D00039
type: Enzyme
active site residues resources: Colworth Medal Lecture. Enzymes in the quantum world.
active site residues resources: Active-site residues are critical for the folding and stability of methylamine dehydrogenase.
active site residues resources: Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase.
active site residues resources: P22619
active site residues resources: P22641
active site residues resources: 1mda
cath: Methylamine Dehydrogenase; Chain H
cath: Electron Transport Ethylamine Dehydrogenase
csa: 2bbk
ec: https://purl.uniprot.org/enzyme/1.4.9.1
kegg cofactor: Tryptophan tryptophylquinone
kegg enzyme: methylamine dehydrogenase (amicyanin)
kegg pathway: Methane metabolism
kegg product: Formaldehyde
kegg product: NH3
kegg product: Reduced amicyanin
kegg substrate: Methylamine
kegg substrate: H2O
kegg substrate: Amicyanin
macie: M0013
pdb: 1maeH
pdb: 1mafH
pdb: 1mdaH
pdb: 1mdaJ
pdb: 1mg2A
pdb: 1mg2E
pdb: 1mg2I
pdb: 1mg2M
pdb: 1mg3A
pdb: 1mg3E
pdb: 1mg3I
pdb: 1mg3M
pdb: 2bbkH
pdb: 2bbkJ
pdb: 2madH
pdb: 2mtaH
pdb: 1maeL
pdb: 1mafL
pdb: 1mdaL
pdb: 1mdaM
pdb: 1mg2B
pdb: 1mg2F
pdb: 1mg2J
pdb: 1mg2N
pdb: 1mg3B
pdb: 1mg3F
pdb: 1mg3J
pdb: 1mg3N
pdb: 2bbkL
pdb: 2bbkM
pdb: 2madL
pdb: 2mtaL
uniprot: P29894
uniprot: P23006
uniprot: P22619
uniprot: P22641
references: Purification, crystallization and preliminary X-ray investigation of quinoprotein methylamine dehydrogenase from Thiobacillus versutus.
references: Preliminary X-ray crystallographic studies of methylamine dehydrogenase and methylamine dehydrogenase--amicyanin complexes from Paracoccus denitrificans.
references: Structure of quinoprotein methylamine dehydrogenase at 2.25 A resolution.
references: Structure determination of quinoprotein methylamine dehydrogenase from Thiobacillus versutus.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00039#5
references: Methylamine oxidase from Arthrobacter P1 as a prototype of eukaryotic plasma amine oxidase and diamine oxidase.
references: Inhibition by cyclopropylamine of the quinoprotein methylamine dehydrogenase is mechanism-based and causes covalent cross-linking of alpha and beta subunits.
references: Direct electrochemistry of the enzyme, methylamine dehydrogenase, from bacterium W3A1.
references: Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase.
references: A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase.
references: The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans.
references: Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin.
references: Reactions of benzylamines with methylamine dehydrogenase. Evidence for a carbanionic reaction intermediate and reaction mechanism similar to eukaryotic quinoproteins.
references: Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor.
references: Three-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans determined by molecular replacement at 2.8 A resolution.
references: Preliminary crystal structure studies of a ternary electron transfer complex between a quinoprotein, a blue copper protein, and a c-type cytochrome.
references: Kinetic and thermodynamic analysis of a physiologic intermolecular electron-transfer reaction between methylamine dehydrogenase and amicyanin.
references: Kinetics of the reduction of wild-type and mutant cytochrome c-550 by methylamine dehydrogenase and amicyanin from Thiobacillus versutus.
references: Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i.
references: Binding of monovalent cations to methylamine dehydrogenase in the semiquinone state and its effect on electron transfer.
references: Evidence for a methylammonium-binding site on methylamine dehydrogenase of Thiobacillus versutus.
references: X-ray studies of quinoproteins.
references: Electron transfer from copper to heme within the methylamine dehydrogenase--amicyanin--cytochrome c-551i complex.

Methylamine Dehydrogenase; Chain H
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.130.10.10

Electron Transport Ethylamine Dehydrogenase
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/2.60.30.10

H2O
type: KeggSubstrate
compound type: H2O
references: KEGG:C00001
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Methane metabolism
type: KeggPathway
references: KEGG:MAP00680

Purification, crystallization and preliminary X-ray investigation of quinoprotein methylamine dehydrogenase from Thiobacillus versutus.
type: BibliographicResource
authors:
  item: Vellieux FM
  item: Frank J
  item: Swarte MB
  item: Groendijk H
  item: Duine JA
  item: Drenth J
  item: Hol WG
journal: Eur J Biochem
pages: 383-6
published year: 1986
volume: 154
references: http://www.ncbi.nlm.nih.gov/pubmed/3943535

A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase.
type: BibliographicResource
authors:
  item: McIntire WS
  item: Wemmer DE
  item: Chistoserdov A
  item: Lidstrom ME
journal: Science
pages: 817-24
published year: 1991
volume: 252
references: http://www.ncbi.nlm.nih.gov/pubmed/2028257

The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans.
type: BibliographicResource
authors:
  item: Chistoserdov AY
  item: Boyd J
  item: Mathews FS
  item: Lidstrom ME
journal: Biochem Biophys Res Commun
pages: 1181-9
published year: 1992
volume: 184
references: http://www.ncbi.nlm.nih.gov/pubmed/1590782

Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin.
type: BibliographicResource
authors:
  item: Chen L
  item: Vellieux FM
  item: et al
  item: Durley R
  item: Poliks BJ
  item: Hamada K
  item: Chen Z
  item: Mathews FS
  item: Davidson VL
  item: Satow Y
  item: Huizinga E
journal: Biochemistry
medline id: 92287919
pages: 4959-64
published year: 1992
volume: 31
references: http://www.ncbi.nlm.nih.gov/pubmed/1599920
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P29894
references: P22619
comment: X-RAY CRYSTALLOGRAPHY OF COMPLEX WITH AMICYANIN

Reactions of benzylamines with methylamine dehydrogenase. Evidence for a carbanionic reaction intermediate and reaction mechanism similar to eukaryotic quinoproteins.
type: BibliographicResource
authors:
  item: Davidson VL
  item: Jones LH
  item: Graichen ME
journal: Biochemistry
pages: 3385-90
published year: 1992
volume: 31
references: http://www.ncbi.nlm.nih.gov/pubmed/1554720

Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor.
type: BibliographicResource
authors:
  item: Huizinga EG
  item: van Zanten BA
  item: Duine JA
  item: Jongejan JA
  item: Huitema F
  item: Wilson KS
  item: Hol WG
journal: Biochemistry
pages: 9789-95
published year: 1992
volume: 31
references: http://www.ncbi.nlm.nih.gov/pubmed/1390754
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Three-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans determined by molecular replacement at 2.8 A resolution.
type: BibliographicResource
authors:
  item: Chen L
  item: Mathews FS
  item: Davidson VL
  item: Huizinga EG
  item: Vellieux FM
  item: Hol WG
journal: Proteins
medline id: 93028362
pages: 288-99
published year: 1992
volume: 14
references: http://www.ncbi.nlm.nih.gov/pubmed/1409575
references: P29894
references: P22619
comment: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)

Preliminary crystal structure studies of a ternary electron transfer complex between a quinoprotein, a blue copper protein, and a c-type cytochrome.
type: BibliographicResource
authors:
  item: Chen L
  item: Mathews FS
  item: Davidson VL
  item: Tegoni M
  item: Rivetti C
  item: Rossi GL
journal: Protein Sci
pages: 147-54
published year: 1993
volume: 2
references: http://www.ncbi.nlm.nih.gov/pubmed/8382992
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Kinetic and thermodynamic analysis of a physiologic intermolecular electron-transfer reaction between methylamine dehydrogenase and amicyanin.
type: BibliographicResource
authors:
  item: Brooks HB
  item: Davidson VL
journal: Biochemistry
pages: 5696-701
published year: 1994
volume: 33
references: http://www.ncbi.nlm.nih.gov/pubmed/8180195

Kinetics of the reduction of wild-type and mutant cytochrome c-550 by methylamine dehydrogenase and amicyanin from Thiobacillus versutus.
type: BibliographicResource
authors:
  item: Ubbink M
  item: Hunt NI
  item: Hill HA
  item: Canters GW
journal: Eur J Biochem
pages: 561-71
published year: 1994
volume: 222
references: http://www.ncbi.nlm.nih.gov/pubmed/8020493

Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i.
type: BibliographicResource
authors:
  item: Chen L
  item: Durley RC
  item: Mathews FS
  item: Davidson VL
journal: Science
medline id: 94188715
pages: 86-90
published year: 1994
volume: 264
references: http://www.ncbi.nlm.nih.gov/pubmed/8140419
references: P29894
references: P22619
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)

Preliminary X-ray crystallographic studies of methylamine dehydrogenase and methylamine dehydrogenase--amicyanin complexes from Paracoccus denitrificans.
type: BibliographicResource
authors:
  item: Chen L
  item: Lim LW
  item: Mathews FS
  item: Davidson VL
  item: Husain M
journal: J Mol Biol
pages: 1137-8
published year: 1988
volume: 203
references: http://www.ncbi.nlm.nih.gov/pubmed/3210240

Binding of monovalent cations to methylamine dehydrogenase in the semiquinone state and its effect on electron transfer.
type: BibliographicResource
authors:
  item: Gorren AC
  item: de Vries S
  item: Duine JA
journal: Biochemistry
pages: 9748-54
published year: 1995
volume: 34
references: http://www.ncbi.nlm.nih.gov/pubmed/7626645

Evidence for a methylammonium-binding site on methylamine dehydrogenase of Thiobacillus versutus.
type: BibliographicResource
authors:
  item: Gorren AC
  item: Moenne-Loccoz P
  item: Backes G
  item: de Vries S
  item: Sanders-Loehr J
  item: Duine JA
journal: Biochemistry
pages: 12926-31
published year: 1995
volume: 34
references: http://www.ncbi.nlm.nih.gov/pubmed/7548050

X-ray studies of quinoproteins.
type: BibliographicResource
authors:
  item: Mathews FS
journal: Methods Enzymol
pages: 191-216
published year: 1995
volume: 258
references: http://www.ncbi.nlm.nih.gov/pubmed/8524150

Electron transfer from copper to heme within the methylamine dehydrogenase--amicyanin--cytochrome c-551i complex.
type: BibliographicResource
authors:
  item: Davidson VL
  item: Jones LH
journal: Biochemistry
pages: 8120-5
published year: 1996
volume: 35
references: http://www.ncbi.nlm.nih.gov/pubmed/8679563

Electrostatic environment of the tryptophylquinone cofactor in methylamine dehydrogenase: evidence from resonance Raman spectroscopy of model compounds.
type: BibliographicResource
authors:
  item: Moenne-Loccoz P
  item: Nakamura N
  item: Itoh S
  item: Fukuzumi S
  item: Gorren AC
  item: Duine JA
  item: Sanders-Loehr J
journal: Biochemistry
pages: 4713-20
published year: 1996
volume: 35
references: http://www.ncbi.nlm.nih.gov/pubmed/8664261

Enzymatic and electron transfer activities in crystalline protein complexes.
type: BibliographicResource
authors:
  item: Merli A
  item: Brodersen DE
  item: Morini B
  item: Chen Z
  item: Durley RC
  item: Mathews FS
  item: Davidson VL
  item: Rossi GL
journal: J Biol Chem
pages: 9177-80
published year: 1996
volume: 271
references: http://www.ncbi.nlm.nih.gov/pubmed/8621571

Catalytic role of monovalent cations in the mechanism of proton transfer which gates an interprotein electron transfer reaction.
type: BibliographicResource
authors:
  item: Bishop GR
  item: Davidson VL
journal: Biochemistry
pages: 13586-92
published year: 1997
volume: 36
references: http://www.ncbi.nlm.nih.gov/pubmed/9354627
comment: X-ray crystallography

Factors which stabilize the methylamine dehydrogenase-amicyanin electron transfer protein complex revealed by site-directed mutagenesis.
type: BibliographicResource
authors:
  item: Davidson VL
  item: Jones LH
  item: Graichen ME
  item: Mathews FS
  item: Hosler JP
journal: Biochemistry
pages: 12733-8
published year: 1997
volume: 36
references: http://www.ncbi.nlm.nih.gov/pubmed/9335529

Crystallographic and spectroscopic studies of native, aminoquinol, and monovalent cation-bound forms of methylamine dehydrogenase from Methylobacterium extorquens AM1.
type: BibliographicResource
authors:
  item: Labesse G
  item: Ferrari D
  item: Chen ZW
  item: Rossi GL
  item: Kuusk V
  item: McIntire WS
  item: Mathews FS
journal: J Biol Chem
pages: 25703-12
published year: 1998
volume: 273
references: http://www.ncbi.nlm.nih.gov/pubmed/9748238

Redox properties of tryptophan tryptophylquinone enzymes. Correlation with structure and reactivity.
type: BibliographicResource
authors:
  item: Zhu Z
  item: Davidson VL
journal: J Biol Chem
pages: 14254-60
published year: 1998
volume: 273
references: http://www.ncbi.nlm.nih.gov/pubmed/9603931

Structure of quinoprotein methylamine dehydrogenase at 2.25 A resolution.
type: BibliographicResource
authors:
  item: Vellieux FM
  item: Hol WG
  item: Huitema F
  item: Groendijk H
  item: Kalk KH
  item: Jzn JF
  item: Jongejan JA
  item: Duine JA
  item: Petratos K
  item: Drenth J
journal: EMBO J
medline id: 90005420
pages: 2171-8
published year: 1989
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/2792083
references: P23006
references: P22641
comment: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS)

Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolution.
type: BibliographicResource
authors:
  item: Chen L
  item: Doi M
  item: Durley RC
  item: Chistoserdov AY
  item: Lidstrom ME
  item: Davidson VL
  item: Mathews FS
journal: J Mol Biol
pages: 131-49
published year: 1998
volume: 276
references: http://www.ncbi.nlm.nih.gov/pubmed/9514722
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Identification of a new reaction intermediate in the oxidation of methylamine dehydrogenase by amicyanin.
type: BibliographicResource
authors:
  item: Zhu Z
  item: Davidson VL
journal: Biochemistry
pages: 4862-7
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10200175

Amperometric detection of histamine with a methylamine dehydrogenase polypyrrole-based sensor.
type: BibliographicResource
authors:
  item: Zeng K
  item: Tachikawa H
  item: Zhu Z
  item: Davidson VL
journal: Anal Chem
pages: 2211-5
published year: 2000
volume: 72
references: http://www.ncbi.nlm.nih.gov/pubmed/10845365

Molecular basis for complex formation between methylamine dehydrogenase and amicyanin revealed by inverse mutagenesis of an interprotein salt bridge.
type: BibliographicResource
authors:
  item: Zhu Z
  item: Jones LH
  item: Graichen ME
  item: Davidson VL
journal: Biochemistry
pages: 8830-6
published year: 2000
volume: 39
references: http://www.ncbi.nlm.nih.gov/pubmed/10913294

Conversion of methylamine dehydrogenase to a long-chain amine dehydrogenase by mutagenesis of a single residue.
type: BibliographicResource
authors:
  item: Zhu Z
  item: Sun D
  item: Davidson VL
journal: Biochemistry
pages: 11184-6
published year: 2000
volume: 39
references: http://www.ncbi.nlm.nih.gov/pubmed/10985763

Characterization of the Tryptophyl-Semiquinone Catalytic Intermediate of Methylamine Dehydrogenase by Electron Spin-Echo Envelope Modulation Spectroscopy.
type: BibliographicResource
authors:
  item: Singh V
  item: Zhu Z
  item: Davidson VL.
  item: McCracken J
journal: J Am Chem Soc
pages: 931-8
published year: 2000
volume: 122

