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1,12-diaminododecane + acceptor + H2O
? + NH3 + reduced acceptor
-
-
-
-
?
1,6-diaminohexane + acceptor + H2O
?
-
acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
-
-
?
1,7-diaminoheptane + acceptor + H2O
?
-
acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
-
-
?
1,8-diaminooctane + H2O + acceptor
?
1-aminopentane + acceptor + H2O
pentanal + NH3 + reduced acceptor
-
acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
-
-
?
12-aminododecane + acceptor + H2O
dodecanal + NH3 + reduced acceptor
-
-
-
-
?
12-aminododecanoic acid + acceptor + H2O
?
-
-
-
-
r
2-phenylethylamine + 2 H2O + 2 acceptor
2-phenylacetic acid + NH3 + 2 reduced acceptor
-
primary amine
-
-
?
2-phenylethylamine + acceptor + H2O
2-phenylacetaldehyde + NH3 + reduced acceptor
-
acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
-
-
?
benzylamine + acceptor + H2O
benzaldehyde + NH3 + reduced acceptor
benzylamine + H2O + ferricyanide
benzaldehyde + NH3 + reduced ferricyanide
-
-
-
-
?
butylamine + acceptor + H2O
butanal + NH3 + reduced acceptor
dithionite + amicyanin + H2O
?
-
two-electron-reduced MADH is obtained by exposing the enzyme either to a 3fold molar excess of methylamine or to 2 mM dithionite
-
-
?
ethylamine + acceptor + H2O
acetaldehyde + NH3 + reduced acceptor
histamine + acceptor + H2O
? + NH3 + reduced acceptor
-
-
-
-
?
methylamine + acceptor + H2O
formaldehyde + NH3 + reduced acceptor
methylamine + acceptor + H2O
methanal + NH3 + reduced acceptor
methylamine + amicyanin + H2O
formaldehyde + NH3 + reduced amicyanin
-
-
-
-
?
methylamine + amicyanin + H2O
formaldehyde + reduced amicyanin + NH3
methylamine + H2O + 2 amicyanin
formaldehyde + NH3 + 2 reduced amicyanin
methylamine + H2O + 2,6-dichloroindophenol
formaldehyde + NH3 + reduced 2,6-dichloroindophenol
-
-
-
-
r
methylamine + H2O + 2,6-dichloroindophenol + phenazine ethosulfate
formaldehyde + NH3 + reduced phenazine ethosulfate + ?
-
-
-
-
r
methylamine + H2O + amicyanin
formaldehyde + ammonia + reduced amicyanin
methylamine + H2O + amicyanin
formaldehyde + NH3 + reduced amicyanin
-
-
-
?
methylamine + H2O + cytochrome c-550
formaldehyde + NH3 + reduced cytochrome c-550
-
-
-
-
r
methylamine + H2O + K3Fe(CN)6
formaldehyde + NH3 + reduced K3Fe(CN)6
-
-
-
-
r
n-butylamine + H2O + ferricyanide
butanal + NH3 + reduced ferricyanide
-
-
-
-
?
n-hexylamine + acceptor + H2O
hexanal + NH3 + reduced acceptor
n-nonylamine + acceptor + H2O
nonanal + NH3 + reduced acceptor
-
-
-
-
?
n-pentylamine + acceptor + H2O
pentanal + NH3 + reduced acceptor
-
-
-
-
?
phenylethylamine + acceptor + H2O
phenylacetaldehyde + NH3 + reduced acceptor
propylamine + acceptor + H2O
propionaldehyde + NH3 + reduced acceptor
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
tryptamine + acceptor + H2O
?
-
-
-
-
?
additional information
?
-
1,8-diaminooctane + H2O + acceptor
?
-
-
-
-
?
1,8-diaminooctane + H2O + acceptor
?
-
-
-
-
?
benzylamine + acceptor + H2O
benzaldehyde + NH3 + reduced acceptor
-
-
-
-
?
benzylamine + acceptor + H2O
benzaldehyde + NH3 + reduced acceptor
-
acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
-
-
?
benzylamine + acceptor + H2O
benzaldehyde + NH3 + reduced acceptor
-
-
-
-
?
benzylamine + acceptor + H2O
benzaldehyde + NH3 + reduced acceptor
-
-
-
-
?
butylamine + acceptor + H2O
butanal + NH3 + reduced acceptor
-
-
-
-
?
butylamine + acceptor + H2O
butanal + NH3 + reduced acceptor
-
acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
-
-
?
butylamine + acceptor + H2O
butanal + NH3 + reduced acceptor
-
-
-
-
?
butylamine + acceptor + H2O
butanal + NH3 + reduced acceptor
-
-
-
-
?
ethylamine + acceptor + H2O
acetaldehyde + NH3 + reduced acceptor
-
-
-
-
?
ethylamine + acceptor + H2O
acetaldehyde + NH3 + reduced acceptor
-
acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
-
-
?
methylamine + acceptor + H2O
formaldehyde + NH3 + reduced acceptor
-
-
-
-
?
methylamine + acceptor + H2O
formaldehyde + NH3 + reduced acceptor
-
-
-
-
?
methylamine + acceptor + H2O
formaldehyde + NH3 + reduced acceptor
-
-
-
-
?
methylamine + acceptor + H2O
formaldehyde + NH3 + reduced acceptor
-
acceptor: amicyanin
-
-
?
methylamine + acceptor + H2O
formaldehyde + NH3 + reduced acceptor
-
acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
-
-
?
methylamine + acceptor + H2O
formaldehyde + NH3 + reduced acceptor
-
-
-
-
?
methylamine + acceptor + H2O
methanal + NH3 + reduced acceptor
Mycobacterium convolutum
-
-
-
-
?
