Literature summary for 4.2.1.17 extracted from

Alipui, O.D.; Zhang, D.; Schulz, H.
Direct hydration of 3-octynoyl-CoA by crotonase: A missing link in Konrad Bloch's enzymatic studies with 3-alkynoyl thioesters (2002), Biochem. Biophys. Res. Commun., 292, 1171-1174.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	the classification is ambiguous because the stereochemistry is not exactly determined	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
420	-	hydration of 3-octynoyl-CoA	Escherichia coli
650	-	hydration of 2,3-octadienoyl-CoA	Escherichia coli
973	-	hydration of 2-trans-octenoyl-CoA	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2,3-octadienoyl-CoA + H2O	the classification is ambiguous because the stereochemistry is not exactly determined	Escherichia coli	3-ketooctanoyl-CoA	-	?
2-trans-octenoyl-CoA + H2O	the classification is ambiguous because the stereochemistry is not exactly determined	Escherichia coli	3-hydroxyoctanoyl-CoA	-	?
3-octynoyl-CoA + H2O	2,3-octadienoyl-CoA is an intermediate. The classification is ambiguous because the stereochemistry is not exactly determined	Escherichia coli	3-ketooctanoyl-CoA	-	?

Synonyms

Synonyms	Comment	Organism
crotonase	the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined	Escherichia coli

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Release 2023.1 (January 2023)