DB code: D00039

CATH domain 2.130.10.10 : Methylamine Dehydrogenase; Chain H
2.60.30.10 : Electron Transport Ethylamine Dehydrogenase Catalytic domain
E.C. 1.4.9.1
CSA 2bbk
M-CSA 2bbk
MACiE M0013

CATH domain Related DB codes (homologues)
2.130.10.10 : Methylamine Dehydrogenase; Chain H S00852 M00329

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P29894 Methylamine dehydrogenase heavy chain
MADH
EC 1.4.9.1
Methylamine dehydrogenase (amicyanin)
PF06433 (Me-amine-dh_H)
[Graphical View]
P23006 Methylamine dehydrogenase heavy chain
MADH
EC 1.4.9.1
Methylamine dehydrogenase (amicyanin)
PF06433 (Me-amine-dh_H)
[Graphical View]
P22619 Methylamine dehydrogenase light chain
MADH
EC 1.4.9.1
Methylamine dehydrogenase (amicyanin)
PF02975 (Me-amine-dh_L)
[Graphical View]
P22641 Methylamine dehydrogenase light chain
MADH
EC 1.4.9.1
Methylamine dehydrogenase (amicyanin)
Methylamine dehydrogenase subunit beta
PF02975 (Me-amine-dh_L)
[Graphical View]

KEGG enzyme name
methylamine dehydrogenase (amicyanin)
amine dehydrogenase
primary-amine dehydrogenase
amine: (acceptor) oxidoreductase (deaminating)
primary-amine:(acceptor) oxidoreductase (deaminating)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P29894 DHMH_PARDE Methylamine + H(2)O + amicyanin = formaldehyde + ammonia + reduced amicyanin. Tetramer of two light and two heavy chains. Periplasm.
P23006 DHMH_PARVE Methylamine + H(2)O + amicyanin = formaldehyde + ammonia + reduced amicyanin. Tetramer of two light and two heavy chains. Periplasm.
P22619 DHML_PARDE Methylamine + H(2)O + amicyanin = formaldehyde + ammonia + reduced amicyanin. Heterotetramer of two light and two heavy chains. Periplasm. Contains 1 tryptophan tryptophylquinone per subunit.
P22641 DHML_PARVE Methylamine + H(2)O + amicyanin = formaldehyde + ammonia + reduced amicyanin. Heterotetramer of two light and two heavy chains. Periplasm. Contains 1 tryptophan tryptophylquinone per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00680 Methane metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id L00002 C00218 C00001 C19671 C00067 C00014 C19672
E.C.
Compound Tryptophan tryptophylquinone Methylamine H2O Amicyanin Formaldehyde NH3 Reduced amicyanin Aminoquinol TTQ
Type amino acids,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms) amine group H2O heavy metal,peptide/protein carbohydrate amine group,organic ion heavy metal,peptide/protein
ChEBI 16830
15377
16842
16134
PubChem 101916295
6329
22247451
962
712
222
1maeH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mafH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mdaH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mdaJ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mg2A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mg2E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mg2I Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mg2M Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mg3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mg3E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mg3I Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mg3M Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2bbkH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2bbkJ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2madH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2mtaH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1maeL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mafL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mdaL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:TRP_107-TRQ_57 Unbound Bound:_CU(chain A) Unbound Unbound Unbound Unbound
1mdaM Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:TRP_107-TRQ_57 Unbound Bound:_CU(chain B) Unbound Unbound Unbound Unbound
1mg2B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:TRP_108-TRQ_57 Unbound Bound:_CU(chain C) Unbound Unbound Unbound Unbound
1mg2F Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:TRP_108-TRQ_57 Unbound Bound:_CU(chain G) Unbound Unbound Unbound Unbound
1mg2J Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:TRP_108-TRQ_57 Unbound Bound:_CU(chain K) Unbound Unbound Unbound Unbound
1mg2N Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:TRP_108-TRQ_57 Unbound Bound:_CU(chain O) Unbound Unbound Unbound Unbound
