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Literature summary extracted from

  • Mathieu, M.; Modis, Y.; Zeelen, J.P.; Engel, C.K.; Abagyan, R.A.; Ahlberg, A.; Rasmussen, B.; Lamzin, V.S.; Kunau, W.H.; Wierenga, R.K.
    The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism (1997), J. Mol. Biol., 273, 714-728.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.16
-
 Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.16 CoA + 3-oxoacyl-CoA Saccharomyces cerevisiae enzyme catalyses the last step in the beta-oxidation cycle acyl-CoA + acetyl-CoA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.16 Saccharomyces cerevisiae P27796
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.16 acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA reaction mechanism Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.16 CoA + 3-oxoacyl-CoA two-step reaction Saccharomyces cerevisiae acyl-CoA + acetyl-CoA
-
 r
2.3.1.16 CoA + 3-oxoacyl-CoA enzyme catalyses the last step in the beta-oxidation cycle Saccharomyces cerevisiae acyl-CoA + acetyl-CoA
-
 ?
2.3.1.16 additional information the active site of thiolase can also catalyse the synthesis of acetyl-Co from two molecules of acetyl-CoA Saccharomyces cerevisiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.16 dimer
-
 Saccharomyces cerevisiae
2.3.1.16 More the high sequence similarity between the tetrameric and dimeric thiolases suggests that the tetrameric thiolases are assemble as a dimer of two thiolase dimers Saccharomyces cerevisiae