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Literature summary 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)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.17 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

EC Number Localization Comment Organism GeneOntology No. Textmining
4.2.1.17 peroxisome
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Rattus norvegicus 5777
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Organism

EC Number Organism UniProt Comment Textmining
4.2.1.17 Rattus norvegicus P07896
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-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.17 purified from rat liver Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.2.1.17 liver
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Rattus norvegicus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.17 (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
-
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Synonyms

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

General Information

EC Number General Information Comment Organism
4.2.1.17 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