1mg3B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:TRP_108-TRW_57 Unbound Bound:_CU(chain C) Unbound Unbound Unbound Intermediate-analogue:TRP_108-TRW_57
1mg3F Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:TRP_108-TRW_57 Unbound Bound:_CU(chain G) Unbound Unbound Unbound Intermediate-analogue:TRP_108-TRW_57
1mg3J Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:TRP_108-TRW_57 Unbound Bound:_CU(chain K) Unbound Unbound Unbound Intermediate-analogue:TRP_108-TRW_57
1mg3N Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:TRP_108-TRW_57 Unbound Bound:_CU(chain O) Unbound Unbound Unbound Intermediate-analogue:TRP_108-TRW_57
2bbkL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:TRP_108-TRP_57 Unbound Unbound Unbound Unbound Unbound Unbound
2bbkM Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:TRP_108-TRP_57 Unbound Unbound Unbound Unbound Unbound Unbound
2madL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:TRP_108-TRP_57 Unbound Unbound Unbound Unbound Unbound Unbound
2mtaL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:TRP_108-TRQ_57 Unbound Bound:_CU(chain A) Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1mda & Swiss-prot;P22619, P22641 & literature [30], [40], [43]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1maeH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1mafH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1mdaH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1mdaJ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1mg2A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant F55A
1mg2E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant F55A
1mg2I Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant F55A
1mg2M Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant F55A
1mg3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant F55A
1mg3E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant F55A
1mg3I Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant F55A
1mg3M Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant F55A
2bbkH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2bbkJ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2madH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2mtaH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1maeL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 32;ASP 76;TYR 119;THR 122 TRP 57;TRP 108(Tryptophan tryptophylquinone)
1mafL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 32;ASP 76;TYR 119;THR 122 TRP 57;TRP 108(Tryptophan tryptophylquinone)
1mdaL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;ASP 76;TYR 117; TRQ 57;TRP 107(Tryptophan tryptophylquinone) mutant D32A, T120S
1mdaM Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;ASP 76;TYR 117; TRQ 57;TRP 107(Tryptophan tryptophylquinone) mutant D32A, T120S
1mg2B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 32;ASP 76;TYR 119;THR 122 TRQ 57;TRP 108(Tryptophan tryptophylquinone)
1mg2F Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 32;ASP 76;TYR 119;THR 122 TRQ 57;TRP 108(Tryptophan tryptophylquinone)
1mg2J Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 32;ASP 76;TYR 119;THR 122 TRQ 57;TRP 108(Tryptophan tryptophylquinone)
1mg2N Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 32;ASP 76;TYR 119;THR 122 TRQ 57;TRP 108(Tryptophan tryptophylquinone)
1mg3B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 32;ASP 76;TYR 119;THR 122 TRW 57;TRP 108(Tryptophan tryptophylquinone-phenylhydrazine)
1mg3F Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 32;ASP 76;TYR 119;THR 122 TRW 57;TRP 108(Tryptophan tryptophylquinone-phenylhydrazine)
1mg3J Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 32;ASP 76;TYR 119;THR 122 TRW 57;TRP 108(Tryptophan tryptophylquinone-phenylhydrazine)
1mg3N Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 32;ASP 76;TYR 119;THR 122 TRW 57;TRP 108(Tryptophan tryptophylquinone-phenylhydrazine)
2bbkL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 32;ASP 76;TYR 119;THR 122 TRP 57;TRP 108(Tryptophan tryptophylquinone)
2bbkM Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 32;ASP 76;TYR 119;THR 122 TRP 57;TRP 108(Tryptophan tryptophylquinone)