methylamine + acceptor + H2O
methanal + NH3 + reduced acceptor
-
-
-
-
?
methylamine + acceptor + H2O
methanal + NH3 + reduced acceptor
-
acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol or amicyanin
-
-
?
methylamine + acceptor + H2O
methanal + NH3 + reduced acceptor
-
-
-
-
?
methylamine + amicyanin + H2O
formaldehyde + reduced amicyanin + NH3
-
amicyanin is the in vivo electron acceptor
-
-
?
methylamine + amicyanin + H2O
formaldehyde + reduced amicyanin + NH3
-
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
-
-
?
methylamine + H2O + 2 amicyanin
formaldehyde + NH3 + 2 reduced amicyanin
-
-
-
?
methylamine + H2O + 2 amicyanin
formaldehyde + NH3 + 2 reduced amicyanin
-
-
-
?
methylamine + H2O + 2 amicyanin
formaldehyde + NH3 + 2 reduced amicyanin
-
-
-
-
?
methylamine + H2O + amicyanin
formaldehyde + ammonia + reduced amicyanin
-
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
-
-
?
methylamine + H2O + amicyanin
formaldehyde + ammonia + reduced amicyanin
-
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
-
-
?
n-hexylamine + acceptor + H2O
hexanal + NH3 + reduced acceptor
-
-
-
-
?
n-hexylamine + acceptor + H2O
hexanal + NH3 + reduced acceptor
-
-
-
-
?
phenylethylamine + acceptor + H2O
phenylacetaldehyde + NH3 + reduced acceptor
-
-
-
-
?
phenylethylamine + acceptor + H2O
phenylacetaldehyde + NH3 + reduced acceptor
-
-
-
-
?
phenylethylamine + acceptor + H2O
phenylacetaldehyde + NH3 + reduced acceptor
-
-
-
-
?
propylamine + acceptor + H2O
propionaldehyde + NH3 + reduced acceptor
-
-
-
-
?
propylamine + acceptor + H2O
propionaldehyde + NH3 + reduced acceptor
-
acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
-
-
?
propylamine + acceptor + H2O
propionaldehyde + NH3 + reduced acceptor
-
-
-
-
?
propylamine + acceptor + H2O
propionaldehyde + NH3 + reduced acceptor
-
-
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
-
acceptor 2,6-dichlorophenolindophenol
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
-
acceptor phenazine ethosulfate or amicyanin
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
-
acceptor potassium ferricyanide, phenazine ethosulfate, 2,6-dichlorophenolindophenol
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
-
acceptor potassium ferricyanide, phenazine ethosulfate, 2,6-dichlorophenolindophenol
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
-
-
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
-
acceptor cytochrome c-550
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
-
acceptor phenazine methosulfate
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
-
acceptor 2,6-dichlorophenol-indophenol, ferricyanide or cytochrome c
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
-
cytochrome c or artificial electron acceptor
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
-
acceptor 2,6-dichlorophenolindophenol
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
-
acceptor phenazine methosulfate
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
-
acceptor 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide and potassium ferricyanide
-
-
?
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
-
acceptor phenazine methosulfate
-
-
?
additional information
?
-
Mycobacterium convolutum
-
broad specificity
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
methylamine dehydrogenase (MADH) requires the cofactor tryptophan tryptophylquinone (TTQ) for activity
-
-
?
additional information
?
-
-
broad specificity
-
-
?
additional information
?
-
-
broad specificity
-
-
?
additional information
?
-
-
broad specificity
-
-
?
additional information
?
-
-
not: FMN, NAD+, NADP+
-
-
?
additional information
?
-
-
little or no activity with isoamines, L-ornithine, L-lysine and certain diamines or polyamines
-
-
?
additional information
?
-
-
an essential enzyme for the aerobic degradation of many primary amines even though they have quite different chemical structures (aromatic or aliphatic)
-
-
?
additional information
?
-
-
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.
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
broad specificity
-
-
?
additional information
?
-
-
broad specificity
-
-
?
additional information
?
-
-
nonspecific oxidizing both short and long primary monoamines and diamines, polyamines, L-noradrenaline, histamine, benzylamine and di-n-hexylamine
-
-
?
additional information
?
-
-
broad specificity
-
-
?
additional information
?
-
-
nonspecific oxidizing both short and long primary monoamines and diamines, polyamines, L-noradrenaline, histamine, benzylamine and di-n-hexylamine
-
-
?
