DB code: D00016

CATH domain 2.140.10.10 : Methanol Dehydrogenase; Chain A Catalytic domain
4.10.160.10 : Methanol Dehydrogenase; Chain B
E.C. 1.1.2.7
CSA 1g72
M-CSA 1g72
MACiE M0099

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam RefSeq
P38539 Methanol dehydrogenase [cytochrome c] subunit 1
EC 1.1.2.7
MDH large subunit alpha
MEDH
PF01011 (PQQ)
[Graphical View]
P16027 Methanol dehydrogenase [cytochrome c] subunit 1
EC 1.1.2.7
MDH large subunit alpha
MEDH
PF01011 (PQQ)
[Graphical View]
YP_002965446.1 (Protein)
NC_012808.1 (DNA/RNA sequence)
P12293 Methanol dehydrogenase [cytochrome c] subunit 1
EC 1.1.2.7
MDH large subunit alpha
MEDH
PF01011 (PQQ)
[Graphical View]
P38540 Methanol dehydrogenase [cytochrome c] subunit 2
EC 1.1.2.7
MDH small subunit beta
MDH-associated peptide
MEDH
PF02315 (MDH)
[Graphical View]
P14775 Methanol dehydrogenase [cytochrome c] subunit 2
EC 1.1.2.7
MDH small subunit beta
MDH-associated peptide
MEDH
PF02315 (MDH)
[Graphical View]
YP_002965443.1 (Protein)
NC_012808.1 (DNA/RNA sequence)
P29898 Methanol dehydrogenase [cytochrome c] subunit 2
EC 1.1.2.7
MDH small subunit beta
MDH-associated peptide
MEDH
PF02315 (MDH)
[Graphical View]

KEGG enzyme name
methanol dehydrogenase (cytochrome c)
methanol dehydrogenase
MDH

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P38539 DHM1_METME A primary alcohol + 2 cytochrome c(L) = an aldehyde + 2 reduced cytochrome c(L). Heterotetramer of 2 alpha and 2 beta subunits. Cell inner membrane, Peripheral membrane protein, Periplasmic side. Note=Periplasmic, but associated with inner membrane. Binds 1 calcium ion per subunit. Binds 1 PQQ per subunit. PQQ is inserted between disulfide Cys-105-Cys-106 and the indole ring of Trp-239.
P16027 DHM1_METEX A primary alcohol + 2 cytochrome c(L) = an aldehyde + 2 reduced cytochrome c(L). Heterotetramer composed of 2 alpha and 2 beta subunits. Cell inner membrane, Peripheral membrane protein, Periplasmic side. Note=Periplasmic, but associated with inner membrane. Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-130-Cys-131 and the indole ring of Trp-270. Binds 1 calcium ion per subunit.
P12293 DHM1_PARDE A primary alcohol + 2 cytochrome c(L) = an aldehyde + 2 reduced cytochrome c(L). Heterotetramer composed of 2 alpha and 2 beta subunits. Periplasm. Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-135-Cys-136 and the indole ring of Trp-275. Binds 1 calcium ion per subunit.
P38540 DHM2_METME A primary alcohol + 2 cytochrome c(L) = an aldehyde + 2 reduced cytochrome c(L). Heterotetramer composed of 2 alpha and 2 beta subunits. Cell inner membrane, Peripheral membrane protein, Periplasmic side. Note=Periplasmic, but associated with inner membrane.
P14775 DHM2_METEX A primary alcohol + 2 cytochrome c(L) = an aldehyde + 2 reduced cytochrome c(L). Heterotetramer composed of 2 alpha and 2 beta subunits. Periplasm.
P29898 DHM2_PARDE A primary alcohol + 2 cytochrome c(L) = an aldehyde + 2 reduced cytochrome c(L). Heterotetramer composed of 2 alpha and 2 beta subunits. Periplasm.

