Literature summary for 5.3.3.8 extracted from

Partanen, S.T.; Novikov, D.K.; Popov, A.N.; Mursula, A.M.; Hiltunen, J.K.; Wierenga, R.K.
The 1.3 A crystal structure of human mitochondrial DELTA3-DELTA2-enoyl-CoA isomerase shows a novel mode of binding for the fatty acyl group (2004), J. Mol. Biol., 342, 1197-1208.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of DELTA3,DELTA2-enoyl-CoA isomerase complexed with the substrate analogue octanoyl-CoA has been refined a 1.3 angstrom resolution	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
E136A	variant to study the importance of Glu136 for catalysis	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Homo sapiens	5739	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P42126	-	-

Purification (Commentary)

Purification (Comment)	Organism
gel filtration	Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	catalytic activity of E136A variant below detection limit	Homo sapiens
21	-	human mitochondrial DELTA3,DELTA2-enoyl-CoA-isomerase	Homo sapiens

Subunits

Subunits	Comment	Organism
trimer	crystallographic analysis	Homo sapiens

Synonyms

Synonyms	Comment	Organism
DELTA3,DELTA2-enoyl-CoA isomerase	-	Homo sapiens

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Release 2023.1 (January 2023)