5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase

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5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase
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EC no. 2.1.1.245
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5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase (EC 2.1.1.245, cdhD (gene), cdhE (gene)) is an enzyme with systematic name 5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein methyltransferase. [1] [2] This enzyme catalyses the following chemical reaction:

[methyl-Co(III) corrinoid Fe-S protein] + tetrahydrosarcinapterin [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrosarcinapterin

This enzyme catalyses the transfer of a methyl group from the cobamide cofactor of a corrinoid/Fe-S protein to the N5 group of tetrahydrosarcinapterin.

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In the chemical sciences, methylation denotes the addition of a methyl group on a substrate, or the substitution of an atom by a methyl group. Methylation is a form of alkylation, with a methyl group replacing a hydrogen atom. These terms are commonly used in chemistry, biochemistry, soil science, and the biological sciences.

<span class="mw-page-title-main">Nitrogenase</span> Class of enzymes

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<span class="mw-page-title-main">Aconitase</span> Class of enzymes

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<span class="mw-page-title-main">Methyltransferase</span> Group of methylating enzymes

Methyltransferases are a large group of enzymes that all methylate their substrates but can be split into several subclasses based on their structural features. The most common class of methyltransferases is class I, all of which contain a Rossmann fold for binding S-Adenosyl methionine (SAM). Class II methyltransferases contain a SET domain, which are exemplified by SET domain histone methyltransferases, and class III methyltransferases, which are membrane associated. Methyltransferases can also be grouped as different types utilizing different substrates in methyl transfer reactions. These types include protein methyltransferases, DNA/RNA methyltransferases, natural product methyltransferases, and non-SAM dependent methyltransferases. SAM is the classical methyl donor for methyltransferases, however, examples of other methyl donors are seen in nature. The general mechanism for methyl transfer is a SN2-like nucleophilic attack where the methionine sulfur serves as the leaving group and the methyl group attached to it acts as the electrophile that transfers the methyl group to the enzyme substrate. SAM is converted to S-Adenosyl homocysteine (SAH) during this process. The breaking of the SAM-methyl bond and the formation of the substrate-methyl bond happen nearly simultaneously. These enzymatic reactions are found in many pathways and are implicated in genetic diseases, cancer, and metabolic diseases. Another type of methyl transfer is the radical S-Adenosyl methionine (SAM) which is the methylation of unactivated carbon atoms in primary metabolites, proteins, lipids, and RNA.

<span class="mw-page-title-main">Dihydropteroate synthase</span> Class of enzymes

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<span class="mw-page-title-main">Protein-glutamate O-methyltransferase</span>

In enzymology, a protein-glutamate O-methyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Biotin synthase</span> Enzyme

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(Methyl-Co methanol-specific corrinoid protein):coenzyme M methyltransferase is an enzyme with systematic name methylated methanol-specific corrinoid protein:coenzyme M methyltransferase. This enzyme catalyses the following chemical reaction

(Methyl-Co methylamine-specific corrinoid protein):coenzyme M methyltransferase is an enzyme with systematic name methylated monomethylamine-specific corrinoid protein:coenzyme M methyltransferase. This enzyme catalyses the following chemical reaction

Methylamine-corrinoid protein Co-methyltransferase is an enzyme with systematic name monomethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase. This enzyme catalyses the following chemical reaction

Dimethylamine-corrinoid protein Co-methyltransferase is an enzyme with systematic name dimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase. This enzyme catalyses the following chemical reaction

Trimethylamine-corrinoid protein Co-methyltransferase is an enzyme with systematic name trimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase. This enzyme catalyses the following chemical reaction

Methylated-thiol-coenzyme M methyltransferase is an enzyme with systematic name methylated-thiol:coenzyme M methyltransferase. This enzyme catalyses the following chemical reaction:

Tetramethylammonium-corrinoid protein Co-methyltransferase is an enzyme with systematic name tetramethylammonium:5-hydroxybenzimidazolylcobamide Co-methyltransferase. This enzyme catalyses the following chemical reaction

(Methyl-Co tetramethylammonium-specific corrinoid protein):coenzyme M methyltransferase is an enzyme with systematic name methylated tetramethylammonium-specific corrinoid protein:coenzyme M methyltransferase. This enzyme catalyses the following chemical reaction

5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase is an enzyme with systematic name 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">CO-methylating acetyl-CoA synthase</span>

Acetyl-CoA synthase (ACS), not to be confused with Acetyl-CoA synthetase or Acetate-CoA ligase, is a nickel-containing enzyme involved in the metabolic processes of cells. Together with Carbon monoxide dehydrogenase (CODH), it forms the bifunctional enzyme Acetyl-CoA Synthase/Carbon Monoxide Dehydrogenase (ACS/CODH) found in anaerobic organisms such as archaea and bacteria. The ACS/CODH enzyme works primarily through the Wood–Ljungdahl pathway which converts carbon dioxide to Acetyl-CoA. The recommended name for this enzyme is CO-methylating acetyl-CoA synthase.

<span class="mw-page-title-main">Cobamide</span> Chemical compound

Cobamide is a naturally occurring chemical compound containing cobalt in the corrinoid family of macrocyclic complexes. Cobamide works as a coenzyme with some enzymes in bacteria. The cobalt atom may have a transferable methyl group attached. It is used for example in 5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase.

References

  1. Maupin-Furlow J, Ferry JG (January 1996). "Characterization of the cdhD and cdhE genes encoding subunits of the corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from Methanosarcina thermophila". Journal of Bacteriology. 178 (2): 340–6. PMC   177663 . PMID   8550451.
  2. Grahame DA, DeMoll E (April 1996). "Partial reactions catalyzed by protein components of the acetyl-CoA decarbonylase synthase enzyme complex from Methanosarcina barkeri". The Journal of Biological Chemistry. 271 (14): 8352–8. doi: 10.1074/jbc.271.14.8352 . PMID   8626532.