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 1.4.99.3 |
PF06433
(Me-amine-dh_H)
[Graphical View] |
| P23006 |
Methylamine dehydrogenase heavy chain
|
MADH
EC 1.4.99.3 |
PF06433
(Me-amine-dh_H)
[Graphical View] |
| P22619 |
Methylamine dehydrogenase light chain
|
MADH
EC 1.4.99.3 |
PF02975
(Me-amine-dh_L)
[Graphical View] |
| P22641 |
Methylamine dehydrogenase light chain
|
MADH
EC 1.4.99.3 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 16830 |
15377 15377 |
16842 16842 |
16134 16134 |
|||||||||
| PubChem |
101916295 101916295 |
6329 6329 |
22247451 962 22247451 962 |
712 712 |
222 222 |
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| 1maeH |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1mafH |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1mdaH |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1mdaJ |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1mg2A |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1mg2E |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1mg2I |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1mg2M |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1mg3A |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1mg3E |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1mg3I |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1mg3M |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2bbkH |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2bbkJ |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2madH |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2mtaH |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1maeL |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1mafL |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1mdaL |
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Bound:TRP_107-TRQ_57 | Unbound | Bound:_CU(chain A) | Unbound | Unbound | Unbound | Unbound | |
| 1mdaM |
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Bound:TRP_107-TRQ_57 | Unbound | Bound:_CU(chain B) | Unbound | Unbound | Unbound | Unbound | |
| 1mg2B |
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Bound:TRP_108-TRQ_57 | Unbound | Bound:_CU(chain C) | Unbound | Unbound | Unbound | Unbound | |
| 1mg2F |
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Bound:TRP_108-TRQ_57 | Unbound | Bound:_CU(chain G) | Unbound | Unbound | Unbound | Unbound | |
| 1mg2J |
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Bound:TRP_108-TRQ_57 | Unbound | Bound:_CU(chain K) | Unbound | Unbound | Unbound | Unbound | |
| 1mg2N |
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Bound:TRP_108-TRQ_57 | Unbound | Bound:_CU(chain O) | Unbound | Unbound | Unbound | Unbound | |
| 1mg3B |
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Analogue:TRP_108-TRW_57 | Unbound | Bound:_CU(chain C) | Unbound | Unbound | Unbound | Intermediate-analogue:TRP_108-TRW_57 | |
| 1mg3F |
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Analogue:TRP_108-TRW_57 | Unbound | Bound:_CU(chain G) | Unbound | Unbound | Unbound | Intermediate-analogue:TRP_108-TRW_57 | |
| 1mg3J |
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Analogue:TRP_108-TRW_57 | Unbound | Bound:_CU(chain K) | Unbound | Unbound | Unbound | Intermediate-analogue:TRP_108-TRW_57 | |
| 1mg3N |
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Analogue:TRP_108-TRW_57 | Unbound | Bound:_CU(chain O) | Unbound | Unbound | Unbound | Intermediate-analogue:TRP_108-TRW_57 | |
| 2bbkL |
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Bound:TRP_108-TRP_57 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2bbkM |
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Bound:TRP_108-TRP_57 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2madL |
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Bound:TRP_108-TRP_57 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2mtaL |
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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 |
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| 1mafH |
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| 1mdaH |
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| 1mdaJ |
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| 1mg2A |
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mutant F55A | ||||
| 1mg2E |
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mutant F55A | ||||
| 1mg2I |
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mutant F55A | ||||
| 1mg2M |
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mutant F55A | ||||
| 1mg3A |
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mutant F55A | ||||
| 1mg3E |
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mutant F55A | ||||
| 1mg3I |
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mutant F55A | ||||
| 1mg3M |
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mutant F55A | ||||
| 2bbkH |
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| 2bbkJ |
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| 2madH |
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| 2mtaH |
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| 1maeL |
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ASP 32;ASP 76;TYR 119;THR 122 | TRP 57;TRP 108(Tryptophan tryptophylquinone) | |||
| 1mafL |
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ASP 32;ASP 76;TYR 119;THR 122 | TRP 57;TRP 108(Tryptophan tryptophylquinone) | |||
| 1mdaL |
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;ASP 76;TYR 117; | TRQ 57;TRP 107(Tryptophan tryptophylquinone) | mutant D32A, T120S | ||
| 1mdaM |
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;ASP 76;TYR 117; | TRQ 57;TRP 107(Tryptophan tryptophylquinone) | mutant D32A, T120S | ||
| 1mg2B |
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ASP 32;ASP 76;TYR 119;THR 122 | TRQ 57;TRP 108(Tryptophan tryptophylquinone) | |||
