Literature summary for 4.2.1.17 extracted from

Jabeen, U.; Salim, A.
Sequence analysis and structure prediction of enoyl-CoA hydratase from Avicennia marina: implication of various amino acid residues on substrate-enzyme interactions (2013), Phytochemistry, 94, 36-44.

Search for more literature for 4.2.1.17

Inhibitors

Inhibitors	Comment	Organism	Structure
acetoacetyl-CoA	competitive inhibitor, binding structure, overview	Avicennia marina
octanoyl-CoA	competitive inhibitor, binding structure, overview	Avicennia marina

Organism

Organism	UniProt	Comment	Textmining
Avicennia marina	Q9SE41	-	-

Synonyms

Synonyms	Comment	Organism
AMECH	-	Avicennia marina

General Information

General Information	Comment	Organism
additional information	identification of residues involved in the ligand-enzyme interaction, homology modeling: the carbonyl group of hexadienoyl-CoA forms H-bonds with Ala32, Gly34, Val36 and Gly83. Phosphate groups of the substrate form two ionic bonds with Arg28. The enzyme shows few distinct structural changes which include structural variation in the mobile loop, formation and loss of certain interactions between the active site residues and substrates. AMECH is a monofunctional enzyme and has one catalytic glutamic acid Glu106, an essential catalytic residue. Asp114 might also be involved in the reaction mechanism, overview	Avicennia marina
physiological function	enoyl-CoA hydratase is one of the enzymes involved in the peroxisomal beta-oxidation cycle	Avicennia marina

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)