Any feedback?
Literature summary extracted from
- Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus (2008), Biochemistry, 47, 6560-6570.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.4.9.1 | expressed in Escherichia coli | Paracoccus versutus |
| 1.4.9.1 | expressed in Escherichia coli BL21 cells | Paracoccus versutus |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.4.9.1 | MADH-amicyanin binary complex, hanging drop vapour diffusion method, in 28-29.5% PEG8000, 0.2 M Li2SO4, and 0.1 M phosphate (pH 6.5) | Paracoccus versutus |
| 1.4.9.1 | the crystal structure of the complex of MADH and amicyanin is determined to 2.5 A using the hanging-drop method. Enzyme is a heterotetramer consisting of two heavy chains and two light chains. The heavy chain of MADH folds into a characteristic, seven-blade beta-propeller domain and contains an N-terminal extension (residues 1-80) that wraps around the neighboring light chain, fixing it to the tetrameric enzyme. The light subunit consists mainly of loop regions with only four beta-strands, stabilized by a total of six disulfide bridges, containing the active site of the enzyme, a tryptophan tryptophylquinone moiety formed by Trp57 covalently linked to Trp108 | Paracoccus versutus |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.4.9.1 | KCl | the rate of transfer of the first electron from methylamine-reduced MADH to amicyanin is increased by monovalent cations | Paracoccus versutus |  |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.4.9.1 | 14200 | - |
SDS-PAGE, beta subunit | Paracoccus versutus |
| 1.4.9.1 | 43300 | - |
SDS-PAGE, alpha subunit | Paracoccus versutus |
| 1.4.9.1 | 138000 | - |
complex of methylamine dehydrogenase and amicyanin, gel filtration | Paracoccus versutus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.4.9.1 | Paracoccus versutus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.4.9.1 | DEAE column chromatography | Paracoccus versutus |
| 1.4.9.1 | using a DEAE column | Paracoccus versutus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.4.9.1 | dithionite + amicyanin + H2O | two-electron-reduced MADH is obtained by exposing the enzyme either to a 3fold molar excess of methylamine or to 2 mM dithionite | Paracoccus versutus | ? | - |
? | |
| 1.4.9.1 | methylamine + acceptor + H2O | - |
Paracoccus versutus | formaldehyde + NH3 + reduced acceptor | - |
? | |
| 1.4.9.1 | methylamine + amicyanin + H2O | two-electron-reduced MADH is obtained by exposing the enzyme either to a 3fold molar excess of methylamine or to 2 mM dithionite. The complex of MADH and amicyanin in solution is studied using nuclear magnetic resonance. Signals of perdeuterated, 15N-enriched amicyanin bound to MADH are observed. Chemical shift perturbation analysis indicates that the dissociation rate constant is 250/sec and that amicyanin assumes a well-defined position in the complex in solution. The most affected residues are in the interface observed in the crystal structure, whereas smaller chemical shift changes extend to deep inside the protein | Paracoccus versutus | formaldehyde + reduced amicyanin + NH3 | - |
? | |
| 1.4.9.1 | phenylethylamine + acceptor + H2O | - |
Paracoccus versutus | phenylacetaldehyde + NH3 + reduced acceptor | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.4.9.1 | heterotetramer | 2 * 43300 + 2 * 14200, X-ray crystallography | Paracoccus versutus |
| 1.4.9.1 | heterotetramer | crystal structure, enzyme shows a alpha2beta2 structure, consisting of two heavy chains and two light chains, alpha subunit: 43300 Da, beta subunit: 14200 Da | Paracoccus versutus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.4.9.1 | MADH | - |
Paracoccus versutus |
| 1.4.9.1 | methylamine dehydrogenase | - |
Paracoccus versutus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.4.9.1 | 0.77 | - |
amicyanin | methylamine-reduced MADH, pH 7.5 using a Ca-HEPES puffer | Paracoccus versutus | |
| 1.4.9.1 | 3.1 | - |
amicyanin | dithionite-reduced MADH, pH 7.5 using a Na,K-phosphate buffer and 0.2 M KCl | Paracoccus versutus | |
| 1.4.9.1 | 74 | - |
amicyanin | methylamine-reduced MADH, pH 7.5 using a Na,K-phosphate buffer and 0.2 M KCl | Paracoccus versutus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.4.9.1 | 7.5 | - |
assay at | Paracoccus versutus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.4.9.1 | heme c | - |
Paracoccus versutus | |
| 1.4.9.1 | tryptophan tryptophylquinone | - |
Paracoccus versutus | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
