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
-
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
- 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
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
1.4.9.1 methylamine dehydrogenase (amicyanin)Advanced search results
results (
results (Reference
top
Reference on EC 1.4.9.1 - methylamine dehydrogenase (amicyanin)
Please use the Reference Search for a specific query.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
-
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
-
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
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.
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
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
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
-
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
-
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
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
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
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
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
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
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
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
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
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
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
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
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)
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)
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
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)
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)
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)
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)
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
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)
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)
-
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)
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)
-
html completed