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0.003
1,12-diaminododecane
-
-
0.021 - 0.72
1,6-diaminohexane
0.007 - 0.38
1,7-Diaminoheptane
0.004 - 2.5
1-aminopentane
0.033
12-aminododecanoic acid
-
-
0.12
2,6-dichloroindophenol
-
-
0.042
cytochrome c-550
-
-
0.014
phenazine ethosulfate
-
-
0.021
1,6-diaminohexane
-
pH 7.5, 30°C, mutant enzyme alphaF55A
0.031
1,6-diaminohexane
-
pH 7.5, 30°C, mutant enzyme betaI107N
0.099
1,6-diaminohexane
-
pH 7.5, 30°C, mutant enzyme alphaF55I
0.17
1,6-diaminohexane
-
pH 7.5, 30°C, mutant enzyme betaI107V
0.72
1,6-diaminohexane
-
pH 7.5, 30°C, wild-type enzyme
0.007
1,7-Diaminoheptane
-
pH 7.5, 30°C, mutant enzyme alphaF55A
0.057
1,7-Diaminoheptane
-
pH 7.5, 30°C, mutant enzyme alphaF55I
0.068
1,7-Diaminoheptane
-
pH 7.5, 30°C, mutant enzyme betaI107N
0.29
1,7-Diaminoheptane
-
pH 7.5, 30°C, mutant enzyme betaI107V
0.38
1,7-Diaminoheptane
-
pH 7.5, 30°C, wild-type enzyme
0.004
1-aminopentane
-
pH 7.5, 30°C, mutant enzyme betaI107N
0.047
1-aminopentane
-
pH 7.5, 30°C, mutant enzyme alphaF55A
0.13
1-aminopentane
-
pH 7.5, 30°C, mutant enzyme betaI107V
0.25
1-aminopentane
-
pH 7.5, 30°C, mutant enzyme alphaF55I
2.5
1-aminopentane
-
pH 7.5, 30°C, wild-type enzyme
0.007
Butylamine
-
pH 7.5, 30°C, mutant enzyme betaI107N
0.088
Butylamine
-
pH 7.5, 30°C, mutant enzyme betaI107V
0.24
Butylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55A
0.37
Butylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55I
0.87
Butylamine
-
pH 7.5, 30°C, wild-type enzyme
0.019
ethylamine
-
pH 7.5, 30°C, wild-type enzyme
0.34
ethylamine
-
pH 7.5, 30°C, mutant enzyme betaI107V
0.36
ethylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55I
0.84
ethylamine
-
pH 7.5, 30°C, mutant enzyme betaI107N
9.2
ethylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55A
0.004
methylamine
-
pH 8.5, 30°C, wild-type enzyme, acceptor amicyanin
0.005
methylamine
-
pH 7.5, 30°C, wild-type enzyme, acceptor amicyanin
0.0059
methylamine
-
with amicyanin as electron acceptor
0.0064
methylamine
-
with phenylazine as electron acceptor
0.009
methylamine
-
pH 7.5, 30°C, wild-type enzyme
0.015
methylamine
-
pH 7.5, 30°C, wild-type enzyme, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol
0.021
methylamine
-
pH 8.5, 30°C, wild-type enzyme, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol
0.06
methylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55I
0.069
methylamine
-
pH 7.5, 30°C, mutant enzyme betaI107V
0.25
methylamine
-
pH 7.5, 30°C, mutant enzyme betaI107N
12.2
methylamine
-
pH 8.5, 30°C, mutant enzyme betaD32N, acceptor amicyanin
14.9
methylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55A
16.7
methylamine
-
pH 7.5, 30°C, mutant enzyme betaD32N, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol
19.6
methylamine
-
pH 7.5, 30°C, mutant enzyme betaD32N, acceptor amicyanin
22.4
methylamine
-
pH 8.5, 30°C, mutant enzyme betaD32N, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol
0.006
Propylamine
-
pH 7.5, 30°C, mutant enzyme betaI107V
0.008
Propylamine
-
pH 7.5, 30°C, mutant enzyme betaI107N
0.036
Propylamine
-
pH 7.5, 30°C, wild-type enzyme
0.2
Propylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55I
1.3
Propylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3.4 - 43
1,6-diaminohexane
3.4 - 32
1,7-Diaminoheptane
1.5
2,6-dichloroindophenol
-
-
3.1
2-Phenylethylamine
-
pH 7.5, 30°C
7.1
phenazine ethosulfate
-
-
additional information
additional information
-
turnover numbers for deuterated substrates
-
3.4
1,6-diaminohexane
-
pH 7.5, 30°C, mutant enzyme alphaF55I
16
1,6-diaminohexane
-
pH 7.5, 30°C, mutant enzyme betaI107N
17
1,6-diaminohexane
-
pH 7.5, 30°C, wild-type enzyme
26
1,6-diaminohexane
-
pH 7.5, 30°C, mutant enzyme betaI107V
43
1,6-diaminohexane
-
pH 7.5, 30°C, mutant enzyme alphaF55A
3.4
1,7-Diaminoheptane
-
pH 7.5, 30°C, mutant enzyme alphaF55I
15
1,7-Diaminoheptane
-
pH 7.5, 30°C, mutant enzyme betaI107N
19
1,7-Diaminoheptane
-
pH 7.5, 30°C, mutant enzyme betaI107V
27
1,7-Diaminoheptane
-
pH 7.5, 30°C, wild-type enzyme
32
1,7-Diaminoheptane
-
pH 7.5, 30°C, mutant enzyme alphaF55A
3.4
1-aminopentane
-
pH 7.5, 30°C, mutant enzyme betaI107V
4.2
1-aminopentane
-
pH 7.5, 30°C, mutant enzyme betaI107N
5.4
1-aminopentane
-
pH 7.5, 30°C, mutant enzyme alphaF55I
17
1-aminopentane
-
pH 7.5, 30°C, wild-type enzyme
20
1-aminopentane
-
pH 7.5, 30°C, mutant enzyme alphaF55A
0.77
amicyanin
-
methylamine-reduced MADH, pH 7.5 using a Ca-HEPES puffer
-
3.1
amicyanin
-
dithionite-reduced MADH, pH 7.5 using a Na,K-phosphate buffer and 0.2 M KCl
-
74
amicyanin
-
methylamine-reduced MADH, pH 7.5 using a Na,K-phosphate buffer and 0.2 M KCl
-
3.8
benzylamine
-
pH 7.5, 30°C
4.2
Butylamine
-
pH 7.5, 30°C, mutant enzyme betaI107N
5.4
Butylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55I
5.8
Butylamine
-
pH 7.5, 30°C
14
Butylamine
-
pH 7.5, 30°C, mutant enzyme betaI107V
22
Butylamine
-
pH 7.5, 30°C, wild-type enzyme
34
Butylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55A
4.5
ethylamine
-
pH 7.5, 30°C, mutant enzyme betaI107N
6.2
ethylamine
-
pH 7.5, 30°C, mutant enzyme betaI107V
15
ethylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55I
23
ethylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55A
24
ethylamine
-
pH 7.5, 30°C, wild-type enzyme
0.14
methylamine
-
pH 7.5, 30°C, mutant enzyme betaD32N, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol
0.19
methylamine
-
pH 8.5, 30°C, mutant enzyme betaD32N, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol
0.47
methylamine
-
pH 7.5, 30°C, mutant enzyme betaD32N, acceptor amicyanin
1.2
methylamine
-
pH 8.5, 30°C, mutant enzyme betaD32N, acceptor amicyanin
2
methylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55I
13.6
methylamine
