|
Enzyme Name | UniProtKB | KEGG |
---|
| P29894 | P23006 | P22619 | P22641 |
---|
Protein name | Methylamine dehydrogenase heavy chain | Methylamine dehydrogenase heavy chain | Methylamine dehydrogenase light chain | Methylamine dehydrogenase light chain | methylamine dehydrogenase (amicyanin)amine dehydrogenaseprimary-amine dehydrogenaseamine: (acceptor) oxidoreductase (deaminating)primary-amine:(acceptor) oxidoreductase (deaminating) |
---|
Synonyms | MADHEC 1.4.9.1Methylamine dehydrogenase (amicyanin) | MADHEC 1.4.9.1Methylamine dehydrogenase (amicyanin) | MADHEC 1.4.9.1Methylamine dehydrogenase (amicyanin) | MADHEC 1.4.9.1Methylamine dehydrogenase (amicyanin)Methylamine dehydrogenase subunit beta |
---|
Pfam | PF06433 (Me-amine-dh_H) [Graphical view]
| PF06433 (Me-amine-dh_H) [Graphical view]
| PF02975 (Me-amine-dh_L) [Graphical view]
| PF02975 (Me-amine-dh_L) [Graphical view]
|
---|
KEGG pathways | MAP code | Pathways |
---|
MAP00680 | Methane metabolism |
UniProtKB:Accession Number | P29894 | P23006 | P22619 | P22641 |
---|
Entry name | DHMH_PARDE | DHMH_PARVE | DHML_PARDE | DHML_PARVE |
---|
Activity | Methylamine + H(2)O + amicyanin = formaldehyde + ammonia + reduced amicyanin. | Methylamine + H(2)O + amicyanin = formaldehyde + ammonia + reduced amicyanin. | Methylamine + H(2)O + amicyanin = formaldehyde + ammonia + reduced amicyanin. | Methylamine + H(2)O + amicyanin = formaldehyde + ammonia + reduced amicyanin. |
---|
Subunit | Tetramer of two light and two heavy chains. | Tetramer of two light and two heavy chains. | Heterotetramer of two light and two heavy chains. | Heterotetramer of two light and two heavy chains. |
---|
Subcellular location | Periplasm. | Periplasm. | Periplasm. | Periplasm. |
---|
Cofactor |
|
| Contains 1 tryptophan tryptophylquinone per subunit. | Contains 1 tryptophan tryptophylquinone per subunit. |
---|
Compound table: links to PDB-related databases & PoSSuM |
---|
| Cofactors | Substrates | Products | intermediates |
---|
KEGG-id | L00002 | C00218 | C00001 | C19671 | C00067 | C00014 | C19672 |
|
---|
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 |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
1mafH |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
1mdaH |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
1mdaJ |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
1mg2A |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
1mg2E |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
1mg2I |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
1mg2M |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
1mg3A |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
1mg3E |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
1mg3I |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
1mg3M |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
2bbkH |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
2bbkJ |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
2madH |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
2mtaH |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
1maeL |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
1mafL |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
1mdaL |  |  |  |  |  |  |  | Bound:TRP 107-TRQ 57 | Unbound | | Bound:_CU(chain A) | Unbound | Unbound | Unbound | Unbound |
---|
1mdaM |  |  |  |  |  |  |  | Bound:TRP 107-TRQ 57 | Unbound | | Bound:_CU(chain B) | Unbound | Unbound | Unbound | Unbound |
---|
1mg2B |  |  |  |  |  |  |  | Bound:TRP 108-TRQ 57 | Unbound | | Bound:_CU(chain C) | Unbound | Unbound | Unbound | Unbound |
---|
1mg2F |  |  |  |  |  |  |  | Bound:TRP 108-TRQ 57 | Unbound | | Bound:_CU(chain G) | Unbound | Unbound | Unbound | Unbound |
---|
1mg2J |  |  |  |  |  |  |  | Bound:TRP 108-TRQ 57 | Unbound | | Bound:_CU(chain K) | Unbound | Unbound | Unbound | Unbound |
---|
1mg2N |  |  |  |  |  |  |  | Bound:TRP 108-TRQ 57 | Unbound | | Bound:_CU(chain O) | Unbound | Unbound | Unbound | Unbound |
---|
1mg3B |  |  |  |  |  |  |  | Analogue:TRP 108-TRW 57 | Unbound | | Bound:_CU(chain C) | Unbound | Unbound | Unbound | Intermediate-analogue:TRP 108-TRW 57 |
---|
1mg3F |  |  |  |  |  |  |  | Analogue:TRP 108-TRW 57 | Unbound | | Bound:_CU(chain G) | Unbound | Unbound | Unbound | Intermediate-analogue:TRP 108-TRW 57 |
---|
1mg3J |  |  |  |  |  |  |  | Analogue:TRP 108-TRW 57 | Unbound | | Bound:_CU(chain K) | Unbound | Unbound | Unbound | Intermediate-analogue:TRP 108-TRW 57 |
---|
1mg3N |  |  |  |  |  |  |  | Analogue:TRP 108-TRW 57 | Unbound | | Bound:_CU(chain O) | Unbound | Unbound | Unbound | Intermediate-analogue:TRP 108-TRW 57 |
---|
2bbkL |  |  |  |  |  |  |  | Bound:TRP 108-TRP 57 | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
2bbkM |  |  |  |  |  |  |  | Bound:TRP 108-TRP 57 | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
2madL |  |  |  |  |  |  |  | Bound:TRP 108-TRP 57 | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound |
---|
2mtaL |  |  |  |  |  |  |  | Bound:TRP 108-TRQ 57 | Unbound | | Bound:_CU(chain A) | Unbound | Unbound | Unbound | Unbound |
---|
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] |
---|
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. |
---|
[2] |
---|
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. |
---|
[3] |
---|
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 UniProtKB | P23006,P22641 |
---|
[4] |
---|
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 UniProtKB | P23006,P22641 |
---|
[5] |
---|
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. |
---|
[6] |
---|
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. |
---|
[7] |
---|
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. |
---|
[8] |
---|
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. |
---|
[9] |
---|
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. |
---|
[10] |
---|
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. |
---|
[11] |
---|
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. |
---|
[12] |
---|
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] |
---|
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. |
---|
[14] |
---|
Comments | X-ray crystallography |
---|
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 |
---|
[15] |
---|
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 UniProtKB | P29894,P22619 |
---|
[16] |
---|
Comments | X-ray crystallography |
---|
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 |
---|
[17] |
---|
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. |
---|
[18] |
---|
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. |
---|
[19] |
---|
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 UniProtKB | P29894,P22619 |
---|
[20] |
---|
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. |
---|
[21] |
---|
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. |
---|
[22] |
---|
