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Thiol S-methyltransferase

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thiol S-methyltransferase
Identifiers
EC no.2.1.1.9
CAS no.9029-81-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a thiol S-methyltransferase (EC 2.1.1.9) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + a thiol {\displaystyle \rightleftharpoons } S-adenosyl-L-homocysteine + a thioether

Thus, the two substrates of this enzyme are S-adenosyl methionine and thiol, whereas its two products are S-adenosylhomocysteine and thioether.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:thiol S-methyltransferase. Other names in common use include S-methyltransferase, thiol methyltransferase, and TMT. This enzyme participates in selenoamino acid metabolism.

References

Transferase: one carbon transferases (EC 2.1)
2.1.1: Methyl-
N-
O-
Homocysteine
Other
2.1.2: Hydroxymethyl-,
Formyl- and Related
Hydroxymethyltransferase
Formyltransferase
Other
2.1.3: Carboxy-
and Carbamoyl
Carboxy
Carbamoyl
2.1.4: Amidine
Enzymes
Activity
Regulation
Classification
Kinetics
Types
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