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
-
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
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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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Substrates Products
Substrates Products on EC 1.4.9.1 - methylamine dehydrogenase (amicyanin)
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REACTION DIAGRAM
1,6-diaminohexane + acceptor + H2O
?
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acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
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-
?
1,7-diaminoheptane + acceptor + H2O
?
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acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
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-
?
1-aminopentane + acceptor + H2O
pentanal + NH3 + reduced acceptor
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acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
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-
?
12-aminododecane + acceptor + H2O
dodecanal + NH3 + reduced acceptor
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-
-
-
?
2-phenylethylamine + 2 H2O + 2 acceptor
2-phenylacetic acid + NH3 + 2 reduced acceptor
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primary amine
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-
?
2-phenylethylamine + acceptor + H2O
2-phenylacetaldehyde + NH3 + reduced acceptor
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acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
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-
?
benzylamine + H2O + ferricyanide
benzaldehyde + NH3 + reduced ferricyanide
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-
-
-
?
dithionite + amicyanin + H2O
?
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two-electron-reduced MADH is obtained by exposing the enzyme either to a 3fold molar excess of methylamine or to 2 mM dithionite
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-
?
methylamine + amicyanin + H2O
formaldehyde + NH3 + reduced amicyanin
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-
-
-
?
methylamine + H2O + 2,6-dichloroindophenol
formaldehyde + NH3 + reduced 2,6-dichloroindophenol
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-
-
-
r
methylamine + H2O + 2,6-dichloroindophenol + phenazine ethosulfate
formaldehyde + NH3 + reduced phenazine ethosulfate + ?
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-
-
-
r
methylamine + H2O + amicyanin
formaldehyde + NH3 + reduced amicyanin
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-
-
?
methylamine + H2O + cytochrome c-550
formaldehyde + NH3 + reduced cytochrome c-550
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-
-
-
r
methylamine + H2O + K3Fe(CN)6
formaldehyde + NH3 + reduced K3Fe(CN)6
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-
-
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r
n-butylamine + H2O + ferricyanide
butanal + NH3 + reduced ferricyanide
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-
-
-
?
benzaldehyde + NH3 + reduced acceptor
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-
-
-
?
benzylamine + acceptor + H2O
benzaldehyde + NH3 + reduced acceptor
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acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
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-
?
benzylamine + acceptor + H2O
benzaldehyde + NH3 + reduced acceptor
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-
-
-
?
butanal + NH3 + reduced acceptor
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-
-
-
?
butylamine + acceptor + H2O
butanal + NH3 + reduced acceptor
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acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
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-
?
butylamine + acceptor + H2O
butanal + NH3 + reduced acceptor
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-
-
-
?
acetaldehyde + NH3 + reduced acceptor
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-
-
-
?
ethylamine + acceptor + H2O
acetaldehyde + NH3 + reduced acceptor
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acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
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-
?
formaldehyde + NH3 + reduced acceptor
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-
-
-
?
methylamine + acceptor + H2O
formaldehyde + NH3 + reduced acceptor
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-
-
-
?
methylamine + acceptor + H2O
formaldehyde + NH3 + reduced acceptor
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-
-
-
?
methylamine + acceptor + H2O
formaldehyde + NH3 + reduced acceptor
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acceptor: amicyanin
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-
?
methylamine + acceptor + H2O
formaldehyde + NH3 + reduced acceptor
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acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
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-
?
methylamine + acceptor + H2O
formaldehyde + NH3 + reduced acceptor
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-
-
-
?
methanal + NH3 + reduced acceptor
Mycobacterium convolutum
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-
-
-
?
methylamine + acceptor + H2O
methanal + NH3 + reduced acceptor
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-
-
-
?
methylamine + acceptor + H2O
methanal + NH3 + reduced acceptor
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acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol or amicyanin
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-
?
methylamine + acceptor + H2O
methanal + NH3 + reduced acceptor
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-
-
-
?
formaldehyde + reduced amicyanin + NH3
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amicyanin is the in vivo electron acceptor
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-
?