KEGG Pathways
Map code Pathways E.C.
MAP00010 Glycolysis / Gluconeogenesis
MAP00625 Chloroalkane and chloroalkene degradation
MAP00680 Methane metabolism
MAP00910 Nitrogen metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00113 C00076 C00226 C18233 C00071 C18234
E.C.
Compound PQQ Calcium Primary alcohol Cytochrome cL Aldehyde Reduced cytochrome cL
Type aromatic ring (with nitrogen atoms),carbohydrate,carboxyl group divalent metal (Ca2+, Mg2+) carbohydrate amide group,amine group,aromatic ring (with nitrogen atoms),carboxyl group,heavy metal,peptide/protein,sulfide group carbohydrate amide group,amine group,aromatic ring (with nitrogen atoms),carboxyl group,heavy metal,peptide/protein,sulfide group
ChEBI 18315
29108
PubChem 1024
271
1b2nA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Bound:MOH Unbound Unbound Unbound
1b2nC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Bound:MOH Unbound Unbound Unbound
1g72A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
1g72C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
3aahA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
3aahC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
4aahA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
4aahC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
1h4iA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
1h4iC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
1h4jA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
1h4jC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
1h4jE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
1h4jG Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
1w6sA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
1w6sC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
1lrwA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
1lrwC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PQQ Bound:_CA Unbound Unbound Unbound Unbound
1b2nB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1b2nD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1g72B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1g72D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3aahB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3aahD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
4aahB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
4aahD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1h4iB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1h4iD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1h4jB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1h4jD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1h4jF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1h4jH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1w6sB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1w6sD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1lrwB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1lrwD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P38539

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1b2nA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;ASP 297 GLU 171;ASN 255(Calcium binding)
1b2nC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;ASP 297 GLU 171;ASN 255(Calcium binding)
1g72A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;ASP 297 GLU 171;ASN 255(Calcium binding)
1g72C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;ASP 297 GLU 171;ASN 255(Calcium binding)
3aahA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;ASP 297 GLU 171;ASN 255(Calcium binding)
3aahC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;ASP 297 GLU 171;ASN 255(Calcium binding)
4aahA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;ASP 297 GLU 171;ASN 255(Calcium binding)
4aahC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;ASP 297 GLU 171;ASN 255(Calcium binding)
1h4iA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;ASP 303 GLU 177;ASN 261(Calcium binding)
1h4iC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;ASP 303 GLU 177;ASN 261(Calcium binding)
1h4jA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;GLU 303 GLU 177;ASN 261(Calcium binding)
1h4jC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;GLU 303 GLU 177;ASN 261(Calcium binding)
1h4jE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;GLU 303 GLU 177;ASN 261(Calcium binding)
1h4jG Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;GLU 303 GLU 177;ASN 261(Calcium binding)
1w6sA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;ASP 303 GLU 177;ASN 261(Calcium binding)
1w6sC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 2103;CYS 2104;ASP 2105;ASP 2303 GLU 2177;ASN 2261(Calcium binding)
1lrwA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;ASP 303 GLU 177;ASN 261(Calcium binding)
1lrwC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 103;CYS 104;ASP 105;ASP 303 GLU 177;ASN 261(Calcium binding)
1b2nB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1b2nD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1g72B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1g72D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3aahB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3aahD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
4aahB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
4aahD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1h4iB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1h4iD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1h4jB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1h4jD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1h4jF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1h4jH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1w6sB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1w6sD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1lrwB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1lrwD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
Fig.7, Fig.8
[4]
Scheme 1, Scheme 2, p.31-33
[9]
p.12957-12958
[10]
Fig.7, Fig.8, p.670-671
[13]
[14]
p.104-105
[15]
p.378
[17]
p.182-184
[18]
p.492-498
[19]
Scheme 1, Scheme 3, Scheme 4, p.11884-11886
[20]
Scheme 2, Scheme 3, p.6565-6570
[21]
Fig.7, p.1218-1220
[23]
Fig.1, Fig.2, p.759-764
[24]
Fig.2, p.9807-9808
[25]
Fig.1, p.432-433
[26]
p.850-853
[27]
Fig. 3, p.3-6
[28]
p.17-19