-
with phenylazine as electron acceptor
18
methylamine
-
pH 8.5, 30°C, wild-type enzyme, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol
20
methylamine
-
pH 7.5, 30°C, mutant enzyme betaI107V
23
methylamine
-
pH 7.5, 30°C, wild-type enzyme, acceptor amicyanin
26
methylamine
-
pH 8.5, 30°C, wild-type enzyme, acceptor amicyanin
30
methylamine
-
with amicyanin as electron acceptor at pH 7
30
methylamine
-
pH 7.5, 30°C, wild-type enzyme
34
methylamine
-
pH 7.5, 30°C, mutant enzyme betaI107N
35
methylamine
-
pH 7.5, 30°C, wild-type enzyme, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol
48.5
methylamine
-
with amicyanin as electron acceptor
55
methylamine
-
with amicyanin as electron acceptor at pH 10
77
methylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55A
3.1
Propylamine
-
pH 7.5, 30°C, mutant enzyme betaI107V
4.1
Propylamine
-
pH 7.5, 30°C, mutant enzyme betaI107N
5.2
Propylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55I
24
Propylamine
-
pH 7.5, 30°C, mutant enzyme alphaF55A
27
Propylamine
-
pH 7.5, 30°C, wild-type enzyme
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trimer
-
alpha,beta,gamma, X-ray crystallography
dimer
-
anion-exchange chromatography and SDS-PAGE, 12000 Da and 42000 Da subunits
dimer
-
anion-exchange chromatography and SDS-PAGE, 12000 Da and 42000 Da subunits
-
dimer
-
alpha,beta, 1 * 59500 + 1 * 36500, SDS-PAGE
dimer
-
alpha,beta, 1 * 59500 + 1 * 36500, SDS-PAGE
-
dimer
-
1 * 58000 + 1 * 42000, SDS-PAGE
dimer
-
1 * 60000 + 1 * 39000, SDS-PAGE
heterotetramer
-
heterotetramer
alpha2beta2
heterotetramer
-
alpha2beta2 protein, with each beta subunit possessing a tryptophan tryptophylquinone, TTQ, protein-derived cofactor
heterotetramer
alpha2beta2, 2 * 42500, alpha-subunit, + 2 * 14200, beta-subunit, SDS-PAGE
heterotetramer
-
2 * 43300 + 2 * 14200, X-ray crystallography
heterotetramer
-
crystal structure, enzyme shows a alpha2beta2 structure, consisting of two heavy chains and two light chains, alpha subunit: 43300 Da, beta subunit: 14200 Da
heterotrimer
-
gel filtration, mass spectroscopy and UV-VIS spectroscopy: the gamma subunit of sQH-AmDH shows a sharp peak at 390 nm in UV-VIS spectrum clearly distinguishable from that of QH-AmDH. Electrospray ionization mass spectrometric analysis shows that the molecular mass of the gamma subunit of sQH-AmDH is larger than that of QH-AmDH by 15.6. The data suggest that the cysteine tryptophylquinone-like moiety (catalytic center) of the gamma subunit of sQH-AmDH is an oxime
heterotrimer
1 * 60000, alpha-subunit, + 1 * 37000, beta-subunit, + 1 * 9000, gamma-subunit, SDS-PAGE
heterotrimer
-
1 * 53917 + 1 * 39234 + 1 * 8597, calculated from amino acid sequence
heterotrimer
-
consists of a four-domain alpha-subunit (about 60000 Da) that harbors a di-heme cytochrome c, a seven-bladed beta-propeller beta-subunit(about 40000 Da) that provides part of the active site, and a small gamma-subunit (about 9000 Da) that contains the cofactor cysteine tryptophylquinone
heterotrimer
-
determinated by in silico-experiments, beta-subunit with 349 aa, gamma-subunit with 79 aa and an alpha-subunit with 494 aa
monomer
-
1 * 47000, SDS-PAGE
monomer
-
1 * 47000, SDS-PAGE
-
tetramer
-
2 * 14000 + 2 * 41000, X-ray crystallography
tetramer
-
2 * 14000 + 2 * 41000, X-ray crystallography
-
additional information
MADH is a 114 kDa alpha2beta2 heterotetramer with two independent active sites, each containing a TTQ cofactor biosynthesized from betaTrp57 and betaTrp108 of the beta-subunit
additional information
MADH is a heterotetramer consisting of two alpha subunits and two beta subunits which are encoded by mauB and mauA, respectively
additional information
QHNDH is composed of three nonidentical subunits, designated alpha, beta, and gamma. The alpha subunit, the largest, has a four-domain structure with two heme c groups contained in the N-terminal diheme cytochrome c-like domain. The beta subunit has a seven-bladed beta propeller structure that is well-conserved across quinoproteins. The gamma subunit, the smallest of the three, is buried inside the alpha subunit. It has a particularly unusual structure consisting mostly of featureless coils with a covalently bound quinone cofactor, cysteine tryptophylquinone (CTQ), derived from Trp and Cys residues, and three intrapeptidyl thioether cross-links formed between Cys and Glu or Asp residues. The gamma subunit clearly indicate that it must undergo multiple posttranslational modifications before it can form an active QHNDH complex with the alpha and beta subunits
additional information
-
QHNDH is composed of three nonidentical subunits, designated alpha, beta, and gamma. The alpha subunit, the largest, has a four-domain structure with two heme c groups contained in the N-terminal diheme cytochrome c-like domain. The beta subunit has a seven-bladed beta propeller structure that is well-conserved across quinoproteins. The gamma subunit, the smallest of the three, is buried inside the alpha subunit. It has a particularly unusual structure consisting mostly of featureless coils with a covalently bound quinone cofactor, cysteine tryptophylquinone (CTQ), derived from Trp and Cys residues, and three intrapeptidyl thioether cross-links formed between Cys and Glu or Asp residues. The gamma subunit clearly indicate that it must undergo multiple posttranslational modifications before it can form an active QHNDH complex with the alpha and beta subunits
additional information
-
protein PeaB, although not interacting with the active QHNDH along the catalytic reaction, is needed for the correct functionality of this enzyme and for the post-translational modification of the gamma-subunit before its translocation to the periplasmic space.
