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Literature summary for 4.2.1.17 extracted from

  • Kasaragod, P.; Venkatesan, R.; Kiema, T.R.; Hiltunen, J.K.; Wierenga, R.K.
    The crystal structure of liganded rat peroxisomal multifunctional enzyme type 1: a flexible molecule with two interconnected active sites (2010), J. Biol. Chem., 285, 24089-24098.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichis coli BL21(DE3) Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
at 2.8 A resolution, multidomain protein having 5 domains: A, B, C, D, and E. The N-terminal part has a crotonase fold, which builds the active site for the DELTA3,DELTA2-enoyl-CoA isomerase (EC 5.3.3.8) and DELTA2-enoyl-CoA hydratase-1 Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome
-
Rattus norvegicus 5777
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P07896
-
-

Purification (Commentary)

Purification (Comment) Organism
purified from rat liver Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E)-enoyl-CoA + H2O 2E-enoyl-CoA is the product of the DELTA3,DELTA2-enoyl-CoA isomerase (EC 5.3.3.8) reaction, which subsequently is converted into (3S)-hydroxyacyl-CoA in the hydration step Rattus norvegicus (3S)-hydroxyacyl-CoA
-
?

Synonyms

Synonyms Comment Organism
DELTA2-enoyl-CoA hydratase-1
-
Rattus norvegicus
rat peroxisomal multifunctional enzyme type 1
-
Rattus norvegicus
rpMFE1
-
Rattus norvegicus

General Information

General Information Comment Organism
physiological function the multifunctional enzyme is involved in an alpha-methylacyl-CoAracemase-MFE2 independent synthesis pathway of bile acids from (24S)-hydroxyoxisterols, is involved in the beta-oxidation of long chain dicarboxylic acids Rattus norvegicus