PubMed ID | 8524150 |
---|
Journal | Methods Enzymol |
---|
Year | 1995 |
---|
Volume | 258 |
---|
Pages | 191-216 |
---|
Authors | Mathews FS |
---|
Title | X-ray studies of quinoproteins. |
---|
[23] |
---|
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. |
---|
[24] |
---|
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. |
---|
[25] |
---|
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. |
---|
[26] |
---|
Comments | X-ray crystallography |
---|
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. |
---|
[27] |
---|
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. |
---|
[28] |
---|
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. |
---|
[29] |
---|
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. |
---|
[30] |
---|
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 |
---|
[31] |
---|
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. |
---|
[32] |
---|
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. |
---|
[33] |
---|
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. |
---|
[34] |
---|
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. |
---|
[35] |
---|
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. |
---|
[36] |
---|
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. |
---|
[37] |
---|
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. |
---|
[38] |
---|
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. |
---|
[39] |
---|
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. |
---|
[40] |
---|
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. |
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[41] |
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PubMed ID | 11707614 |
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Journal | Protein Eng |
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Year | 2001 |
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Volume | 14 |
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Pages | 675-81 |
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Authors | Sun D, Jones LH, Mathews FS, Davidson VL |
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Title | Active-site residues are critical for the folding and stability of methylamine dehydrogenase. |
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[42] |
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Comments | X-ray crystallography |
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PubMed ID | 12437349 |
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Journal | Biochemistry |
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Year | 2002 |
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Volume | 41 |
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Pages | 13926-33 |
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Authors | Sun D, Chen ZW, Mathews FS, Davidson VL |
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Title | Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyanin. |
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Related PDB | 1mg2,1mg3 |
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[43] |
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PubMed ID | 12084049 |
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Journal | Eur J Biochem |
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Year | 2002 |
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Volume | 269 |
---|
Pages | 3096-102 |
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Authors | Sutcliffe MJ, Scrutton NS |
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Title | A new conceptual framework for enzyme catalysis. Hydrogen tunnelling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes. |
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[44] |
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PubMed ID | 11733518 |
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Journal | J Biol Chem |
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Year | 2002 |
---|
Volume | 277 |
---|
Pages | 4119-22 |
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Authors | Wang Y, Sun D, Davidson VL |
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Title | Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase. |
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[45] |
---|
PubMed ID | 12686138 |
---|
Journal | Biochim Biophys Acta |
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Year | 2003 |
---|
Volume | 1647 |
---|
Pages | 230-3 |
---|
Authors | Davidson VL |
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Title | Probing mechanisms of catalysis and electron transfer by methylamine dehydrogenase by site-directed mutagenesis of alpha Phe55. |
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[46] |
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PubMed ID | 12686155 |
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Journal | Biochim Biophys Acta |
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Year | 2003 |
---|
Volume | 1647 |
---|
Pages | 337-42 |
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Authors | Ferrari D, Merli A, Peracchi A, Di Valentin M, Carbonera D, Rossi GL |
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Title | Catalysis and electron transfer in protein crystals: the binary and ternary complexes of methylamine dehydrogenase with electron acceptors. |
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[47] |
---|
PubMed ID | 12555860 |
---|
Journal | Faraday Discuss |
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Year | 2003 |
---|
Volume | 122 |
---|
Pages | 223-42; discussion 269-82 |
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Authors | Tresadern G, Nunez S, Faulder PF, Wang H, Hillier IH, Burton NA |
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Title | Direct dynamics calculations of reaction rate and kinetic isotope effects in enzyme catalysed reactions. |
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[48] |
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PubMed ID | 12630872 |
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Journal | J Am Chem Soc |
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Year | 2003 |
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Volume | 125 |
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Pages | 3224-5 |
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Authors | Davidson VL, Sun D |
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Title | Evidence for substrate activation of electron transfer from methylamine dehydrogenase to amicyanin. |
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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.
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created | updated |
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2005-05-30 | 2012-10-03 |
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