Rat peroxisomal multifunctional enzyme type 1 (perMFE-1) is a monomeric protein of β-oxidation. We have defined five functional domains (A, B, C, D and E) in the perMFE-1 based on comparison of the amino acid sequence with homologous proteins from databases and structural data of the hydratase-1/isomerases (H1/I) and (3S)-hydroxyacyl-CoA dehydrogenases (HAD). Domain A (residues 1—190) comprises the H1/I fold and catalyses both 2-enoyl-CoA hydratase-1 and Δ3—Δ2-enoyl-CoA isomerase reactions. Domain B (residues 191—280) links domain A to the (3S)-dehydrogenase region, which includes both domain C (residues 281—474) and domain D (residues 480—583). Domains C and D carry features of the dinucleotide-binding and the dimerization domains of monofunctional HADs respectively. Domain E (residues 584—722) has sequence similarity to domain D of the perMFE-1, which suggests that it has evolved via partial gene duplication. 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—479)Δ, in which the domain C is deleted, is stable and has hydratase-1 activity. It is proposed that the extreme C-terminal domain E in perMFE-1 serves the following three functions: (i) participation in the folding of the N-terminus into a functionally competent H1/I fold, (ii) stabilization of the dehydrogenation domains by interaction with the domain D and (iii) the targeting of the perMFE-1 to peroxisomes via its C-terminal tripeptide.
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October 2002
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Research Article|
October 15 2002
Organization of the multifunctional enzyme type 1: interaction between N- and C-terminal domains is required for the hydratase-1/isomerase activity
Tiila-Riikka KIEMA;
Tiila-Riikka KIEMA
∗Biocenter Oulu and Department of Biochemistry, University of Oulu, P.O. Box 3000, FIN-90014, Finland,
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Jukka P. TASKINEN;
Jukka P. TASKINEN
∗Biocenter Oulu and Department of Biochemistry, University of Oulu, P.O. Box 3000, FIN-90014, Finland,
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Päivi L. PIRILÄ;
Päivi L. PIRILÄ
∗Biocenter Oulu and Department of Biochemistry, University of Oulu, P.O. Box 3000, FIN-90014, Finland,
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Kari T. KOIVURANTA;
Kari T. KOIVURANTA
∗Biocenter Oulu and Department of Biochemistry, University of Oulu, P.O. Box 3000, FIN-90014, Finland,
†VTT Biotechnology, P.O. Box 1500, FIN-02044 VTT, Finland
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Rik K. WIERENGA;
Rik K. WIERENGA
∗Biocenter Oulu and Department of Biochemistry, University of Oulu, P.O. Box 3000, FIN-90014, Finland,
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J. Kalervo HILTUNEN
J. Kalervo HILTUNEN
1
∗Biocenter Oulu and Department of Biochemistry, University of Oulu, P.O. Box 3000, FIN-90014, Finland,
1To whom correspondence should be addressed (e-mail Kalervo.Hiltunen@oulu.fi).
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Publisher: Portland Press Ltd
Received:
February 19 2002
Revision Received:
June 18 2002
Accepted:
July 10 2002
Accepted Manuscript online:
July 10 2002
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London ©2002
2002
Biochem J (2002) 367 (2): 433–441.
Article history
Received:
February 19 2002
Revision Received:
June 18 2002
Accepted:
July 10 2002
Accepted Manuscript online:
July 10 2002
Citation
Tiila-Riikka KIEMA, Jukka P. TASKINEN, Päivi L. PIRILÄ, Kari T. KOIVURANTA, Rik K. WIERENGA, J. Kalervo HILTUNEN; Organization of the multifunctional enzyme type 1: interaction between N- and C-terminal domains is required for the hydratase-1/isomerase activity. Biochem J 15 October 2002; 367 (2): 433–441. doi: https://doi.org/10.1042/bj20020292
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