Enzymes
UniProtKB help_outline | 265 proteins |
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Reaction participants Show >> << Hide
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Namehelp_outline
Co(I)-[dimethylamine-specific corrinoid protein]
Identifier
RHEA-COMP:11123
Reactive part
help_outline
- Name help_outline Co+ Identifier CHEBI:85033 (CAS: 16610-75-6) help_outline Charge 1 Formula Co InChIKeyhelp_outline BFVNPAKTAJENJQ-UHFFFAOYSA-N SMILEShelp_outline [Co+] 2D coordinates Mol file for the small molecule Search links Involved in 32 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline dimethylamine Identifier CHEBI:58040 Charge 1 Formula C2H8N InChIKeyhelp_outline ROSDSFDQCJNGOL-UHFFFAOYSA-O SMILEShelp_outline C[NH2+]C 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
methyl-Co(III)-[dimethylamine-specific corrinoid protein]
Identifier
RHEA-COMP:11122
Reactive part
help_outline
- Name help_outline methyl-Co(III) Identifier CHEBI:85035 Charge 2 Formula CH3Co InChIKeyhelp_outline YMTZLGGIBUNCMX-UHFFFAOYSA-N SMILEShelp_outline C[Co++] 2D coordinates Mol file for the small molecule Search links Involved in 29 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline methylamine Identifier CHEBI:59338 Charge 1 Formula CH6N InChIKeyhelp_outline BAVYZALUXZFZLV-UHFFFAOYSA-O SMILEShelp_outline C[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 27 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:41175 | RHEA:41176 | RHEA:41177 | RHEA:41178 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases.
Krzycki J.A.
Methanogenesis from trimethylamine, dimethylamine or monomethylamine is initiated by a series of corrinoid-dependent methyltransferases. The non-homologous genes encoding the full-length methyltransferases each possess an in-frame UAG (amber) codon that does not terminate translation. The amber co ... >> More
Methanogenesis from trimethylamine, dimethylamine or monomethylamine is initiated by a series of corrinoid-dependent methyltransferases. The non-homologous genes encoding the full-length methyltransferases each possess an in-frame UAG (amber) codon that does not terminate translation. The amber codon is decoded by a dedicated tRNA, and corresponds to the novel amino acid pyrrolysine in one of the methyltransferases, indicating pyrrolysine to be the 22nd genetically encoded amino acid. Pyrrolysine has the structure of lysine with the (epsilon)N in amide linkage with a pyrroline ring. The reactivity of the electrophilic imine bond is the basis for the proposed function of pyrrolysine in activating and optimally orienting methylamine for methyl transfer to the cobalt ion of a cognate corrinoid protein. This reaction is essential for methane formation from methylamines, and may underlie the retention of pyrrolysine in the genetic code of methanogens. << Less
Curr Opin Chem Biol 8:484-491(2004) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Purification and characterization of dimethylamine:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri Fusaro.
Wassenaar R.W., Keltjens J.T., van der Drift C., Vogels G.D.
Dimethylamine:5-hydroxybenzimidazolylcobamide methyltransferase (DMA-MT) was purified from cells of Methanosarcina barkeri Fusaro grown on trimethylamine. In the presence of methylcobalamine:coenzyme M methyltransferase isoenzyme II [MT2(II)] the enzyme quite specifically catalyzed the stoichiomet ... >> More
Dimethylamine:5-hydroxybenzimidazolylcobamide methyltransferase (DMA-MT) was purified from cells of Methanosarcina barkeri Fusaro grown on trimethylamine. In the presence of methylcobalamine:coenzyme M methyltransferase isoenzyme II [MT2(II)] the enzyme quite specifically catalyzed the stoichiometric conversion of dimethylamine (apparent Km = 0.45 mM) and 2-mercaptoethane-sulfonate (coenzyme M) to monomethylamine and methyl-coenzyme M. Monomethylamine was a competitive inhibitor of the reaction (Ki = 4.5 mM). The apparent molecular mass of DMA-MT was 100 kDa and the enzyme was found to be a dimer, composed of identical 50-kDa subunits. A corrinoid content of 0.9 +/-0.1 mol B12/mol holoenzyme was calculated from HPLC analysis. The as-isolated methyltransferase was inactive, but it could be reductively reactivated. Activation required the presence of methyltransferase-activating protein, ATP and dimethylamine. Incubation with these compounds resulted in the methylation of the corrinoid prosthetic group. << Less
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Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri.
Ferguson D.J. Jr., Gorlatova N., Grahame D.A., Krzycki J.A.
Methyl transfer from dimethylamine to coenzyme M was reconstituted in vitro for the first time using only highly purified proteins. These proteins isolated from Methanosarcina barkeri included the previously unidentified corrinoid protein MtbC, which copurified with MtbA, the methylcorrinoid:Coenz ... >> More
Methyl transfer from dimethylamine to coenzyme M was reconstituted in vitro for the first time using only highly purified proteins. These proteins isolated from Methanosarcina barkeri included the previously unidentified corrinoid protein MtbC, which copurified with MtbA, the methylcorrinoid:Coenzyme M methyltransferase specific for methanogenesis from methylamines. MtbC binds 1.0 mol of corrinoid cofactor/mol of 24-kDa polypeptide and stimulated dimethylamine:coenzyme M methyl transfer 3.4-fold in a cell extract. Purified MtbC and MtbA were used to assay and purify a dimethylamine:corrinoid methyltransferase, MtbB1. MtbB1 is a 230-kDa protein composed of 51-kDa subunits that do not possess a corrinoid prosthetic group. Purified MtbB1, MtbC, and MtbA were the sole protein requirements for in vitro dimethylamine:coenzyme M methyl transfer. An MtbB1:MtbC ratio of 1 was optimal for coenzyme M methylation with dimethylamine. MtbB1 methylated either corrinoid bound to MtbC or free cob(I)alamin with dimethylamine, indicating MtbB1 carries an active site for dimethylamine demethylation and corrinoid methylation. Experiments in which different proteins of the resolved monomethylamine:coenzyme M methyl transfer reaction replaced proteins involved in dimethylamine:coenzyme M methyl transfer indicated high specificity of MtbB1 and MtbC in dimethylamine:coenzyme M methyl transfer activity. These results indicate MtbB1 demethylates dimethylamine and specifically methylates the corrinoid prosthetic group of MtbC, which is subsequently demethylated by MtbA to methylate coenzyme M during methanogenesis from dimethylamine. << Less
J. Biol. Chem. 275:29053-29060(2000) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
Comments
As the precise nature of the cobalamin present in the corrinoid protein is not known, it has not been included in the reactive part of the macromolecule.