References
[1]
Resource
Comments
Medline ID
PubMed ID 3098983
Journal J Mol Biol
Year 1986
Volume 191
Pages 141-2
Authors Lim LW, Xia Z, Mathews FS, Davidson VL
Title Preliminary X-ray crystallographic study of methanol dehydrogenase from Methylophilus methylotrophus.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 3030752
Journal Eur J Biochem
Year 1987
Volume 164
Pages 223-7
Authors Parker MW, Cornish A, Gossain V, Best DJ
Title Purification, crystallisation and preliminary X-ray diffraction characterisation of methanol dehydrogenase from Methylosinus trichosporium OB3b.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 3289922
Journal Eur J Biochem
Year 1988
Volume 174
Pages 331-8
Authors Frank J Jr, Dijkstra M, Duine JA, Balny C
Title Kinetic and spectral studies on the redox forms of methanol dehydrogenase from Hyphomicrobium X.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 2673028
Journal Antonie Van Leeuwenhoek
Year 1989
Volume 56
Pages 25-34
Authors Frank J, Dijkstra M, Balny C, Verwiel PE, Duine JA
Title Methanol dehydrogenase: mechanism of action.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 2687021
Journal FEBS Lett
Year 1989
Volume 258
Pages 175-6
Authors Xia ZX, Hao ZP, Mathews FS, Davidson VL
Title Crystallization and preliminary X-ray crystallographic study of the quinoprotein methanol dehydrogenase from bacterium W3A1.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)
Medline ID 93054513
PubMed ID 1331050
Journal J Biol Chem
Year 1992
Volume 267
Pages 22289-97
Authors Xia ZX, Dai WW, Xiong JP, Hao ZP, Davidson VL, White S, Mathews FS
Title The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-A resolution.
Related PDB
Related UniProtKB P38539 P38540
[8]
Resource
Comments
Medline ID
PubMed ID 1447790
Journal J Mol Biol
Year 1992
Volume 228
Pages 302-5
Authors Ghosh M, Harlos K, Blake CC, Richardson I, Anthony C
Title Crystallization and preliminary crystallographic investigation of methanol dehydrogenase from Methylobacterium extorquens AM1.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
Medline ID 94059969
PubMed ID 8241148
Journal Biochemistry
Year 1993
Volume 32
Pages 12955-8
Authors White S, Boyd G, Mathews FS, Xia ZX, Dai WW, Zhang YF, Davidson VL
Title The active site structure of the calcium-containing quinoprotein methanol dehydrogenase.
Related PDB
Related UniProtKB P38539 P38540
[10]
Resource
Comments
Medline ID
PubMed ID 7818466
Journal Biochem J
Year 1994
Volume 304
Pages 665-74
Authors Anthony C, Ghosh M, Blake CC
Title The structure and function of methanol dehydrogenase and related quinoproteins containing pyrrolo-quinoline quinone.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 7945232
Journal Biochem J
Year 1994
Volume 303
Pages 141-5
Authors Harris TK, Davidson VL
Title Thermal stability of methanol dehydrogenase is altered by the replacement of enzyme-bound Ca2+ with Sr2+.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 7918485
Journal Biochemistry
Year 1994
Volume 33
Pages 12600-8
Authors Harris TK, Davidson VL, Chen L, Mathews FS, Xia ZX
Title Ionic strength dependence of the reaction between methanol dehydrogenase and cytochrome c-551i: evidence of conformationally coupled electron transfer.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 8032156
Journal EXS
Year 1994
Volume 71
Pages 251-60
Authors Ghosh M, Avezoux A, Anthony C, Harlos K, Blake CC
Title X-ray structure of PQQ-dependent methanol dehydrogenase.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 7656012
Journal Nat Struct Biol
Year 1994
Volume 1
Pages 102-5
Authors Blake CC, Ghosh M, Harlos K, Avezoux A, Anthony C
Title The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 7772016
Journal Biochem J
Year 1995
Volume 308
Pages 375-9
Authors Cozier GE, Giles IG, Anthony C
Title The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens.
Related PDB
Related UniProtKB
[16]
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
[17]
Resource
Comments
Medline ID
PubMed ID 7735834
Journal Structure
Year 1995
Volume 3
Pages 177-87
Authors Ghosh M, Anthony C, Harlos K, Goodwin MG, Blake C
Title The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A.
Related PDB 1h4i
Related UniProtKB
[18]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8676383
Journal J Mol Biol
Year 1996
Volume 259
Pages 480-501
Authors Xia Z, Dai W, Zhang Y, White SA, Boyd GD, Mathews FS
Title Determination of the gene sequence and the three-dimensional structure at 2.4 angstroms resolution of methanol dehydrogenase from Methylophilus W3A1.
Related PDB 3aah 4aah
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 9342331
Journal Proc Natl Acad Sci U S A
Year 1997
Volume 94
Pages 11881-6
Authors Zheng YJ, Bruice TC
Title Conformation of coenzyme pyrroloquinoline quinone and role of Ca2+ in the catalytic mechanism of quinoprotein methanol dehydrogenase.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 9572874
Journal Biochemistry
Year 1998
Volume 37
Pages 6562-71
Authors Itoh S, Kawakami H, Fukuzumi S
Title Model studies on calcium-containing quinoprotein alcohol dehydrogenases. Catalytic role of Ca2+ for the oxidation of alcohols by coenzyme PQQ (4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2, 7,9-tricarboxylic acid).
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 9930981
Journal Biochemistry
Year 1999
Volume 38
Pages 1214-20
Authors Xia ZX, He YN, Dai WW, White SA, Boyd GD, Mathews FS
Title Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 A resolution.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 11195971
Journal J Protein Chem
Year 2000
Volume 19
Pages 469-73
Authors Zhao Y, Wang G, Cao Z, Wang Y, Cheng H, Zhou HM
Title Effects of Ca2+ on the activity and stability of methanol dehydrogenase.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 11761326
Journal Antioxid Redox Signal
Year 2001
Volume 3
Pages 757-74
Authors Anthony C
Title Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 11502173
Journal Biochemistry
Year 2001
Volume 40
Pages 9799-809
Authors Afolabi PR, Mohammed F, Amaratunga K, Majekodunmi O, Dales SL, Gill R, Thompson D, Cooper JB, Wood SP, Goodwin PM, Anthony C
Title Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L).
Related PDB 1h4j
Related UniProtKB
[25]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11149955
Journal Proc Natl Acad Sci U S A
Year 2001
Volume 98
Pages 432-4
Authors Zheng YJ, Xia Zx, Chen Zw, Mathews FS, Bruice TC
Title Catalytic mechanism of quinoprotein methanol dehydrogenase: A theoretical and x-ray crystallographic investigation.
Related PDB 1g72 1b2n
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 14505072
Journal J Biol Inorg Chem
Year 2003
Volume 8
Pages 843-54
Authors Xia ZX, Dai WW, He YN, White SA, Mathews FS, Davidson VL
Title X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i.
Related PDB 1lrw
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 15234264
Journal Arch Biochem Biophys
Year 2004
Volume 428
Pages 2-9
Authors Anthony C
Title The quinoprotein dehydrogenases for methanol and glucose.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 15234265
Journal Arch Biochem Biophys
Year 2004
Volume 428
Pages 10-21
Authors Toyama H, Mathews FS, Adachi O, Matsushita K
Title Quinohemoprotein alcohol dehydrogenases: structure, function, and physiology.
Related PDB
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 15520392
Journal Proc Natl Acad Sci U S A
Year 2004
Volume 101
Pages 15887-92
Authors Reddy SY, Bruice TC
Title Mechanisms of ammonia activation and ammonium ion inhibition of quinoprotein methanol dehydrogenase: a computational approach.
Related PDB
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 15608378
Journal Acta Crystallogr D Biol Crystallogr
Year 2005
Volume 61
Pages 75-9
Authors Williams PA, Coates L, Mohammed F, Gill R, Erskine PT, Coker A, Wood SP, Anthony C, Cooper JB
Title The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens.
Related PDB 1w6s
Related UniProtKB