| 1mg2F |
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ASP 32;ASP 76;TYR 119;THR 122 | TRQ 57;TRP 108(Tryptophan tryptophylquinone) | |||
| 1mg2J |
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ASP 32;ASP 76;TYR 119;THR 122 | TRQ 57;TRP 108(Tryptophan tryptophylquinone) | |||
| 1mg2N |
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ASP 32;ASP 76;TYR 119;THR 122 | TRQ 57;TRP 108(Tryptophan tryptophylquinone) | |||
| 1mg3B |
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ASP 32;ASP 76;TYR 119;THR 122 | TRW 57;TRP 108(Tryptophan tryptophylquinone-phenylhydrazine) | |||
| 1mg3F |
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ASP 32;ASP 76;TYR 119;THR 122 | TRW 57;TRP 108(Tryptophan tryptophylquinone-phenylhydrazine) | |||
| 1mg3J |
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ASP 32;ASP 76;TYR 119;THR 122 | TRW 57;TRP 108(Tryptophan tryptophylquinone-phenylhydrazine) | |||
| 1mg3N |
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ASP 32;ASP 76;TYR 119;THR 122 | TRW 57;TRP 108(Tryptophan tryptophylquinone-phenylhydrazine) | |||
| 2bbkL |
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ASP 32;ASP 76;TYR 119;THR 122 | TRP 57;TRP 108(Tryptophan tryptophylquinone) | |||
| 2bbkM |
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ASP 32;ASP 76;TYR 119;THR 122 | TRP 57;TRP 108(Tryptophan tryptophylquinone) | |||
| 2madL |
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ASP 32;ASP 76;TYR 119;THR 122 | TRP 57;TRP 108(Tryptophan tryptophylquinone) | |||
| 2mtaL |
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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 | |
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[10]
|
Scheme 1, Scheme 2, Scheme 3, p.821-823 | |
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[12]
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p.4962-4964 | |
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[13]
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Fig.6, p.3389-3390 | |
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[14]
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||
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[16]
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p.151-152 | |
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[17]
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Fig.5, p.5697-5701 | |
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[19]
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Fig.4, p.89 | |
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[20]
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Fig.3 | |
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[26]
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Fig.1, Fig.6 | |
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[30]
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Fig.13, p.144-146 | |
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[31]
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Scheme 2 | |
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[32]
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Fig.5, p.4865-4867 | |
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[36]
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Fig.2, p.933 | |
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[37]
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Fig.2, Fig.7, Fig.8, p.121-123, p.131-138 | |
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[38]
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Fig.2 | |
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[39]
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Fig.1 | |
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[40]
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Fig.1 | |
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[41]
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p.680-681 | |
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[42]
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Fig.2, Fig.7 | |
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[43]
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Fig.2, p.3098-3099 | |
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[45]
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||
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[47]
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Fig.3, Fig.6, p.228-230 | |
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[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, |
| 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, |
| 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. |
| 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, |
| 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, |
| 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, |
| 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. |
| 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. |
| 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. |
| 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. |
| 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. |
| 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, Amicyanin (Swiss-prot;P22364) is a primary acceptor, (A) Exchange of double-bonded atoms (carbonyl bond by amine; Schiff-base formation), (B) Isomerization (shift of double-bond position): (C) Exchange of double-bonded atoms (Schiff-base deformation by water), (D) Electron transfer from aminoquinol TTQ to copper of the primary acceptor protein, (E) Exchange of double-bonded atoms (Schiff-base deformation by water), The transferred electron is transferred further to Heme group of the secondary acceptor, |
| Created | Updated |
|---|---|
| 2005-05-30 | 2012-10-03 |