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Information on EC 1.4.9.1 - methylamine dehydrogenase (amicyanin) and Organism(s) Paracoccus denitrificans and UniProt Accession A1BB97

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IUBMB Comments
Contains tryptophan tryptophylquinone (TTQ) cofactor. The enzyme oxidizes aliphatic monoamines and diamines, histamine and ethanolamine, but not secondary and tertiary amines, quaternary ammonium salts or aromatic amines.
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Paracoccus denitrificans
UNIPROT: A1BB97 not found.
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Word Map
The taxonomic range for the selected organisms is: Paracoccus denitrificans
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
+
2
amicyanin
=
+
+
2
reduced amicyanin
Synonyms
methylamine dehydrogenase, quinohemoprotein amine dehydrogenase, qhndh, heme 2, qh-amdh, sqh-amdh, quinohemoprotein amine dehydrogenases, primary-amine dehydrogenase, quinohaemoprotein amine dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amine: oxidoreductase (acceptor deaminating)
-
-
-
-
dehydrogenase, amine
-
-
-
-
Heme 2
-
inactive form of QH-AmDH
methylamine dehydrogenase
primary-amine dehydrogenase
-
-
-
-
QH-AmDH
-
different from MADH
QHNDH
quinohemoprotein amine dehydrogenase
sQH-AmDH
-
silent form of QH-AmDH
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
methylamine + H2O + 2 amicyanin = formaldehyde + NH3 + 2 reduced amicyanin
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
oxidative deamination
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
methylamine:amicyanin oxidoreductase (deaminating)
Contains tryptophan tryptophylquinone (TTQ) cofactor. The enzyme oxidizes aliphatic monoamines and diamines, histamine and ethanolamine, but not secondary and tertiary amines, quaternary ammonium salts or aromatic amines.
CAS REGISTRY NUMBER
COMMENTARY hide
55476-92-1
-
60496-14-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,6-diaminohexane + acceptor + H2O
?
show the reaction diagram
-
acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
-
-
?
1,7-diaminoheptane + acceptor + H2O
?
show the reaction diagram
-
acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
-
-
?
1-aminopentane + acceptor + H2O
pentanal + NH3 + reduced acceptor
show the reaction diagram
-
acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
-
-
?
2-phenylethylamine + acceptor + H2O
2-phenylacetaldehyde + NH3 + reduced acceptor
show the reaction diagram
-
acceptor: phenazine ethosulfate/2,6-dichlorophenolindophenol
-
-
?
benzylamine + acceptor + H2O
benzaldehyde + NH3 + reduced acceptor
show the reaction diagram
benzylamine + H2O + ferricyanide
benzaldehyde + NH3 + reduced ferricyanide
show the reaction diagram
-
-
-
-
?
butylamine + acceptor + H2O
butanal + NH3 + reduced acceptor
show the reaction diagram
ethylamine + acceptor + H2O
acetaldehyde + NH3 + reduced acceptor
show the reaction diagram
histamine + acceptor + H2O
? + NH3 + reduced acceptor
show the reaction diagram
-
-
-
-
?
methylamine + acceptor + H2O
formaldehyde + NH3 + reduced acceptor
show the reaction diagram
methylamine + acceptor + H2O
methanal + NH3 + reduced acceptor
show the reaction diagram
methylamine + amicyanin + H2O
formaldehyde + NH3 + reduced amicyanin
show the reaction diagram
-
-
-
-
?
methylamine + H2O + 2 amicyanin
formaldehyde + NH3 + 2 reduced amicyanin
show the reaction diagram
methylamine + H2O + 2,6-dichloroindophenol
formaldehyde + NH3 + reduced 2,6-dichloroindophenol
show the reaction diagram
-
-
-
-
r
methylamine + H2O + 2,6-dichloroindophenol + phenazine ethosulfate
formaldehyde + NH3 + reduced phenazine ethosulfate + ?
show the reaction diagram
-
-
-
-
r
methylamine + H2O + amicyanin
formaldehyde + ammonia + reduced amicyanin
show the reaction diagram
methylamine + H2O + amicyanin
formaldehyde + NH3 + reduced amicyanin
show the reaction diagram
-
-
-
?
methylamine + H2O + K3Fe(CN)6
formaldehyde + NH3 + reduced K3Fe(CN)6
show the reaction diagram
-
-
-
-
r
n-butylamine + H2O + ferricyanide
butanal + NH3 + reduced ferricyanide
show the reaction diagram
-
-
-
-
?
