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AMINO-ACID-SEQUENCE SIMILARITIES OF THE MITOCHONDRIAL SHORT CHAIN DELTA-3,DELTA-2-ENOYL-COA ISOMERASE AND PEROXISOMAL MULTIFUNCTIONAL DELTA-3,DELTA-2-ENOYL-COA ISOMERASE, 2-ENOYL-COA HYDRATASE, 3-HYDROXYACYL-COA DEHYDROGENASE ENZYME IN RAT-LIVER - THE PROPOSED OCCURRENCE OF ISOMERIZATION AND HYDRATION IN THE SAME CATALYTIC DOMAIN OF THE MULTIFUNCTIONAL ENZYME

PALOSAARI, PM; Vihinen, Mauno LU ; MANTSALA, PI; ALEXSON, SEH; PIHLAJANIEMI, T and HILTUNEN, JK (1991) In Journal of Biological Chemistry 266(17). p.10750-10753
Abstract
We report the isolation and characterization of a cDNA encoding the mitochondrial short chain DELTA-3,DELTA-2-enoyl-CoA isomerase from rat liver. Tryptic fragments of the purified protein were generated, purified, and sequenced. A rat liver cDNA library, constructed in the plasmid vector pUEX1 was screened with oligonucleotides synthesized on the basis of peptide sequences. The obtained clone contained 783 bases predicting to code the entire mature protein of 261 amino acids. The molecular weight of 29,300 predicted from cDNA-derived sequences was consistent with the subunit size determined earlier. A high degree of similarity was noted between the amino acid sequence of isomerase and that of the amino-terminal half of peroxisomal... (More)
We report the isolation and characterization of a cDNA encoding the mitochondrial short chain DELTA-3,DELTA-2-enoyl-CoA isomerase from rat liver. Tryptic fragments of the purified protein were generated, purified, and sequenced. A rat liver cDNA library, constructed in the plasmid vector pUEX1 was screened with oligonucleotides synthesized on the basis of peptide sequences. The obtained clone contained 783 bases predicting to code the entire mature protein of 261 amino acids. The molecular weight of 29,300 predicted from cDNA-derived sequences was consistent with the subunit size determined earlier. A high degree of similarity was noted between the amino acid sequence of isomerase and that of the amino-terminal half of peroxisomal multifunctional isomerase-hydratase-dehydrogenase enzyme and mitochondrial 2-enoyl-CoA hydratase in rat liver. These similarities also appeared at the level of predicted secondary structural elements, suggesting that the rat multifunctional enzyme has both the isomerization and hydration activities in the amino-terminal domain. This idea is further supported by the proposed existence of only one CoA-binding site in the amino-terminal half of the multifunctional enzyme and by previous studies suggesting that the transfer of the substrate from the isomerization site to the hydration site occurs without aqueous bulk phase (Palosaari P. M., and Hiltunen, J. K. (1990) J. Biol. Chem. 265, 2446-2449). (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
266
issue
17
pages
10750 - 10753
publisher
ASBMB
external identifiers
  • wos:A1991FQ77400010
ISSN
1083-351X
language
English
LU publication?
no
id
f9480bc9-8b1a-4e71-b47c-bac3bc4f3be8 (old id 3853524)
date added to LUP
2013-06-28 15:18:36
date last changed
2016-06-29 08:55:06
@article{f9480bc9-8b1a-4e71-b47c-bac3bc4f3be8,
  abstract     = {We report the isolation and characterization of a cDNA encoding the mitochondrial short chain DELTA-3,DELTA-2-enoyl-CoA isomerase from rat liver. Tryptic fragments of the purified protein were generated, purified, and sequenced. A rat liver cDNA library, constructed in the plasmid vector pUEX1 was screened with oligonucleotides synthesized on the basis of peptide sequences. The obtained clone contained 783 bases predicting to code the entire mature protein of 261 amino acids. The molecular weight of 29,300 predicted from cDNA-derived sequences was consistent with the subunit size determined earlier. A high degree of similarity was noted between the amino acid sequence of isomerase and that of the amino-terminal half of peroxisomal multifunctional isomerase-hydratase-dehydrogenase enzyme and mitochondrial 2-enoyl-CoA hydratase in rat liver. These similarities also appeared at the level of predicted secondary structural elements, suggesting that the rat multifunctional enzyme has both the isomerization and hydration activities in the amino-terminal domain. This idea is further supported by the proposed existence of only one CoA-binding site in the amino-terminal half of the multifunctional enzyme and by previous studies suggesting that the transfer of the substrate from the isomerization site to the hydration site occurs without aqueous bulk phase (Palosaari P. M., and Hiltunen, J. K. (1990) J. Biol. Chem. 265, 2446-2449).},
  author       = {PALOSAARI, PM and Vihinen, Mauno and MANTSALA, PI and ALEXSON, SEH and PIHLAJANIEMI, T and HILTUNEN, JK},
  issn         = {1083-351X},
  language     = {eng},
  number       = {17},
  pages        = {10750--10753},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {AMINO-ACID-SEQUENCE SIMILARITIES OF THE MITOCHONDRIAL SHORT CHAIN DELTA-3,DELTA-2-ENOYL-COA ISOMERASE AND PEROXISOMAL MULTIFUNCTIONAL DELTA-3,DELTA-2-ENOYL-COA ISOMERASE, 2-ENOYL-COA HYDRATASE, 3-HYDROXYACYL-COA DEHYDROGENASE ENZYME IN RAT-LIVER - THE PROPOSED OCCURRENCE OF ISOMERIZATION AND HYDRATION IN THE SAME CATALYTIC DOMAIN OF THE MULTIFUNCTIONAL ENZYME},
  volume       = {266},
  year         = {1991},
}