davidson
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interprotein
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extorquens
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azurins
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quinol
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six-electron
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substrate-derived
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reorganizational
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n-methylglutamate
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n-butylamine
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diferrous
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aminoquinols
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high-valence
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methylomonas
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mathews
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analysis
- 1.4.9.1
- tryptophylquinone
- ttq
- paracoccus
- denitrificans
- maug
-
quinoproteins
-
diheme
- versutus
-
bis-feiv
-
protein-derived
- methylobacterium
-
premadh
-
thiobacillus
-
davidson
-
interprotein
- extorquens
- azurins
- quinol
-
six-electron
-
substrate-derived
-
reorganizational
- n-methylglutamate
- n-butylamine
-
diferrous
-
aminoquinols
-
high-valence
- methylomonas
-
mathews
- analysis
Reaction
+ + 2 amicyanin = + + 2 reduced amicyanin
Synonyms
amine dehydrogenase, amine: oxidoreductase (acceptor deaminating), dehydrogenase, amine, EC 1.4.98.1, EC 1.4.99.3, Heme 2, MADH, mauA, methylamine dehydrogenase, primary-amine dehydrogenase, QH-AmDH, QHNDH, quinohaemoprotein amine dehydrogenase, quinohemoprotein amine dehydrogenase, quinohemoprotein amine dehydrogenases, sQH-AmDH
ECTree
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Natural Substrates Products
Natural Substrates Products on EC 1.4.9.1 - methylamine dehydrogenase (amicyanin)
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REACTION DIAGRAM
2-phenylethylamine + 2 H2O + 2 acceptor
2-phenylacetic acid + NH3 + 2 reduced acceptor
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primary amine
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methylamine + amicyanin + H2O
formaldehyde + reduced amicyanin + NH3
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amicyanin is the in vivo electron acceptor
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methylamine + H2O + amicyanin
formaldehyde + NH3 + reduced amicyanin
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formaldehyde + NH3 + 2 reduced amicyanin
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methylamine + H2O + 2 amicyanin
formaldehyde + NH3 + 2 reduced amicyanin
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methylamine + H2O + 2 amicyanin
formaldehyde + NH3 + 2 reduced amicyanin
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amicyanin ami catalyzes the electron transfer from MADH to the terminal oxidase, without the need for any c-type cytochrome. In the absence of either MADH or cytochrome aa3, amicanin is not capable of oxygen reduction on the same time scale. The oxygen consumption depends nearly linearly on the amicyanin concentration up to at least 100 microM. Experiments demonstrate a remarkable number of possibilities for the electron transfer. The interactions appear to be governed exclusively by the electrostatic nature of each of the proteins. Paracoccus denitrificans provides a pool of cytochromes for efficient electron transfer via weak, ill-defined interactions
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additional information
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an essential enzyme for the aerobic degradation of many primary amines even though they have quite different chemical structures (aromatic or aliphatic)
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additional information
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when different QHNDH mutants (peaA, peaC and peaD) are transformed with a genetic construction containing the peaABCD cluster, all the recombinant strains efficiently catabolized 2-phenylethylamine as well as other primary amines like propyl-, butyl- and pentylamine.
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