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Literature summary for 6.2.1.1 extracted from

  • Abe, T.; Hashimoto, Y.; Hosaka, H.; Tomita-Yokotani, K.; Kobayashi, M.
    Discovery of amide (peptide) bond synthetic activity in acyl-CoA synthetase (2008), J. Biol. Chem., 283, 11312-11321.
    View publication on PubMed
Search for more literature for 6.2.1.1

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + acetate + CoA Saccharomyces cerevisiae
-
 AMP + diphosphate + acetyl-CoA
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation highly purified enzyme Saccharomyces cerevisiae
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + acetate + CoA
-
 Saccharomyces cerevisiae AMP + diphosphate + acetyl-CoA
-
 ?
additional information the enzyme also forms a carbon-nitrogen bond, reaction of EC 6.3.1 acid-ammonia (or amide) ligase, i.e. amide synthase, and EC 6.3.2 acid-amino acid ligase, i.e. peptide synthase, comprising the amino group of the cysteine and the carboxyl group of the acid, overview Saccharomyces cerevisiae ?
-
 ?

Synonyms

Synonyms Comment Organism
Acetyl-CoA synthetase
-
 Saccharomyces cerevisiae
More acetyl-CoA synthetase belongs to the superfamily of adenylate-forming enzymes, whose three-dimensional structures are analogous to one another Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
 assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Saccharomyces cerevisiae