Noda C, Ito K, Nakamura T, Ichihara A
Institute for Enzyme Research, University of Tokushima, Japan.
FEBS Lett. 1988 Jul 18;234(2):331-5. doi: 10.1016/0014-5793(88)80110-8.
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 34,462 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.
大鼠肝脏丝氨酸脱水酶mRNA的核苷酸序列已从先前在本实验室克隆的重组cDNA克隆以及从引物延伸cDNA文库筛选出的重组cDNA克隆中确定。1322个核苷酸的序列包括整个蛋白质编码区以及3'端和5'端的非编码区。推导的多肽由327个氨基酸残基组成，计算分子量为34,462道尔顿。将丝氨酸脱水酶多肽的氨基酸序列与酵母生物合成苏氨酸脱水酶和大肠杆菌生物降解苏氨酸脱水酶的氨基酸序列进行比较，发现了不同程度的同源性。一个七肽序列Gly-Ser-Phe-Lys-Ile-Arg-Gly，它是酵母和大肠杆菌苏氨酸脱水酶中的吡哆醛结合位点，被发现是一个高度保守的序列。