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betaD32N
-
preparation contains a major species with six disulfides but no oxygen incorporated into betaTrp57 and a minor species with both oxygens incorporated, which is active. 1000fold increase in KM-value for methylamine
betaD76N
-
mutant enzyme is completely inactive
F55A
-
mutation of the alpha subunit
F55E
-
mutation of the alpha subunit
T122A
-
the presence of Thr122 has a deleterious effect on the proton transfer step that is proposed to determine the rate of the reaction, the substitution of Thr122 by Ala does not significantly modify the preference of the proton by atom OD2 of Asp76
K14E
-
mutation of cytochrome c-550
K14Q
-
mutation of cytochrome c-550
alphaF55A
-
1656fold increase in Km-value for methylamine compared to wild-type enzyme, 484fold increase in Km-value for ethylamine compared to wild-type enzyme, 36fold increase in Km-value for propylamine compared to wild-type enzyme, 3.6fold decrease in Km-value for butylamine compared to wild-type enzyme, 53.2fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 34.3fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 54.3fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme
alphaF55A
-
inactivation by the mechanism-based inhibitor cyclopropylamine 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
alphaF55A
-
mutation decreases the affinity for binding of monovalent cations, Na+ or K+. 1656fold increase in Km-value for methylamine compared to wild-type enzyme, 484fold increase in Km-value for ethylamine compared to wild-type enzyme, 36fold increase in Km-value for propylamine compared to wild-type enzyme, 3.6fold decrease in Km-value for butylamine compared to wild-type enzyme, 53.2fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 34.3fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 54.3fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme
alphaF55A
-
mutation increases the rate of the electron transfer reaction from the fully reduced tryptophan tryptophylquinone tryptophan tryptophylquinone methylamine dehydrogenase to amicyanin. Little difference in the overal structure of alphaF55A in complex with its electron acceptors, amicyanin and cytochrome c-551i, relative to the native complex. There are significant changes in the solvent content of the active site and substrate channel
alphaF55I
-
1.2fold decrease in Km-value for methylamine compared to wild-type enzyme, 18.9fold increase in Km-value for ethylamine compared to wild-type enzyme, 5.6fold increase in Km-value for propylamine compared to wild-type enzyme, 4.2fold decrease in Km-value for butylamine compared to wild-type enzyme, 10fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 7.3fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 6.7fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzym. Ability to discriminate between amines of different chain length is abolished
alphaF55I
-
inactivation by the mechanism-based inhibitor cyclopropylamine 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
alphaF55I
-
mutation has no effect on binding of monovalent cation. 1.2fold decrease in Km-value for methylamine compared to wild-type enzyme, 18.9fold increase in Km-value for ethylamine compared to wild-type enzyme, 5.6fold increase in Km-value for propylamine compared to wild-type enzyme, 4.2fold decrease in Km-value for butylamine compared to wild-type enzyme, 10fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 7.3fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 6.7fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme
betaI107N
-
27.8fold increase in Km-value for methylamine compared to wild-type enzyme, 44.2fold increase in Km-value for ethylamine compared to wild-type enzyme, 8.5fold decrease in Km-value for propylamine compared to wild-type enzyme, 124fold decrease in Km-value for butylamine compared to wild-type enzyme, 62.5fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 23.2fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 5.6fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme
betaI107N
-
27.8fold increase in Km-value for methylamine compared to wild-type enzyme, 44.2fold increase in Km-value for ethylamine compared to wild-type enzyme, 8.5fold decrease in Km-value for propylamine compared to wild-type enzyme, 124fold decrease in Km-value for butylamine compared to wild-type enzyme, 62.5fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 23.2fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 5.6fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme. Mutant enzyme exhibity a strong preference for 1-aminopentane compared to strong preference for methylamine of the wild-type enzyme
betaI107V
-
7.7fold increase in Km-value for methylamine compared to wild-type enzyme, 17.9fold increase in Km-value for ethylamine compared to wild-type enzyme, 6fold decrease in Km-value for propylamine compared to wild-type enzyme, 9.9fold decrease in Km-value for butylamine compared to wild-type enzyme, 19.2fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 4.2fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 1.3fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme
betaI107V
-
mutant enzyme exhibits a strong preference for propylamine compared to strong preference for methylamine of the wild-type enzyme. 7.7fold increase in Km-value for methylamine compared to wild-type enzyme, 17.9fold increase in Km-value for ethylamine compared to wild-type enzyme, 6fold decrease in Km-value for propylamine compared to wild-type enzyme, 9.9fold decrease in Km-value for butylamine compared to wild-type enzyme, 19.2fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 4.2fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 1.3fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme
additional information
generation of of the gene disrupted mutant strains PdDELTAqhpF, PdDELTAqhpG, and PdDELTAqhpR
additional information
-
generation of of the gene disrupted mutant strains PdDELTAqhpF, PdDELTAqhpG, and PdDELTAqhpR
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Shinagawa, E.; Matsushita, K.; Nakashima, K.; Adachi, O.; Ameyama, M.