2madL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 32;ASP 76;TYR 119;THR 122 TRP 57;TRP 108(Tryptophan tryptophylquinone)
2mtaL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 32;ASP 76;TYR 119;THR 122 TRQ 57;TRP 108(Tryptophan tryptophylquinone)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[7]
Fig.6
[10]
Scheme 1, Scheme 2, Scheme 3, p.821-823
[12]
p.4962-4964
[13]
Fig.6, p.3389-3390
[14]
[16]
p.151-152
[17]
Fig.5, p.5697-5701
[19]
Fig.4, p.89
[20]
Fig.3
[26]
Fig.1, Fig.6
[30]
Fig.13, p.144-146
[31]
Scheme 2
[32]
Fig.5, p.4865-4867
[36]
Fig.2, p.933
[37]
Fig.2, Fig.7, Fig.8, p.121-123, p.131-138
[38]
Fig.2
[39]
Fig.1
[40]
Fig.1
[41]
p.680-681
[42]
Fig.2, Fig.7
[43]
Fig.2, p.3098-3099
[45]
[47]
Fig.3, Fig.6, p.228-230
[48]
Fig.1, p.3224

References
[1]
Resource
Comments
Medline ID
PubMed ID 3943535
Journal Eur J Biochem
Year 1986
Volume 154
Pages 383-6
Authors Vellieux FM, Frank J, Swarte MB, Groendijk H, Duine JA, Drenth J, Hol WG
Title Purification, crystallization and preliminary X-ray investigation of quinoprotein methylamine dehydrogenase from Thiobacillus versutus.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 3210240
Journal J Mol Biol
Year 1988
Volume 203
Pages 1137-8
Authors Chen L, Lim LW, Mathews FS, Davidson VL, Husain M
Title Preliminary X-ray crystallographic studies of methylamine dehydrogenase and methylamine dehydrogenase--amicyanin complexes from Paracoccus denitrificans.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS)
Medline ID 90005420
PubMed ID 2792083
Journal EMBO J
Year 1989
Volume 8
Pages 2171-8
Authors Vellieux FM, Huitema F, Groendijk H, Kalk KH, Jzn JF, Jongejan JA, Duine JA, Petratos K, Drenth J, Hol WG
Title Structure of quinoprotein methylamine dehydrogenase at 2.25 A resolution.
Related PDB
Related UniProtKB P23006 P22641
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS)
Medline ID 91197438
PubMed ID 2085423
Journal Acta Crystallogr B
Year 1990
Volume 46
Pages 806-23
Authors Vellieux FM, Kalk KH, Drenth J, Hol WG
Title Structure determination of quinoprotein methylamine dehydrogenase from Thiobacillus versutus.
Related PDB
Related UniProtKB P23006 P22641
[5]
Resource
Comments
Medline ID
PubMed ID 2121141
Journal Biochem Biophys Res Commun
Year 1990
Volume 172
Pages 211-6
Authors Chistoserdov AY, Tsygankov YD, Lidstrom ME
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.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 1965196
Journal J Neural Transm Suppl
Year 1990
Volume 32
Pages 315-8
Authors McIntire WS, Dooley DM, McGuirl MA, Cote CE, Bates JL
Title Methylamine oxidase from Arthrobacter P1 as a prototype of eukaryotic plasma amine oxidase and diamine oxidase.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 1993204
Journal Biochemistry
Year 1991
Volume 30
Pages 1924-8
Authors Davidson VL, Jones LH
Title Inhibition by cyclopropylamine of the quinoprotein methylamine dehydrogenase is mechanism-based and causes covalent cross-linking of alpha and beta subunits.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 2065680
Journal Eur J Biochem
Year 1991
Volume 199
Pages 73-8
Authors Burrows AL, Hill HA, Leese TA, Mcintire WS, Nakayama H, Sanghera GS
Title Direct electrochemistry of the enzyme, methylamine dehydrogenase, from bacterium W3A1.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 1879526
Journal FEBS Lett
Year 1991
Volume 287
Pages 163-6
Authors Chen LY, Mathews FS, Davidson VL, Huizinga EG, Vellieux FM, Duine JA, Hol WG
Title Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 2028257
Journal Science
Year 1991
Volume 252
Pages 817-24
Authors McIntire WS, Wemmer DE, Chistoserdov A, Lidstrom ME
Title A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 1590782
Journal Biochem Biophys Res Commun
Year 1992
Volume 184
Pages 1181-9
Authors Chistoserdov AY, Boyd J, Mathews FS, Lidstrom ME
Title The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans.
Related PDB
Related UniProtKB
[12]
Resource
Comments X-RAY CRYSTALLOGRAPHY OF COMPLEX WITH AMICYANIN
Medline ID 92287919
PubMed ID 1599920
Journal Biochemistry
Year 1992
Volume 31
Pages 4959-64
Authors Chen L, Durley R, Poliks BJ, Hamada K, Chen Z, Mathews FS, Davidson VL, Satow Y, Huizinga E, Vellieux FM, et al
Title Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin.
