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Literature summary for 6.2.1.76 extracted from

  • Jung, J.W.; An, J.H.; Na, K.B.; Kim, Y.S.; Lee, W.
    The active site and substrates binding mode of malonyl-CoA synthetase determined by transferred nuclear Overhauser effect spectroscopy, site-directed mutagenesis, and comparative modeling studies (2000), Protein Sci., 9, 1294-1303 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
K170M mutant enzyme retains 35% of its activity Rhizobium leguminosarum
R168G mutation reduces 63% of enzyme activity Rhizobium leguminosarum
R168G/K170M the mutant enzyme retains 12% of its activity Rhizobium leguminosarum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + malonate + CoA Rhizobium leguminosarum
-
 AMP + diphosphate + malonyl-CoA
-
 ?

Organism

Organism UniProt Comment Textmining
Rhizobium leguminosarum Q9ZIP5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + malonate + CoA
-
 Rhizobium leguminosarum AMP + diphosphate + malonyl-CoA
-
 ?

Synonyms

Synonyms Comment Organism
MCS
-
 Rhizobium leguminosarum