Methylamine dehydrogenase. Structure and function of electron transfer complexes.
type: BibliographicResource
authors:
  item: Davidson VL
journal: Subcell Biochem
pages: 119-43
published year: 2000
volume: 35
references: http://www.ncbi.nlm.nih.gov/pubmed/11192720

Re-engineering monovalent cation binding sites of methylamine dehydrogenase: effects on spectral properties and gated electron transfer.
type: BibliographicResource
authors:
  item: Sun D
  item: Davidson VL
journal: Biochemistry
pages: 12285-91
published year: 2001
volume: 40
references: http://www.ncbi.nlm.nih.gov/pubmed/11591147

QM/MM studies show substantial tunneling for the hydrogen-transfer reaction in methylamine dehydrogenase.
type: BibliographicResource
authors:
  item: Faulder PF
  item: Tresadern G
  item: Chohan KK
  item: Scrutton NS
  item: Sutcliffe MJ
  item: Hillier IH
  item: Burton NA
journal: J Am Chem Soc
pages: 8604-5
published year: 2001
volume: 123
references: http://www.ncbi.nlm.nih.gov/pubmed/11525672

Structure determination of quinoprotein methylamine dehydrogenase from Thiobacillus versutus.
type: BibliographicResource
authors:
  item: Vellieux FM
  item: Kalk KH
  item: Drenth J
  item: Hol WG
journal: Acta Crystallogr B
medline id: 91197438
pages: 806-23
published year: 1990
volume: 46
references: http://www.ncbi.nlm.nih.gov/pubmed/2085423
references: P23006
references: P22641
comment: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS)

Importance of barrier shape in enzyme-catalyzed reactions. Vibrationally assisted hydrogen tunneling in tryptophan tryptophylquinone-dependent amine dehydrogenases.
type: BibliographicResource
authors:
  item: Basran J
  item: Patel S
  item: Sutcliffe MJ
  item: Scrutton NS
journal: J Biol Chem
pages: 6234-42
published year: 2001
volume: 276
references: http://www.ncbi.nlm.nih.gov/pubmed/11087744

Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyanin.
type: BibliographicResource
authors:
  item: Sun D
  item: Chen ZW
  item: Mathews FS
  item: Davidson VL
journal: Biochemistry
pages: 13926-33
published year: 2002
volume: 41
references: http://www.ncbi.nlm.nih.gov/pubmed/12437349
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

A new conceptual framework for enzyme catalysis. Hydrogen tunnelling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes.
type: BibliographicResource
authors:
  item: Sutcliffe MJ
  item: Scrutton NS
journal: Eur J Biochem
pages: 3096-102
published year: 2002
volume: 269
references: http://www.ncbi.nlm.nih.gov/pubmed/12084049

Probing mechanisms of catalysis and electron transfer by methylamine dehydrogenase by site-directed mutagenesis of alpha Phe55.
type: BibliographicResource
authors:
  item: Davidson VL
journal: Biochim Biophys Acta
pages: 230-3
published year: 2003
volume: 1647
references: http://www.ncbi.nlm.nih.gov/pubmed/12686138

Catalysis and electron transfer in protein crystals: the binary and ternary complexes of methylamine dehydrogenase with electron acceptors.
type: BibliographicResource
authors:
  item: Ferrari D
  item: Merli A
  item: Peracchi A
  item: Di Valentin M
  item: Carbonera D
  item: Rossi GL
journal: Biochim Biophys Acta
pages: 337-42
published year: 2003
volume: 1647
references: http://www.ncbi.nlm.nih.gov/pubmed/12686155

Direct dynamics calculations of reaction rate and kinetic isotope effects in enzyme catalysed reactions.
type: BibliographicResource
authors:
  item: Tresadern G
  item: Nunez S
  item: Faulder PF
  item: Wang H
  item: Hillier IH
  item: Burton NA
journal: Faraday Discuss
pages: 223-42; discussion 269-82
published year: 2003
volume: 122
references: http://www.ncbi.nlm.nih.gov/pubmed/12555860

