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 subunit 1
|
EC
1.1.99.8
MDH large alpha subunit MEDH |
PF01011
(PQQ)
[Graphical View] |
|
| P16027 |
Methanol dehydrogenase subunit 1
|
EC
1.1.99.8
MDH large alpha subunit MEDH |
PF01011
(PQQ)
[Graphical View] |
YP_002965446.1
(Protein)
NC_012808.1 (DNA/RNA sequence) |
| P12293 |
Methanol dehydrogenase subunit 1
|
EC
1.1.99.8
MDH large alpha subunit MEDH |
PF01011
(PQQ)
[Graphical View] |
|
| P38540 |
Methanol dehydrogenase subunit 2
|
EC
1.1.99.8
MDH small subunit beta MDH-associated peptide MEDH |
PF02315
(MDH)
[Graphical View] |
|
| P14775 |
Methanol dehydrogenase subunit 2
|
EC
1.1.99.8
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 subunit 2
|
EC
1.1.99.8
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 18315 |
29108 29108 |
||||||||||
| PubChem |
1024 1024 |
271 271 |
||||||||||
| 1b2nA |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Bound:MOH | Unbound | Unbound | Unbound | |
| 1b2nC |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Bound:MOH | Unbound | Unbound | Unbound | |
| 1g72A |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 1g72C |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 3aahA |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 3aahC |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 4aahA |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 4aahC |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 1h4iA |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 1h4iC |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 1h4jA |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 1h4jC |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 1h4jE |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 1h4jG |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 1w6sA |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 1w6sC |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 1lrwA |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 1lrwC |
|
|
|
|
|
Bound:PQQ | Bound:_CA | Unbound | Unbound | Unbound | Unbound | |
| 1b2nB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1b2nD |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1g72B |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1g72D |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3aahB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3aahD |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 4aahB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 4aahD |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1h4iB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1h4iD |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1h4jB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1h4jD |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1h4jF |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1h4jH |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1w6sB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1w6sD |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1lrwB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1lrwD |
|
|
|
|
|
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 |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;ASP 297 | GLU 171;ASN 255(Calcium binding) | |||
| 1b2nC |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;ASP 297 | GLU 171;ASN 255(Calcium binding) | |||
| 1g72A |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;ASP 297 | GLU 171;ASN 255(Calcium binding) | |||
| 1g72C |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;ASP 297 | GLU 171;ASN 255(Calcium binding) | |||
| 3aahA |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;ASP 297 | GLU 171;ASN 255(Calcium binding) | |||
| 3aahC |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;ASP 297 | GLU 171;ASN 255(Calcium binding) | |||
| 4aahA |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;ASP 297 | GLU 171;ASN 255(Calcium binding) | |||
| 4aahC |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;ASP 297 | GLU 171;ASN 255(Calcium binding) | |||
| 1h4iA |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;ASP 303 | GLU 177;ASN 261(Calcium binding) | |||
| 1h4iC |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;ASP 303 | GLU 177;ASN 261(Calcium binding) | |||
| 1h4jA |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;GLU 303 | GLU 177;ASN 261(Calcium binding) | |||
| 1h4jC |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;GLU 303 | GLU 177;ASN 261(Calcium binding) | |||
| 1h4jE |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;GLU 303 | GLU 177;ASN 261(Calcium binding) | |||
| 1h4jG |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;GLU 303 | GLU 177;ASN 261(Calcium binding) | |||
| 1w6sA |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;ASP 303 | GLU 177;ASN 261(Calcium binding) | |||
| 1w6sC |
|
|
|
|
|
CYS 2103;CYS 2104;ASP 2105;ASP 2303 | GLU 2177;ASN 2261(Calcium binding) | |||
| 1lrwA |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;ASP 303 | GLU 177;ASN 261(Calcium binding) | |||
| 1lrwC |
|
|
|
|
|
CYS 103;CYS 104;ASP 105;ASP 303 | GLU 177;ASN 261(Calcium binding) | |||
| 1b2nB |
|
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|
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|
|||||
| 1b2nD |
|
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|||||
| 1g72B |
|
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|||||
| 1g72D |
|
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|||||
| 3aahB |
|
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|||||
| 3aahD |
|
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|||||
| 4aahB |
|
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|
|||||
| 4aahD |
|
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|||||
| 1h4iB |
|
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|||||
| 1h4iD |
|
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|||||
| 1h4jB |
|
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| 1h4jD |
|
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| 1h4jF |
|
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| 1h4jH |
|
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| 1w6sB |
|
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|||||
| 1w6sD |
|
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| 1lrwB |
|
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| 1lrwD |
|
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| 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, |
| 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. |
| 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, |
| 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, |
| 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, Thus, (A) Hydride transfer from a primary alcohole to PQQ, (B) Single electron transfer from PQQH2 to the electron transfer, 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. NADP-dependent ALDH (E.C. ALDH3 (E.C. NADP-dependent GAPDH (E.C. NAD(P)-dependent GAPDH (phosphorylating) (E.C. GAPDH (phosphorylating) (E.C. NADP-dependent GAPDH (phosphorylating) (E.C. |
| Created | Updated |
|---|---|
| 2005-01-18 | 2012-10-03 |