phenylethylamine + acceptor + H2O
phenylacetaldehyde + NH3 + reduced acceptor
show the reaction diagram
-
-
-
-
?
propylamine + acceptor + H2O
propionaldehyde + NH3 + reduced acceptor
show the reaction diagram
RCH2NH2 + acceptor + H2O
RCHO + NH3 + reduced acceptor
show the reaction diagram
tryptamine + acceptor + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
methylamine + H2O + 2 amicyanin
formaldehyde + NH3 + 2 reduced amicyanin
show the reaction diagram
methylamine + H2O + amicyanin
formaldehyde + NH3 + reduced amicyanin
show the reaction diagram
-
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine tryptophylquinone
heme c
quinoid cofactor
-
alpha subunit contains unknown quinoid cofactor
-
tryptophan tryptophylquinone
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
monovalent cations affect spectral properties and rate of gated electron transfer from reduced enzyme to electron acceptor
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
amicyanin mutant M98K
-
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
-
cyclopropylamine
-
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
hydroxylamine
-
-
phenylhydrazine
Semicarbazide
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benzylamine
-
activates sQH-AmDH
Dithionite
-
rapidly activates sQH-AmDH, activation process involves a reduction process
dithiothreitol
-
rapidly activates sQH-AmDH, activation process involves a reduction process
MauG
-
n-butylamine
-
activates sQH-AmDH
additional information
the gene which encodes MauG is located in the methylamine utilization (mau) gene cluster of several gram negative bacteria. The mau cluster contains the two structural genes for MADH as well as accessory proteins that are required for MADH biogenesis
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021 - 0.72
1,6-diaminohexane
0.007 - 0.38
1,7-Diaminoheptane
0.004 - 2.5
1-aminopentane
0.12
2,6-dichloroindophenol
-
-
0.007 - 0.87
Butylamine
0.019 - 9.2
ethylamine
0.78
K3Fe(CN)6
-
-
0.004 - 22.4
methylamine
0.014
phenazine ethosulfate
-
-
0.006 - 1.3
Propylamine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.4 - 43
1,6-diaminohexane
3.4 - 32
1,7-Diaminoheptane
3.4 - 20
1-aminopentane
1.5
2,6-dichloroindophenol
-
-
3.1
2-Phenylethylamine
-
pH 7.5, 30°C
3.8 - 22
benzylamine
4.2 - 34
Butylamine
4.5 - 24
ethylamine
15
K3Fe(CN)6
-
-
0.14 - 77
methylamine
7.1
phenazine ethosulfate
-
-
26
phenethylamine
-
-
3.1 - 27
Propylamine
additional information
additional information
-
turnover numbers for deuterated substrates
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the qhp genes are very widely distributed, not only in many Gram-negative species but also in a few Gram-positive bacteria, bacterial distribution of qhp and associated genes, overview. The subunits constituting QHNDH are encoded by ORF1 (alpha subunit), ORF4 (beta subunit), and ORF3 (gamma subunit). Of the other genes in the operon, ORF2 encodes an [Fe-S] cluster and S-adenosylmethionine (SAM)-binding protein, a member of the radical SAM superfamily, and ORF5 encodes a protein of approximately 22.5 kDa belonging to subfamily S8A of peptidase family S8 (the subtilisin family) with the conserved Asp/His/Ser catalytic triad characteristic of this subfamily
malfunction
the genes mauF and mauE are membrane proteins with no homology to characterized proteins, and are thought to be involved in transport of MADH subunits into the periplasm. Knocking out either gene leads to no detectable beta-subunit in the periplasm, and an unusual beta-subunit leader sequence is consistent with it being trafficked by a specific transporter. The loss of mauF and mauE additionally leads to a drastic reduction in alpha-subunit. The third gene, mauD, is homologous to disulfide isomerases, and is likely specific to the MADH beta-subunit, which has six disulfides. In the absence of mauD, periplasmic alpha-subunit levels are close to normal, but again there is no detectable beta-subunit implying that the disulfides are key to beta-subunit stability. When the final required gene, mauG, is knocked out, there are normal levels of MADH alpha- and beta-subunit in the periplasm, but no methylamine dehydrogenase activity is present. This has focused attention on the mauG gene product as a likely participant in TTQ biosynthesis
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHMH_PARDE
417
0
45440
Swiss-Prot
-
DHML_PARDE
188
0
20393
Swiss-Prot
-
DHMH_PARDE
417
0
45440
Swiss-Prot
other Location (Reliability: 1)
Q8VUT0_PARDE
512
0
54999
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
gel filtration
119000
36500
59500
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
