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Primary structure of rat liver serine dehydratase deduced from the cDNA sequence
Author(s) -
Noda Chiseko,
Ito Keiko,
Nakamura Toshikazu,
Ichihara Akira
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80110-8
Subject(s) - complementary dna , biochemistry , nucleic acid sequence , dehydratase , biology , peptide sequence , microbiology and biotechnology , protein primary structure , threonine , amino acid , serine , cdna library , enzyme , dna , gene
The nucleotide sequence of serine dehydratase mRNA of rat liver has been determined from a recombinant cDNA clone, previously cloned in this laboratory, and from a recombinant cDNA clone screened from a primer‐extended cDNA library. The sequence of 1322 nucleotides includes the entire protein coding region and noncoding regions on the 3′‐ and 5′‐sides. The deduced polypeptide consists of 327 amino acid residues with a calculated molecular mass of 34462 Da. Comparison of the amino acid sequences of the serine dehydratase polypeptide with those of biosynthetic threonine dehydratase of yeast and biodegradative threonine dehydratase of E. coli revealed various extents of homology. A heptapeptide sequence, Gly‐Ser‐Phe‐Lys‐Ile‐Arg‐Gly, which is the pyridoxal‐binding site in the yeast and E. coli threonine dehydratases, was found as a highly conserved sequence.