Evidence for substrate activation of electron transfer from methylamine dehydrogenase to amicyanin.
type: BibliographicResource
authors:
  item: Davidson VL
  item: Sun D
journal: J Am Chem Soc
pages: 3224-5
published year: 2003
volume: 125
references: http://www.ncbi.nlm.nih.gov/pubmed/12630872

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00039#5
type: BibliographicResource
title: Cloning and sequencing of the structural gene for the small subunit of methylamine dehydrogenase from Methylobacterium extorquens AM1: evidence for two tryptophan residues involved in the active center.
authors:
  item: Chistoserdov AY
  item: Tsygankov YD
  item: Lidstrom ME
journal: Biochem Biophys Res Commun
pages: 211-6
published year: 1990
volume: 172
references: http://www.ncbi.nlm.nih.gov/pubmed/2121141

Methylamine oxidase from Arthrobacter P1 as a prototype of eukaryotic plasma amine oxidase and diamine oxidase.
type: BibliographicResource
authors:
  item: McIntire WS
  item: Dooley DM
  item: McGuirl MA
  item: Cote CE
  item: Bates JL
journal: J Neural Transm Suppl
pages: 315-8
published year: 1990
volume: 32
references: http://www.ncbi.nlm.nih.gov/pubmed/1965196

Inhibition by cyclopropylamine of the quinoprotein methylamine dehydrogenase is mechanism-based and causes covalent cross-linking of alpha and beta subunits.
type: BibliographicResource
authors:
  item: Davidson VL
  item: Jones LH
journal: Biochemistry
pages: 1924-8
published year: 1991
volume: 30
references: http://www.ncbi.nlm.nih.gov/pubmed/1993204

Direct electrochemistry of the enzyme, methylamine dehydrogenase, from bacterium W3A1.
type: BibliographicResource
authors:
  item: Burrows AL
  item: Hill HA
  item: Leese TA
  item: Mcintire WS
  item: Nakayama H
  item: Sanghera GS
journal: Eur J Biochem
pages: 73-8
published year: 1991
volume: 199
references: http://www.ncbi.nlm.nih.gov/pubmed/2065680

Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase.
type: BibliographicResource
authors:
  item: Chen LY
  item: Mathews FS
  item: Davidson VL
  item: Huizinga EG
  item: Vellieux FM
  item: Duine JA
  item: Hol WG
journal: FEBS Lett
pages: 163-6
published year: 1991
volume: 287
references: http://www.ncbi.nlm.nih.gov/pubmed/1879526

Colworth Medal Lecture. Enzymes in the quantum world.
type: BibliographicResource
authors:
  item: Scrutton NS
journal: Biochem Soc Trans
pages: 767-79
published year: 1999
volume: 27
references: http://www.ncbi.nlm.nih.gov/pubmed/10830100

Active-site residues are critical for the folding and stability of methylamine dehydrogenase.
type: BibliographicResource
authors:
  item: Sun D
  item: Jones LH
  item: Mathews FS
  item: Davidson VL
journal: Protein Eng
pages: 675-81
published year: 2001
volume: 14
references: http://www.ncbi.nlm.nih.gov/pubmed/11707614

Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase.
type: BibliographicResource
authors:
  item: Wang Y
  item: Sun D
  item: Davidson VL
journal: J Biol Chem
pages: 4119-22
published year: 2002
volume: 277
references: http://www.ncbi.nlm.nih.gov/pubmed/11733518

1mdaL
type: Pdb
catalytic residue: ;ASP 76;TYR 117;
modified residue: TRQ 57;TRP 107(Tryptophan tryptophylquinone)
references: 1mda
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mda
comment: mutant D32A, T120S

1mdaM
type: Pdb
catalytic residue: ;ASP 76;TYR 117;
modified residue: TRQ 57;TRP 107(Tryptophan tryptophylquinone)
references: 1mda
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mda
comment: mutant D32A, T120S

