[Proline specific peptidases and their specific inhibitors].
Several proline specific peptidases were newly isolated from mammalian organs, plants and microorganisms, and their enzymatic properties characterized. The genes of prolyl endopeptidase, aminopeptidase P and proline iminopeptidase from some microorganisms were cloned and their nucleotide sequences determined. By high expression of these genes in Escherichia coli, the enzymes became possible to be used for the industrial application as well as its basic research. Novel inhibitors specific for the prolyl endopeptidase and dipeptidyl aminopeptidase IV were synthesized and some inhibitors for prolyl endopeptidase found to show an anti-amnesic effect.
Yoshimoto
T
T
School of Pharmaceutical Sciences, Nagasaki University, Japan.
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000235:genetics / Q000302:isolation & purification; D000818:Animals; D001419:Bacteria / Q000201:enzymology; D001483:Base Sequence; D003001:Cloning, Molecular; D010450:Endopeptidases / Q000737:chemistry / Q000235:genetics*; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D008969:Molecular Sequence Data; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases; D013379:Substrate Specificity; D013844:Thiazoles; D053778:Thiazolidines
D013844:Thiazoles; D053778:Thiazolidines; C062563:Z-thioPro-thiazolidine; D010450:Endopeptidases; D000626:Aminopeptidases; C022450:prolyl aminopeptidase; C022750:X-Pro aminopeptidase; D012697:Serine Endopeptidases; C000705287:PREPL protein, human; D000085822:Prolyl Oligopeptidases