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Literature summary for 4.2.1.17 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)

Cloned (Comment) Organism
expression in Pichia pastoris Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
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

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P14604
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Rattus norvegicus

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
multifunctional enzyme type 1
-
Rattus norvegicus
perMFE-1
-
Rattus norvegicus