1mg2B
type: Pdb
catalytic residue: ASP 32;ASP 76;TYR 119;THR 122
modified residue: TRQ 57;TRP 108(Tryptophan tryptophylquinone)
references: 1mg2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg2

1mg2F
type: Pdb
catalytic residue: ASP 32;ASP 76;TYR 119;THR 122
modified residue: TRQ 57;TRP 108(Tryptophan tryptophylquinone)
references: 1mg2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg2

1mg2J
type: Pdb
catalytic residue: ASP 32;ASP 76;TYR 119;THR 122
modified residue: TRQ 57;TRP 108(Tryptophan tryptophylquinone)
references: 1mg2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg2

1mg2N
type: Pdb
catalytic residue: ASP 32;ASP 76;TYR 119;THR 122
modified residue: TRQ 57;TRP 108(Tryptophan tryptophylquinone)
references: 1mg2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg2

2mtaL
type: Pdb
catalytic residue: ASP 32;ASP 76;TYR 119;THR 122
modified residue: TRQ 57;TRP 108(Tryptophan tryptophylquinone)
references: 2mta
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2mta

1mg3B
type: Pdb
catalytic residue: ASP 32;ASP 76;TYR 119;THR 122
modified residue: TRW 57;TRP 108(Tryptophan tryptophylquinone-phenylhydrazine)
references: 1mg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg3

1mg3F
type: Pdb
catalytic residue: ASP 32;ASP 76;TYR 119;THR 122
modified residue: TRW 57;TRP 108(Tryptophan tryptophylquinone-phenylhydrazine)
references: 1mg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg3

1mg3J
type: Pdb
catalytic residue: ASP 32;ASP 76;TYR 119;THR 122
modified residue: TRW 57;TRP 108(Tryptophan tryptophylquinone-phenylhydrazine)
references: 1mg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg3

1mg3N
type: Pdb
catalytic residue: ASP 32;ASP 76;TYR 119;THR 122
modified residue: TRW 57;TRP 108(Tryptophan tryptophylquinone-phenylhydrazine)
references: 1mg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg3

2bbkL
type: Pdb
catalytic residue: ASP 32;ASP 76;TYR 119;THR 122
modified residue: TRP 57;TRP 108(Tryptophan tryptophylquinone)
references: 2bbk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bbk

2bbkM
type: Pdb
catalytic residue: ASP 32;ASP 76;TYR 119;THR 122
modified residue: TRP 57;TRP 108(Tryptophan tryptophylquinone)
references: 2bbk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bbk

2madL
type: Pdb
catalytic residue: ASP 32;ASP 76;TYR 119;THR 122
modified residue: TRP 57;TRP 108(Tryptophan tryptophylquinone)
references: 2mad
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2mad

1maeL
type: Pdb
catalytic residue: ASP 32;ASP 76;TYR 119;THR 122
modified residue: TRP 57;TRP 108(Tryptophan tryptophylquinone)
references: 1mae
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mae

1mafL
type: Pdb
catalytic residue: ASP 32;ASP 76;TYR 119;THR 122
modified residue: TRP 57;TRP 108(Tryptophan tryptophylquinone)
references: 1maf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1maf

1mg2A
type: Pdb
references: 1mg2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg2
comment: mutant F55A

1mg2E
type: Pdb
references: 1mg2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg2
comment: mutant F55A

1mg2I
type: Pdb
references: 1mg2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg2
comment: mutant F55A

1mg2M
type: Pdb
references: 1mg2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg2
comment: mutant F55A

1mg3A
type: Pdb
references: 1mg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg3
comment: mutant F55A

1mg3E
type: Pdb
references: 1mg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg3
comment: mutant F55A

1mg3I
type: Pdb
references: 1mg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg3
comment: mutant F55A

1mg3M
type: Pdb
references: 1mg3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mg3
comment: mutant F55A

Amicyanin
type: KeggSubstrate
compound type: heavy metal
compound type: peptide/protein
references: KEGG:C19671

