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Literature summary extracted from

  • Kiema, T.R.; Taskinen, J.P.; Pirilae, P.L.; Koivuranta, K.T.; Wierenga, R.K.; Hiltunen, J.K.
    Organization of the multifunctional enzyme type 1: interaction between N- and C-terminal domains is required for the hydratase-1/isomerase activity (2002), Biochem. J., 367, 433-441.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.17 expression in Pichia pastoris Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.17 additional information experiments with engineered perMFE-1 variants demonstrate that the H1/I competence of domain A requires stabilizing interactions with domains D and E. The variant His-perMFE (residues 288-79)DELTA, in which the domain C is deleted, is stable and has hydratase-1 activity Rattus norvegicus

Localization

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

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.17 Rattus norvegicus P14604
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.17 recombinant enzyme Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.17 trans-2-decenoyl-CoA + H2O
-
 Rattus norvegicus (3S)-hydroxydecanoyl-CoA
-
 ?
4.2.1.17 trans-2-hexenoyl-CoA + H2O
-
 Rattus norvegicus (3S)-3-hydroxyhexanoyl-CoA
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.17 More perMFE-1 can be divided into ®ve separate domains or parts Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
4.2.1.17 multifunctional enzyme type 1
-
 Rattus norvegicus
4.2.1.17 perMFE-1
-
 Rattus norvegicus