Comments
Cytochrome c proteins, such as cytochrome cL (PDB; 1umm) and cytochrome c-551i (PDB; 1fi3), which are electron transfer proteins, play a role as a substrate, which accepts two electrons from this enzyme.
Thus, this enzyme catalyzes the following reactions:
(A) Hydride transfer from a primary alcohole to PQQ, giving an aldehyde and PQQH2.
(B) Single electron transfer from PQQH2 to the electron transfer, cytochrome c. (This reaction occurs twice.)
Asp105 and disulfide bond between Cys103-Cys104 might be involved in the electron transfer (see [27]).
***
The related enzymes are as follows:
ALDH (acceptor) (E.C.1.1.99.8) corresponds to this entry (D00016),
ALDH1 and 2 (E.C. 1.2.1.3) correspond to D00019 (in EzCatDB),
NADP-dependent ALDH (E.C. 1.2.1.4) corresponds to D00475,
ALDH3 (E.C. 1.2.1.5) corresponds to D00020,
NADP-dependent GAPDH (E.C. 1.2.1.9) corresponds to D00022,
NAD(P)-dependent GAPDH (phosphorylating) (E.C. 1.2.1.59) corresponds to D00476,
GAPDH (phosphorylating) (E.C. 1.2.1.12) corresponds to D00024,
NADP-dependent GAPDH (phosphorylating) (E.C. 1.2.1.13) has no entry currently.

Created Updated
2005-01-18 2012-10-03