Crystallization and properties of amine dehydrogenase from Pseudomonas sp.
Agric. Biol. Chem.
52
2255-2263
1988
Pseudomonas sp.
-
brenda
Niimura, Y.; Omori, T.; Minoda, Y.
Purification and properties of an amine dehydrogenase from Pseudomonas K95 grown on 1,12-diaminododecane (DAD)
Agric. Biol. Chem.
50
1445-1451
1986
Pseudomonas sp., Pseudomonas sp. K95
-
brenda
Boulton, C.A.; Large, P.J.
Properties of Pseudomonas AM1 primary-amine dehydrogenase immobilized on agarose
Biochim. Biophys. Acta
570
22-30
1979
Pseudomonas sp., Pseudomonas sp. AM1
brenda
Eady, R.R.; Large, P.J.
Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine
Biochem. J.
106
245-255
1968
Pseudomonas sp.
brenda
Durham, D.R.; Perry, J.J.
Amine dehydrogenase of Pseudomonas putida: properties of the heme-prosthetic group
J. Bacteriol.
135
981-986
1978
Pseudomonas putida
brenda
Durham, D.R.; Perry, J.J.
Purification and characterization of a heme-containing amine dehydrogenase from Pseudomonas putida
J. Bacteriol.
134
837-843
1978
Pseudomonas putida
brenda
Durham, D.R.; Perry, J.J.
The inducible amine dehydrogenase in Pseudomonas putida NP and its role in the metabolism of benzylamine
J. Gen. Microbiol.
105
39-44
1978
Pseudomonas putida
-
brenda
Cerniglia, C.E.; Perry, J.J.
Metabolism of n-propylamine, isopropylamine, and 1,3-propane diamine by Mycobacterium convolutum
J. Bacteriol.
124
285-289
1975
Mycobacterium convolutum
brenda
De Beer, R.; Duine, J.A.; Frank, J.; Large, P.J.
The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1: evidence for a quinone structure
Biochim. Biophys. Acta
622
370-374
1980
Pseudomonas sp., Pseudomonas sp. AM1
brenda
Eady, R.R.; Large, P.J.
Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM1
Biochem. J.
123
757-771
1971
Pseudomonas sp., Pseudomonas sp. AM1
brenda
Brooks, H.B.; Jones, L.H.; Davidson, V.L.
Deuterium kinetic isotope effect and stopped-flow kinetic studies of the quinoprotein methylamine dehydrogenase
Biochemistry
32
2725-2729
1993
Paracoccus denitrificans
brenda
Gorren, A.C.F.; Duine, J.A.
The effects of pH and cations on the spectral and kinetic properties of methylamine dehydrogenase from Thiobacillus versutus
Biochemistry
33
12202-12209
1994
Paracoccus versutus
brenda
Ubbink, M.; Hunt, N.I.; Hill, H.A.O.; Canters, G.W.
Kinetics of the reduction of wild-type and mutant cytochrome c-550 by methylamine dehydrogenase and amicyanin from Thiobacillus versutus
Eur. J. Biochem.
222
561-571
1994
Paracoccus versutus
brenda
Labesse, G.; Ferrari, D.; Chen, Z.W.; Rossi, G.L.; Kuusk, V.; McIntire, W.S.; Mathews, F.S.
Crystallographic and spectroscopic studies of native, aminoquinol, and monovalent cation-bound forms of methylamine dehydrogenase from Methylobacterium extorquens AM1
J. Biol. Chem.
273
25703-25712
1998
Methylorubrum extorquens, Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
brenda
Takagi, K.; Torimura, M.; Kawaguchi, K.; Kano, K.; Ikeda, T.
Biochemical and electrochemical characterization of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans
Biochemistry
38
6935-6942
1999
Paracoccus denitrificans, Paracoccus denitrificans IFO 12442
brenda
Sun, D.; Davidson, V.L.
Re-engineering monovalent cation binding sites of methylamine dehydrogenase: effects on spectral properties and gated electron transfer
Biochemistry
40
12285-12291
2001
Paracoccus denitrificans
brenda
Bao, L.; Sun, D.; Tachikawa, H.; Davidson, V.L.
Improved sensitivity of a histamine sensor using an engineered methylamine dehydrogenase
Anal. Chem.
74
1144-1148
2002
Paracoccus denitrificans
brenda
Satoh, A.; Kim, J.K.; Miyahara, I.; Devreese, B.; Vandenberghe, I.; Hacisalihoglu, A.; Okajima, T.; Kuroda, S.i.; Adachi, O.; Duine, J.A.; Van Beeumen, J.; Tanizawa, K.; Hirotsu, K.
Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida: identification of a novel quinone cofactor encaged by multiple thioether cross-bridges
J. Biol. Chem.
277
2830-2834
2002
Pseudomonas putida
brenda
Datta, S.; Ikeda, T.; Kano, K.; Mathews, F.S.
Structure of the phenylhydrazine adduct of the quinohemoprotein amine dehydrogenase from Paracoccus denitrificans at 1.7 A resolution
Acta Crystallogr. Sect. D
59
1551-1556
2003
Paracoccus denitrificans
brenda
Sun, D.; Chen, Z.W.; Mathews, F.S.; Davidson, V.L.
Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyanin
Biochemistry
41
13926-13933
2002
Paracoccus denitrificans
brenda
Sun, D.; Ono, K.; Okajima, T.; Tanizawa, K.; Uchida, M.; Yamamoto, Y.; Mathews, F.S.; Davidson, V.L.
Chemical and kinetic reaction mechanisms of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans
Biochemistry
42
10896-10903
2003
Paracoccus denitrificans
brenda
Davidson, V.L.
Probing mechanisms of catalysis and electron transfer by methylamine dehydrogenase by site-directed mutagenesis of alpha Phe55
Biochim. Biophys. Acta
1647
230-233
2003
Paracoccus denitrificans
brenda
Sun, D.; Davidson, V.L.
Inter-subunit cross-linking of methylamine dehydrogenase by cyclopropylamine requires residue alphaPhe55
FEBS Lett.
517
172-174
2002
Paracoccus denitrificans
brenda
Wang, Y.; Sun, D.; Davidson, V.L.
Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase
J. Biol. Chem.
277
4119-4122
2002
Paracoccus denitrificans
brenda
Jones, L.H.; Pearson, A.R.; Tang, Y.; Wilmot, C.M.; Davidson, V.L.
Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase
J. Biol. Chem.
280
17392-17396
2005
Paracoccus denitrificans
brenda
Sun, D.; Li, X.; Mathews, F.S.; Davidson, V.L.
Site-directed mutagenesis of proline 94 to alanine in amicyanin converts a true electron transfer reaction into one that is kinetically coupled
Biochemistry
44
7200-7206
2005
Paracoccus denitrificans
brenda
Ma, J.K.; Carrell, C.J.; Mathews, F.S.; Davidson, V.L.
Site-directed mutagenesis of proline 52 to glycine in amicyanin converts a true electron transfer reaction into one that is conformationally gated
Biochemistry
45
8284-8293
2006
Paracoccus denitrificans
brenda
Wang, Y.; Li, X.; Jones, L.H.; Pearson, A.R.; Wilmot, C.M.; Davidson, V.L.
MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase
J. Am. Chem. Soc.
127
8258-8259
2005
Paracoccus denitrificans
brenda
Ono, K.; Okajima, T.; Tani, M.; Kuroda, S.; Sun, D.; Davidson, V.L.; Tanizawa, K.
Involvement of a putative [Fe-S]-cluster-binding protein in the biogenesis of quinohemoprotein amine dehydrogenase
J. Biol. Chem.
281
13672-13684
2006
Paracoccus denitrificans
brenda
Pierdominici-Sottile, G.; Echave, J.; Palma, J.
Molecular dynamics study of the active site of methylamine dehydrogenase
J. Phys. Chem. B
110
11592-11599
2006
Paracoccus denitrificans
brenda
Vandenberghe, I.; Kim, J.K.; Devreese, B.; Hacisalihoglu, A.; Iwabuki, H.; Okajima, T.; Kuroda, S.; Adachi, O.; Jongejan, J.A.; Duine, J.A.; Tanizawa, K.; Van Beeumen, J.
The covalent structure of the small subunit from Pseudomonas putida amine dehydrogenase reveals the presence of three novel types of internal cross-linkages, all involving cysteine in a thioether bond
J. Biol. Chem.
276
42923-42931
2001
Pseudomonas putida
brenda
Ma, J.K.; Wang, Y.; Carrell, C.J.; Mathews, F.S.; Davidson, V.L.
A single methionine residue dictates the kinetic mechanism of interprotein electron transfer from methylamine dehydrogenase to amicyanin
Biochemistry
46
11137-11146
2007
Paracoccus denitrificans
brenda
Li, X.; Fu, R.; Liu, A.; Davidson, V.L.
Kinetic and physical evidence that the diheme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinone
Biochemistry
47
2908-2912
2008
Paracoccus denitrificans
brenda
Cavalieri, C.; Biermann, N.; Vlasie, M.D.; Einsle, O.; Merli, A.; Ferrari, D.; Rossi, G.L.; Ubbink, M.
Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus
Biochemistry
47
6560-6570
2008
Paracoccus versutus
brenda
Pierdominici-Sottile, G.; Marti, M.A.; Palma, J.
The role of residue Thr122 of methylamine dehydrogenase on the proton transfer from the iminoquinone intermediate to residue Asp76
Chem. Phys. Lett.
456
243-246
2008
Paracoccus denitrificans
-
brenda
Ranaghan, K.E.; Masgrau, L.; Scrutton, N.S.; Sutcliffe, M.J.; Mulholland, A.J.
Analysis of classical and quantum paths for deprotonation of methylamine by methylamine dehydrogenase
ChemPhysChem
8
1816-1835
2007
Paracoccus denitrificans
brenda
Arias, S.; Olivera, E.R.; Arcos, M.; Naharro, G.; Luengo, J.M.
Genetic analyses and molecular characterization of the pathways involved in the conversion of 2-phenylethylamine and 2-phenylethanol into phenylacetic acid in Pseudomonas putida U
Environ. Microbiol.
10
413-432
2008
Pseudomonas putida
brenda
Pearson, A.R.; Pahl, R.; Kovaleva, E.G.; Davidson, V.L.; Wilmot, C.M.
Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry
J. Synchrotron Radiat.
14
92-98
2007
Paracoccus denitrificans
brenda
Fujieda, N.; Mori, M.; Ikeda, T.; Kano, K.
The silent form of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans
Biosci. Biotechnol. Biochem.
73
524-529
2009
Paracoccus denitrificans
brenda
Hilbrig, F.; Jerome, V.; Salzig, M.; Freitag, R.