Tryptophan tryptophylquinone
type: KeggCofactor
compound type: amino acids
compound type: aromatic ring (only carbon atom)
compound type: aromatic ring (with nitrogen atoms)
references: KEGG:L00002
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NH3
type: KeggProduct
compound type: amine group
compound type: organic ion
references: KEGG:C00014
references: CHEBI:16134
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Formaldehyde
type: KeggProduct
compound type: carbohydrate
references: KEGG:C00067
references: CHEBI:16842
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Methylamine
type: KeggSubstrate
compound type: amine group
references: KEGG:C00218
references: CHEBI:16830
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Reduced amicyanin
type: KeggProduct
compound type: heavy metal
compound type: peptide/protein
references: KEGG:C19672

amine dehydrogenase
type: KeggEnzyme

primary-amine dehydrogenase
type: KeggEnzyme

amine: (acceptor) oxidoreductase (deaminating)
type: KeggEnzyme

primary-amine:(acceptor) oxidoreductase (deaminating)
type: KeggEnzyme

Analogue
compound: Tryptophan tryptophylquinone
ligand het code: TRP_108-TRW_57
pdb: 1mg3B

Analogue
compound: Tryptophan tryptophylquinone
ligand het code: TRP_108-TRW_57
pdb: 1mg3F

Analogue
compound: Tryptophan tryptophylquinone
ligand het code: TRP_108-TRW_57
pdb: 1mg3J

Analogue
compound: Tryptophan tryptophylquinone
ligand het code: TRP_108-TRW_57
pdb: 1mg3N

IntermediateAnalogue
ligand het code: TRP_108-TRW_57
pdb: 1mg3B

IntermediateAnalogue
ligand het code: TRP_108-TRW_57
pdb: 1mg3F

IntermediateAnalogue
ligand het code: TRP_108-TRW_57
pdb: 1mg3J

IntermediateAnalogue
ligand het code: TRP_108-TRW_57
pdb: 1mg3N

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig.6

ReferenceForCatalyticMechanism
reference index: 10
reference section: Scheme 1, Scheme 2, Scheme 3, p.821-823

ReferenceForCatalyticMechanism
reference index: 12
reference section: p.4962-4964

ReferenceForCatalyticMechanism
reference index: 13
reference section: Fig.6, p.3389-3390

ReferenceForCatalyticMechanism
reference index: 14

ReferenceForCatalyticMechanism
reference index: 16
reference section: p.151-152

ReferenceForCatalyticMechanism
reference index: 17
reference section: Fig.5, p.5697-5701

ReferenceForCatalyticMechanism
reference index: 19
reference section: Fig.4, p.89

ReferenceForCatalyticMechanism
reference index: 20
reference section: Fig.3

ReferenceForCatalyticMechanism
reference index: 26
reference section: Fig.1, Fig.6

ReferenceForCatalyticMechanism
reference index: 30
reference section: Fig.13, p.144-146

ReferenceForCatalyticMechanism
reference index: 31
reference section: Scheme 2

ReferenceForCatalyticMechanism
reference index: 32
reference section: Fig.5, p.4865-4867

ReferenceForCatalyticMechanism
reference index: 36
reference section: Fig.2, p.933

ReferenceForCatalyticMechanism
reference index: 37
reference section: Fig.2, Fig.7, Fig.8, p.121-123, p.131-138

ReferenceForCatalyticMechanism
reference index: 38
reference section: Fig.2

ReferenceForCatalyticMechanism
reference index: 39
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 40
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 41
reference section: p.680-681

ReferenceForCatalyticMechanism
reference index: 42
reference section: Fig.2, Fig.7

ReferenceForCatalyticMechanism
reference index: 43
reference section: Fig.2, p.3098-3099

ReferenceForCatalyticMechanism
reference index: 45

ReferenceForCatalyticMechanism
reference index: 47
reference section: Fig.3, Fig.6, p.228-230

ReferenceForCatalyticMechanism
reference index: 48
reference section: Fig.1, p.3224