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Catalysis of the ligation of a fatty acid to an acceptor, coupled to the hydrolysis of ATP. Catalysis of the reaction: hydrogen (2R,3S)-3-methyloxiran-2-ylphosphonic acid + glutathione = hydrogen (1R,2R)-1-glutathio-2-hydroxypropylphosphonic acid. Catalysis of the reaction: hydrogen (2R,3S)-3-methyloxiran-2-ylphosphonic acid + L-cysteine = hydrogen (1R,2R)-1- L-cysteine-2-hydroxypropylphosphonic acid. Catalysis of the ligation of two substances with concomitant breaking of a diphosphate linkage, usually in a nucleoside triphosphate. Ligase is the systematic name for any enzyme of EC class 6. Catalysis of the reaction: substrate + ATP + CoASH = AMP + diphosphate + substrate-CoA. Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. Catalysis of the ligation of an acid and a thiol via a carbon-sulfur bond with concomitant breakage of a diphosphate linkage, usually in a nucleoside triphosphate. Catalysis of the ligation of two substances via a carbon-sulfur bond with concomitant breakage of a diphosphate linkage, usually in a nucleoside triphosphate.

View Gene Ontology (GO) Term

GO TERM SUMMARY

Name: ligase activity, forming carbon-sulfur bonds
Acc: GO:0016877
Aspect: Molecular Function
Desc: Catalysis of the ligation of two substances via a carbon-sulfur bond with concomitant breakage of a diphosphate linkage, usually in a nucleoside triphosphate.
Synonyms:
  • ligase activity, forming carbon-sulphur bonds
Proteins in PDR annotated with:
   This term: 2 [Search]
   Term or descendants: 254 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0016877 - ligase activity, forming carbon-sulfur bonds (interactive image map)

YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle