[Basic (cleaving arginine and lysine residues) metallocarboxypeptidase of mammalian tissue: structure, properties and function].
The structure, physical, chemical and catalitical properties, functions and biological role of mammalian basic carboxypeptidases are observing. On the strength of the genetic and filogenic research data it is supposed the existence of a family of basic metal-dependent carboxypeptidases and the plan of it evolution is proposed. The connections between structure, localisation and function of this enzyme are discussed.
Vernigora
A N
AN
Department of Chemistry, Penza State Pedagogical University, Russia.
Gengin
M T
MT
D001120:Arginine / Q000737:chemistry*; D043424:Carboxypeptidase B; D025901:Carboxypeptidase B2; D043423:Carboxypeptidase H; D002268:Carboxypeptidases / Q000737:chemistry; D006801:Humans; D008239:Lysine / Q000737:chemistry*; D001121:Lysine Carboxypeptidase / Q000737:chemistry* / Q000502:physiology; D013329:Structure-Activity Relationship
D001120:Arginine; D002268:Carboxypeptidases; D043423:Carboxypeptidase H; D043424:Carboxypeptidase B; D025901:Carboxypeptidase B2; D001121:Lysine Carboxypeptidase; D008239:Lysine
Osnovnye (otshchepliaiushchie ostatki arginina i lizina) metallokarboksipeptidazy tkaneĭ mlekopitaiushchikh: struktura, svoĭstva i funktsii.