cDNA cloning and amino acid sequence of human mitochondrial delta 3 delta 2-enoyl-CoA isomerase: comparison of the human enzyme with its rat counterpart, mitochondrial short-chain isomerase.
We report the isolation of a cDNA encoding a mature human monofunctional delta 3 delta 2-enoyl-CoA isomerase and the determination of its nucleotide sequence. The purified uncleaved protein, as well as several internal tryptic and CNBr fragments, were subjected to N-terminal peptide sequencing. The deduced amino acid sequence of the mature protein consists of 260 amino acids with a predicted M(r) of 28735. The human mitochondrial isomerase exhibits a 74% (78%) sequence identity with the corresponding rat counterpart at amino acid (nucleotide) level(s). Many basic amino acid residues in rat isomerase have been changed to acidic or neutral residues in human enzyme, explaining the differences observed between these proteins.
Kilponen
J M
JM
Biocenter Oulu, Finland.
Häyrinen
H M
HM
Rehn
M
M
Hiltunen
J K
JK
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D019748:Carbon-Carbon Double Bond Isomerases; D003001:Cloning, Molecular; D018076:DNA, Complementary; D064006:Dodecenoyl-CoA Isomerase; D006801:Humans; D007535:Isomerases / Q000235:genetics*; D008930:Mitochondria, Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D051381:Rats; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D007535:Isomerases; D019748:Carbon-Carbon Double Bond Isomerases; D064006:Dodecenoyl-CoA Isomerase; C576298:ECI1 protein, human; C119738:ECI2 protein, human