methylamine + amicyanin + H2O
formaldehyde + reduced amicyanin + NH3
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two-electron-reduced MADH is obtained by exposing the enzyme either to a 3fold molar excess of methylamine or to 2 mM dithionite. The complex of MADH and amicyanin in solution is studied using nuclear magnetic resonance. Signals of perdeuterated, 15N-enriched amicyanin bound to MADH are observed. Chemical shift perturbation analysis indicates that the dissociation rate constant is 250/sec and that amicyanin assumes a well-defined position in the complex in solution. The most affected residues are in the interface observed in the crystal structure, whereas smaller chemical shift changes extend to deep inside the protein
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-
?
formaldehyde + NH3 + 2 reduced amicyanin
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-
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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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-
-
-
?
formaldehyde + ammonia + reduced amicyanin
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electron transfer from MADH to cytochrome c-551i does not involve a ternary complex but occurs via a ping-pong mechanism in which amicyanin uses the same interface for the reactions with MADH and cytochrome c-551i. Amicyanin binds tightly to MADH with an interface that matches the one observed in the crystal structure and that mostly overlaps with the binding site for cytochrome c-551i. Amicyanin can react rapidly with cytochrome c-551i, but association of amicyanin with MADH inhibits this reaction
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-
?
methylamine + H2O + amicyanin
formaldehyde + ammonia + reduced amicyanin
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P96A and P96G mutations in amycyanin do not affect the spectroscopic or redox properties of amicyanin but increase the Kd value for complex formation with MADH and alter the kinetic mechanism for the interprotein elcetron transfer reaction. The crystal structure of P96G amicyanin is very similar to that of native amicyanin, but in addition to the change in Pro96, the side chains of residues Phe97 and Arg99, which make contacts with MADH that are important for stabilizing the amicyanin-MADH complex, are oriented differently
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-
?
phenylacetaldehyde + NH3 + reduced acceptor
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-
-
-
?
phenylethylamine + acceptor + H2O
phenylacetaldehyde + NH3 + reduced acceptor
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-
-
-
?
phenylethylamine + acceptor + H2O
phenylacetaldehyde + NH3 + reduced acceptor
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-
-
-
?
propionaldehyde + NH3 + reduced acceptor
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-
-
-
?
propylamine + acceptor + H2O
propionaldehyde + NH3 + reduced acceptor
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acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
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-
?
propylamine + acceptor + H2O
propionaldehyde + NH3 + reduced acceptor
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-
-
-
?
propylamine + acceptor + H2O
propionaldehyde + NH3 + reduced acceptor
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-
-
-
?
RCHO + NH3 + reduced acceptor
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acceptor 2,6-dichlorophenolindophenol
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-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
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acceptor phenazine ethosulfate or amicyanin
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-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
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acceptor potassium ferricyanide, phenazine ethosulfate, 2,6-dichlorophenolindophenol
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
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acceptor potassium ferricyanide, phenazine ethosulfate, 2,6-dichlorophenolindophenol
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
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acceptor cytochrome c-550
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
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acceptor phenazine methosulfate
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
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acceptor 2,6-dichlorophenol-indophenol, ferricyanide or cytochrome c
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
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cytochrome c or artificial electron acceptor
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
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acceptor 2,6-dichlorophenolindophenol
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
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acceptor phenazine methosulfate
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
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acceptor 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide and potassium ferricyanide
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
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acceptor phenazine methosulfate
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-
?
additional information
?
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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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methylamine dehydrogenase (MADH) requires the cofactor tryptophan tryptophylquinone (TTQ) for activity
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?
additional information
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little or no activity with isoamines, L-ornithine, L-lysine and certain diamines or polyamines
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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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-
?
additional information
?
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nonspecific oxidizing both short and long primary monoamines and diamines, polyamines, L-noradrenaline, histamine, benzylamine and di-n-hexylamine
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-
?
additional information
?
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nonspecific oxidizing both short and long primary monoamines and diamines, polyamines, L-noradrenaline, histamine, benzylamine and di-n-hexylamine
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-
?