Related PDB 1mda
Related UniProtKB P29894 P22619
[13]
Resource
Comments
Medline ID
PubMed ID 1554720
Journal Biochemistry
Year 1992
Volume 31
Pages 3385-90
Authors Davidson VL, Jones LH, Graichen ME
Title Reactions of benzylamines with methylamine dehydrogenase. Evidence for a carbanionic reaction intermediate and reaction mechanism similar to eukaryotic quinoproteins.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 1390754
Journal Biochemistry
Year 1992
Volume 31
Pages 9789-95
Authors Huizinga EG, van Zanten BA, Duine JA, Jongejan JA, Huitema F, Wilson KS, Hol WG
Title Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor.
Related PDB 1mae 1maf 2mad
Related UniProtKB
[15]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)
Medline ID 93028362
PubMed ID 1409575
Journal Proteins
Year 1992
Volume 14
Pages 288-99
Authors Chen L, Mathews FS, Davidson VL, Huizinga EG, Vellieux FM, Hol WG
Title Three-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans determined by molecular replacement at 2.8 A resolution.
Related PDB
Related UniProtKB P29894 P22619
[16]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8382992
Journal Protein Sci
Year 1993
Volume 2
Pages 147-54
Authors Chen L, Mathews FS, Davidson VL, Tegoni M, Rivetti C, Rossi GL
Title Preliminary crystal structure studies of a ternary electron transfer complex between a quinoprotein, a blue copper protein, and a c-type cytochrome.
Related PDB 2mta
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 8180195
Journal Biochemistry
Year 1994
Volume 33
Pages 5696-701
Authors Brooks HB, Davidson VL
Title Kinetic and thermodynamic analysis of a physiologic intermolecular electron-transfer reaction between methylamine dehydrogenase and amicyanin.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 8020493
Journal Eur J Biochem
Year 1994
Volume 222
Pages 561-71
Authors Ubbink M, Hunt NI, Hill HA, Canters GW
Title Kinetics of the reduction of wild-type and mutant cytochrome c-550 by methylamine dehydrogenase and amicyanin from Thiobacillus versutus.
Related PDB
Related UniProtKB
[19]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
Medline ID 94188715
PubMed ID 8140419
Journal Science
Year 1994
Volume 264
Pages 86-90
Authors Chen L, Durley RC, Mathews FS, Davidson VL
Title Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i.
Related PDB
Related UniProtKB P29894 P22619
[20]
Resource
Comments
Medline ID
PubMed ID 7626645
Journal Biochemistry
Year 1995
Volume 34
Pages 9748-54
Authors Gorren AC, de Vries S, Duine JA
Title Binding of monovalent cations to methylamine dehydrogenase in the semiquinone state and its effect on electron transfer.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 7548050
Journal Biochemistry
Year 1995
Volume 34
Pages 12926-31
Authors Gorren AC, Moenne-Loccoz P, Backes G, de Vries S, Sanders-Loehr J, Duine JA
Title Evidence for a methylammonium-binding site on methylamine dehydrogenase of Thiobacillus versutus.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 8524150
Journal Methods Enzymol
Year 1995
Volume 258
Pages 191-216
Authors Mathews FS
Title X-ray studies of quinoproteins.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 8679563
Journal Biochemistry
Year 1996
Volume 35
Pages 8120-5
Authors Davidson VL, Jones LH
Title Electron transfer from copper to heme within the methylamine dehydrogenase--amicyanin--cytochrome c-551i complex.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 8664261
Journal Biochemistry
Year 1996
Volume 35
Pages 4713-20
Authors Moenne-Loccoz P, Nakamura N, Itoh S, Fukuzumi S, Gorren AC, Duine JA, Sanders-Loehr J
Title Electrostatic environment of the tryptophylquinone cofactor in methylamine dehydrogenase: evidence from resonance Raman spectroscopy of model compounds.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 8621571
Journal J Biol Chem
Year 1996
Volume 271
Pages 9177-80
Authors Merli A, Brodersen DE, Morini B, Chen Z, Durley RC, Mathews FS, Davidson VL, Rossi GL
Title Enzymatic and electron transfer activities in crystalline protein complexes.
