ABSTRACT
Two cDNAs encoding rice (Oryza sativa L.) S-adenosyl-L-methionine synthetase (SAMS) have been cloned, sequenced and identified. The deduced protein sequences share a high homology (90-94%) with those of other plant SAMS and are 60-62% identical to yeast, rat and human SAMS. The rice SAMS genes are differentially regulated in a tissue-specific manner and by a salt stress, while they are coordinately expressed during growth of the rice cell culture.
Subject(s)
Methionine Adenosyltransferase/genetics , Oryza/genetics , Amino Acid Sequence , Animals , Base Sequence , Cloning, Molecular , DNA, Complementary , Humans , Molecular Sequence Data , Oryza/enzymology , Restriction Mapping , Sequence Homology, Amino AcidABSTRACT
A peptide having enzyme-like catalytic activity has been designed and synthesized. Computer modeling was used to design a bundle of four short parallel amphipathic helical peptides bearing the serine protease catalytic site residues serine, histidine, and aspartic acid at the amino end of the bundle in the same spatial arrangement as in chymotrypsin (ChTr). The necessary "oxyanion hole" and substrate binding pocket for acetyltyrosine ethyl ester, a classical ChTr substrate, were included in the design. The four chains were linked covalently at their carboxyl ends. The peptide has affinity for ChTr ester substrates similar to that of ChTr and hydrolyzes them at rates approximately 0.01 that of ChTr; total turnovers greater than 100 have been observed. The peptide is inhibited by ChTr specific inhibitors and is inactive toward benzoyl arginine ethyl ester, a trypsin substrate. The peptide is inactivated by heating above 60 degrees C, but recovers full catalytic activity upon cooling and lyophilization from acetic acid.
