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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Inhibitors
Inhibitors on EC 1.4.9.1 - methylamine dehydrogenase (amicyanin)
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amicyanin mutant M98K
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mutant acts as a competitive inhibitor in the reaction of native amicyanin with methylamine dehydrogenase indicating that the M98K mutation has not affected the affinity for its natural electron donor. The crystal structure of M98K amicyanin reveals an overall structure very similar to native amicyanin but the type I binding site is occupied by zinc instead of copper
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cyclopropylamine
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mechanism-based inhibitor. The resulting inactivation is accompanied by the formation of a covalent cross-link between the alpha and beta subunits of the enzyme. No cross-linking is seen with mutant enzymes alphaF55A or alphaF55I mutant enzymes. With mutant enzyme alphaF55E cross-linking of subunits is observed
additional information
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immobilized enzyme: little change in sensitivity to inhibition
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phenylhydrazine
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O6 of cysteine tryptophylquinone is the site of inhibitory attack by phenylhydrazine