Related PDB
Related UniProtKB
[26]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9354627
Journal Biochemistry
Year 1997
Volume 36
Pages 13586-92
Authors Bishop GR, Davidson VL
Title Catalytic role of monovalent cations in the mechanism of proton transfer which gates an interprotein electron transfer reaction.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 9335529
Journal Biochemistry
Year 1997
Volume 36
Pages 12733-8
Authors Davidson VL, Jones LH, Graichen ME, Mathews FS, Hosler JP
Title Factors which stabilize the methylamine dehydrogenase-amicyanin electron transfer protein complex revealed by site-directed mutagenesis.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 9748238
Journal J Biol Chem
Year 1998
Volume 273
Pages 25703-12
Authors Labesse G, Ferrari D, Chen ZW, Rossi GL, Kuusk V, McIntire WS, Mathews FS
Title Crystallographic and spectroscopic studies of native, aminoquinol, and monovalent cation-bound forms of methylamine dehydrogenase from Methylobacterium extorquens AM1.
Related PDB
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 9603931
Journal J Biol Chem
Year 1998
Volume 273
Pages 14254-60
Authors Zhu Z, Davidson VL
Title Redox properties of tryptophan tryptophylquinone enzymes. Correlation with structure and reactivity.
Related PDB
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 9514722
Journal J Mol Biol
Year 1998
Volume 276
Pages 131-49
Authors Chen L, Doi M, Durley RC, Chistoserdov AY, Lidstrom ME, Davidson VL, Mathews FS
Title Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolution.
Related PDB 2bbk
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 10830100
Journal Biochem Soc Trans
Year 1999
Volume 27
Pages 767-79
Authors Scrutton NS
Title Colworth Medal Lecture. Enzymes in the quantum world.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 10200175
Journal Biochemistry
Year 1999
Volume 38
Pages 4862-7
Authors Zhu Z, Davidson VL
Title Identification of a new reaction intermediate in the oxidation of methylamine dehydrogenase by amicyanin.
Related PDB
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 10845365
Journal Anal Chem
Year 2000
Volume 72
Pages 2211-5
Authors Zeng K, Tachikawa H, Zhu Z, Davidson VL
Title Amperometric detection of histamine with a methylamine dehydrogenase polypyrrole-based sensor.
Related PDB
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 10913294
Journal Biochemistry
Year 2000
Volume 39
Pages 8830-6
Authors Zhu Z, Jones LH, Graichen ME, Davidson VL
Title Molecular basis for complex formation between methylamine dehydrogenase and amicyanin revealed by inverse mutagenesis of an interprotein salt bridge.
Related PDB
Related UniProtKB
[35]
Resource
Comments
Medline ID
PubMed ID 10985763
Journal Biochemistry
Year 2000
Volume 39
Pages 11184-6
Authors Zhu Z, Sun D, Davidson VL
Title Conversion of methylamine dehydrogenase to a long-chain amine dehydrogenase by mutagenesis of a single residue.
Related PDB
Related UniProtKB
[36]
Resource
Comments
Medline ID
PubMed ID
Journal J Am Chem Soc
Year 2000
Volume 122
Pages 931-8
Authors Singh V, Zhu Z, Davidson VL., McCracken J
Title Characterization of the Tryptophyl-Semiquinone Catalytic Intermediate of Methylamine Dehydrogenase by Electron Spin-Echo Envelope Modulation Spectroscopy.
Related PDB
Related UniProtKB
[37]
Resource
Comments
Medline ID
PubMed ID 11192720
Journal Subcell Biochem
Year 2000
Volume 35
Pages 119-43
Authors Davidson VL
Title Methylamine dehydrogenase. Structure and function of electron transfer complexes.
Related PDB
Related UniProtKB
[38]
Resource
Comments
Medline ID
PubMed ID 11591147
Journal Biochemistry
Year 2001
Volume 40
Pages 12285-91
Authors Sun D, Davidson VL
Title Re-engineering monovalent cation binding sites of methylamine dehydrogenase: effects on spectral properties and gated electron transfer.
Related PDB
Related UniProtKB
[39]
Resource
Comments
Medline ID
PubMed ID 11525672
Journal J Am Chem Soc
Year 2001
Volume 123
Pages 8604-5
Authors Faulder PF, Tresadern G, Chohan KK, Scrutton NS, Sutcliffe MJ, Hillier IH, Burton NA
Title QM/MM studies show substantial tunneling for the hydrogen-transfer reaction in methylamine dehydrogenase.