alpha,beta, 1 * 59500 + 1 * 36500, SDS-PAGE
heterotetramer
heterotrimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
as MADH/amicyanin binary complex
-
crystals are grown in presence of 100 mM sodium citrate, pH 5.6, 18% PEG 4000 and 21% t-butyl alcohol. Complex of enzyme with the inhibitor phenylhydrazine determined at 1.7 A resolution
-
in complex with electron transfer protein amicyanin and with amicyanin mutant P52G. Model of electron transfer reaction between enzyme and amicyanin
-
macroseeding using a 9-to-1 mixture of monobasic sodium (3 M) and dibasic potassium (3 M) phosphate solutions as precipitant
-
MauG in complex with pre-methylamine dehydrogenase, hanging drop vapor diffusion method, using 23-25% (w/v) PEG 8000, 0.1 M sodium acetate, 0.1 M MES pH 6.4, at 20°C
MauG in complex with preMADH, X-ray diffraction structure determination and analysis at 2.1 resolution
MauG-pre-enzyme complex, hanging drop vapor diffusion method, using 0.1 M sodium acetate, 0.1 M MES pH 6.4, 22-26% PEG 8000
molecular dynamics simulations of the complex of redox proteins methylamine dehydrogenase and amicyanin to generate configurations over a duration of 40 ns in conjunction with an electron trnasfer pathway analysis. In the wild-type complex, the most frequently occurring molecular configurations afford superior electronic coupling due to the consistent presence of a water molecule hydrogen-bonded between the donor and acceptor sites. The water bridge function of nearby solvent-organizing residues by limiting the exchange of water molecules between the sterically constrained electron transfer region and the more turbulent surrounding bulk. When the water bridge is affected by a mutation, bulk solvent molecules disrupt it, resulting in reduced electronic coupling
-
preMADH complexed with MauG, X-ray diffraction structure determination and analysis at 2.1 A resolution
-
purified preenzyme pre-MADH in complex with activator mutant Q103N MauG, X-ray diffraction structure determination and analysis
sitting drop method, crystal structure of alphaF55A in complex with its electron acceptors, amicyanin and cytochrome c-551i. Little difference in the overal structure is seen, relative to the native complex. There are significant changes in the solvent content of the active site and substrate channel. Crystal structure of alphaF55A with phenylhydrazine covalently bound to tryptophan tryptophylquinone in the active site
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alphaF55A
alphaF55I
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
betaI107N
betaI107V
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
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiLoad Superdex 200 gel filtration
-
ion-exchange chromatography with DEAE-Toyopearl resin
-
nickel-affinity column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Rhodobacter sphaeroides
genes qhpA, qhpB, and qhpC encoding the alpha, beta, and gamma subunits of QHNDH, respectively. The structural genes encoding the three QHNDH subunits constitute an operon harboring six apparent open reading frames (ORFs) that are transcribed in a coordinated manner upon addition of amines to the culture medium. qhpADCBEF genes constitute a hexacistronic operon. DNA and amino acid sequence determination and analysis, and reverse transcription PCR expression analysis. Regulation of qhp genes, overview
heterologous expression of mutated alpha subunit in Rhodobacter sphaeroides
-
MADH is a heterotetramer consisting of two alpha subunits and two beta subunits which are encoded by mauB and mauA, respectively
PreMADH can be generated by expression of recombinant MADH in the background of a mauG deletion
-
recombinant expression of pre-MADH in Rhodobacter sphaeroides
the methylamine utilization (mau) gene cluster contains 11genes, two of which encode the 42.5 kDa alpha-(mauB) and the 14.2 kDa beta-subunits (mauA) of MADH, recombinant co-overexpression of genes mauAB in Rhodobacter sphaeroides in the presence of mauDEFG, the four genes required for MADH maturation results in an alpha2beta2 MADH protein that has no catalytic activity, because the protein contains all six beta-subunit disulfides, but has a partially synthesized TTQ cofactor with only a single -OH group added to the indole of betaTrp57 (betaTrp57-OH)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
an AraC family transcriptional regulator, ancoded by gene qhpR, activates expression of the qhp operon in response to the addition of n-butylamine to the culture medium
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
immobilized enzyme used as histamine biosensor
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team