Literature summary 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.

Inhibitors

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.2.1.17	Avicennia marina	Q9SE41	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
4.2.1.17	AMECH	-	Avicennia marina

General Information

EC Number	General Information	Comment	Organism
4.2.1.17	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
4.2.1.17	physiological function	enoyl-CoA hydratase is one of the enzymes involved in the peroxisomal beta-oxidation cycle	Avicennia marina

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Release 2023.1 (January 2023)