Related PDB
Related UniProtKB
[40]
Resource
Comments
Medline ID
PubMed ID 11087744
Journal J Biol Chem
Year 2001
Volume 276
Pages 6234-42
Authors Basran J, Patel S, Sutcliffe MJ, Scrutton NS
Title Importance of barrier shape in enzyme-catalyzed reactions. Vibrationally assisted hydrogen tunneling in tryptophan tryptophylquinone-dependent amine dehydrogenases.
Related PDB
Related UniProtKB
[41]
Resource
Comments
Medline ID
PubMed ID 11707614
Journal Protein Eng
Year 2001
Volume 14
Pages 675-81
Authors Sun D, Jones LH, Mathews FS, Davidson VL
Title Active-site residues are critical for the folding and stability of methylamine dehydrogenase.
Related PDB
Related UniProtKB
[42]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12437349
Journal Biochemistry
Year 2002
Volume 41
Pages 13926-33
Authors Sun D, Chen ZW, Mathews FS, Davidson VL
Title Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyanin.
Related PDB 1mg2 1mg3
Related UniProtKB
[43]
Resource
Comments
Medline ID
PubMed ID 12084049
Journal Eur J Biochem
Year 2002
Volume 269
Pages 3096-102
Authors Sutcliffe MJ, Scrutton NS
Title A new conceptual framework for enzyme catalysis. Hydrogen tunnelling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes.
Related PDB
Related UniProtKB
[44]
Resource
Comments
Medline ID
PubMed ID 11733518
Journal J Biol Chem
Year 2002
Volume 277
Pages 4119-22
Authors Wang Y, Sun D, Davidson VL
Title Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase.
Related PDB
Related UniProtKB
[45]
Resource
Comments
Medline ID
PubMed ID 12686138
Journal Biochim Biophys Acta
Year 2003
Volume 1647
Pages 230-3
Authors Davidson VL
Title Probing mechanisms of catalysis and electron transfer by methylamine dehydrogenase by site-directed mutagenesis of alpha Phe55.
Related PDB
Related UniProtKB
[46]
Resource
Comments
Medline ID
PubMed ID 12686155
Journal Biochim Biophys Acta
Year 2003
Volume 1647
Pages 337-42
Authors Ferrari D, Merli A, Peracchi A, Di Valentin M, Carbonera D, Rossi GL
Title Catalysis and electron transfer in protein crystals: the binary and ternary complexes of methylamine dehydrogenase with electron acceptors.
Related PDB
Related UniProtKB
[47]
Resource
Comments
Medline ID
PubMed ID 12555860
Journal Faraday Discuss
Year 2003
Volume 122
Pages 223-42; discussion 269-82
Authors Tresadern G, Nunez S, Faulder PF, Wang H, Hillier IH, Burton NA
Title Direct dynamics calculations of reaction rate and kinetic isotope effects in enzyme catalysed reactions.
Related PDB
Related UniProtKB
[48]
Resource
Comments
Medline ID
PubMed ID 12630872
Journal J Am Chem Soc
Year 2003
Volume 125
Pages 3224-5
Authors Davidson VL, Sun D
Title Evidence for substrate activation of electron transfer from methylamine dehydrogenase to amicyanin.
Related PDB
Related UniProtKB

Comments
Trp57 is modified and covalently bonded to the sidechain of Trp108 to form a cofactor, tryptophan tryptophylquinone (TTQ).
Amicyanin (Swiss-prot;P22364) is a primary acceptor, whilst cytochrome c (Swiss-prot;P29899) is a secondary acceptor. Thus, this enzyme catalyzes the following reactions (see [30], [37]):
(A) Exchange of double-bonded atoms (carbonyl bond by amine; Schiff-base formation), releasing H2O:
(B) Isomerization (shift of double-bond position):
(C) Exchange of double-bonded atoms (Schiff-base deformation by water), giving aldehyde product and aminoquinol TTQ:
(D) Electron transfer from aminoquinol TTQ to copper of the primary acceptor protein, amicyanin, leading to formation of aminosemiquinone TTQ:
(E) Exchange of double-bonded atoms (Schiff-base deformation by water), giving TTQ and ammonia:
The transferred electron is transferred further to Heme group of the secondary acceptor, cytochrome c.

Created Updated
2005-05-30 2012-10-03