Strategy for the isolation of native dehydrogenases with potential for biosensor development from the organism Hyphomicrobium zavarzinii ZV580
J. Chromatogr. A
1216
3518-3525
2009
Hyphomicrobium zavarzinii, Hyphomicrobium zavarzinii ZV580
brenda
Shin, S.; Abu Tarboush, N.; Davidson, V.L.
Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase
Biochemistry
49
5810-5816
2010
Paracoccus denitrificans
brenda
Jensen, L.M.; Sanishvili, R.; Davidson, V.L.; Wilmot, C.M.
In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex
Science
327
1392-1394
2010
Paracoccus denitrificans
brenda
Choi, M.; Sukumar, N.; Mathews, F.S.; Liu, A.; Davidson, V.L.
Proline 96 of the copper ligand loop of amicyanin regulates electron transfer from methylamine dehydrogenase by positioning other residues at the protein-protein interface
Biochemistry
50
1265-1273
2011
Paracoccus denitrificans
brenda
Meschi, F.; Wiertz, F.; Klauss, L.; Cavalieri, C.; Blok, A.; Ludwig, B.; Heering, H.A.; Merli, A.; Rossi, G.L.; Ubbink, M.
Amicyanin transfers electrons from methylamine dehydrogenase to cytochrome c-551i via a ping-pong mechanism, not a ternary complex
J. Am. Chem. Soc.
132
14537-14545
2010
Paracoccus denitrificans
brenda
Meschi, F.; Wiertz, F.; Klauss, L.; Blok, A.; Ludwig, B.; Merli, A.; Heering, H.A.; Rossi, G.L.; Ubbink, M.
Efficient electron transfer in a protein network lacking specific interactions
J. Am. Chem. Soc.
133
16861-16867
2011
Paracoccus denitrificans
brenda
Sukumar, N.; Choi, M.; Davidson, V.L.
Replacement of the axial copper ligand methionine with lysine in amicyanin converts it to a zinc-binding protein that no longer binds copper
J. Inorg. Biochem.
105
1638-1644
2011
Paracoccus denitrificans
brenda
de la Lande, A.; Babcock, N.S.; Rezac, J.; Sanders, B.C.; Salahub, D.R.
Surface residues dynamically organize water bridges to enhance electron transfer between proteins
Proc. Natl. Acad. Sci. USA
107
11799-11804
2010
Paracoccus denitrificans
brenda
Yukl, E.T.; Jensen, L.M.; Davidson, V.L.; Wilmot, C.M.
Structures of MauG in complex with quinol and quinone MADH
Acta Crystallogr. Sect. F
69
738-743
2013
Paracoccus denitrificans (Q51658)
brenda
Yukl, E.T.; Goblirsch, B.R.; Davidson, V.L.; Wilmot, C.M.
Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: implications for the mechanism of dioxygen activation
Biochemistry
50
2931-2938
2011
Paracoccus denitrificans (Q51658)
brenda
Choi, M.; Shin, S.; Davidson, V.L.
Characterization of electron tunneling and hole hopping reactions between different forms of MauG and methylamine dehydrogenase within a natural protein complex
Biochemistry
51
6942-6949
2012
Paracoccus denitrificans
brenda
Abu Tarboush, N.; Jensen, L.M.; Wilmot, C.M.; Davidson, V.L.
A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis
FEBS Lett.
587
1736-1741
2013
Paracoccus denitrificans (A1BBA0 and A1BB97)
brenda
Shin, S.; Davidson, V.L.
MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis
Arch. Biochem. Biophys.
544
112-118
2014
Paracoccus denitrificans (P22619 AND P29894)
brenda
Shin, S.; Feng, M.; Davidson, V.L.
Mutation of Trp93 of MauG to tyrosine causes loss of bound Ca2+ and alters the kinetic mechanism of tryptophan tryptophylquinone cofactor biosynthesis
Biochem. J.
456
129-137
2013
Paracoccus denitrificans (P22619 AND P29894)
brenda
Shin, S.; Yukl, E.T.; Sehanobish, E.; Wilmot, C.M.; Davidson, V.L.
Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG
Biochemistry
53
1342-1349
2014
Paracoccus denitrificans (P22619 AND P29894)
brenda
Nakai, T.; Deguchi, T.; Frebort, I.; Tanizawa, K.; Okajima, T.
Identification of genes essential for the biogenesis of quinohemoprotein amine dehydrogenase
Biochemistry
53
895-907
2014
Paracoccus denitrificans (P22619 AND P29894), Paracoccus denitrificans
brenda
Zelleke, T.; Marx, D.
Free-energy landscape and proton transfer pathways in oxidative deamination by methylamine dehydrogenase
Chemphyschem
18
208-222
2017
Paracoccus denitrificans (P22619 AND P29894)
brenda
Wilmot, C.; Yukl, E.
MauG A di-heme enzyme required for methylamine dehydrogenase maturation
Dalton Trans.
42
3127-3135
2013
Paracoccus denitrificans (P22619 AND P29894)
-
brenda
Feng, M.; Ma, Z.; Crudup, B.F.; Davidson, V.L.
Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 A away
FEBS Lett.
591
1566-1572
2017
Paracoccus denitrificans (P22619 AND P29894)
brenda
Jo, M.; Shin, S.; Choi, M.
Intra-electron transfer of amicyanin from newly derived active site to redox potential tuned type 1 copper site
Appl. Biol. Chem.
61
181-187
2018
Paracoccus denitrificans (P22619)
-
brenda
Jeoung, S.; Shin, S.; Choi, M.
Copper-binding energetics of amicyanin in different folding states
Metallomics
12
273-279
2020
Paracoccus denitrificans (P22619), Paracoccus denitrificans
brenda