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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Cofactor
Cofactor on EC 1.4.9.1 - methylamine dehydrogenase (amicyanin)
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quinoid cofactor
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alpha subunit contains unknown quinoid cofactor
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quinone
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contains a quinone similar to but not identical with the prosthetic group of EC 1.1.99.8
cysteine tryptophylquinone
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cofactor is derived from a pair of gene-encoded amino acids by post-translational modification
cysteine tryptophylquinone
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This enzyme contains an unusual redox cofactor (CTQ) and two hemes acting as redox active groups
heme c
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two heme c cofactors mediate the transfer of the substrate-derived electrons from cysteine tryptophylquinone to an external electron acceptor
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tryptophan tryptophylquinone
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contains a tryptophan tryptophylquinone prosthetic group
tryptophan tryptophylquinone
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each beta-subunit possesses a prosthetic group
tryptophan tryptophylquinone
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a two-electron redox cofactor, each beta subunit of the heterotetrameric enzyme NADH possesses a tryptophan tryptophylquinone, TTQ, protein-derived cofactor. TTQ is formed by post-translational modification of two tryptophan residues of the preMADH polypeptide chain through the diheme enzyme MauG. This six-electron oxidation of preMADH requires long-range electron transfer as the structure of the MauG-preMADH complex reveals that the shortest distance between the modified residues of preMADH and the nearest heme of MauG is 14.0 A, overview
tryptophan tryptophylquinone
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MauG is a diheme enzyme that catalyzes the final steps in the biosynthesis of the cofactor tryptophan tryptophylquinone in the enzyme
tryptophan tryptophylquinone
TTQ, methylamine dehydrogenase requires the cofactor tryptophan tryptophylquinone for activity. TTQ is a posttranslational modification that results from an 8-electron oxidation of two specific tryptophans in the MADH beta-subunit, betaTrp57 and betaTrp108. The final 6-electron oxidation is catalyzed by the unusual c-type di-heme enzyme, MauG. The di-ferric enzyme can react with H2O2, but atypically for c-type hemes the di-ferrous enzyme can react with O2 as well. In both cases, an unprecedented bis-Fe(IV) redox state is formed, composed of a ferryl heme (Fe(IV)=O) and the second heme as Fe(IV) stabilized by His-Tyr axial ligation. Bis-Fe(IV) MauG acts as a potent 2-electron oxidant. Catalysis is long-range and requires a hole hopping electron transfer mechanism. TTQ structure analysis, overview
tryptophan tryptophylquinone
TTQ, the catalytic cofactor of enzyme MADH. Activator enzyme MauG is involved in TTQ biosynthesis. Mutation of Trp93 of MauG to tyrosine causes loss of bound Ca2+ and alters the kinetic mechanism of tryptophan tryptophylquinone cofactor biosynthesis. The substrate for MauG-dependent TTQ biosynthesis is preMADH
tryptophan tryptophylquinone
TTQ, the catalytic cofactor of enzyme MADH. It is not an exogenous cofactor but is instead derived from posttranslational modifications of the beta subunits of MADH
tryptophan tryptophylquinone
TTQ, the catalytic cofactor of enzyme MADH. It is not an exogenous cofactor but is instead derived from posttranslational modifications of the beta subunits of MADH as evidenced from the crystal structure of MADH. Kinetic mechanism of MauG-dependent TTQ biosynthesis, overview
tryptophan tryptophylquinone
TTQ, the quinone cofactor of the enzyme. QhpG is involved in the quinone cofactor formation