Enzymatic properties of thiol-dependent serine proteinase of Bacillus intermedius 3-19

dc.contributor.author	Itskovich E.
dc.contributor.author	Balaban N.
dc.contributor.author	Mardanova A.
dc.contributor.author	Shakirov E.
dc.contributor.author	Sharipova M.
dc.contributor.author	Leshchinskaya I.
dc.contributor.author	Ksenofontov A.
dc.contributor.author	Rudenskaya G.
dc.date.accessioned	2018-09-17T20:08:37Z
dc.date.available	2018-09-17T20:08:37Z
dc.date.issued	1997
dc.identifier.issn	0006-2979
dc.identifier.uri	https://dspace.kpfu.ru/xmlui/handle/net/133092
dc.description.abstract	Effects of a thiol-dependent serine proteinase of Bacillus intermedius on peptide substrates and insulin B-chain were studied. The enzyme preferably splits peptide bonds formed by carboxyl groups of hydrophobic amino acids. Ca2+ increases the thermal stability of the proteinase significantly. The kinetic characteristics of hydrolysis of Z-Ala-Ala-Leu-pNA by this enzyme was determined as Km = 1.25 mM and kcat = 0.15 sec-1. The enzyme has high stability to DMFA and isopropanol, and is able to catalyze peptide bond synthesis.
dc.relation.ispartofseries	Biochemistry (Moscow)
dc.subject	Enzymatic synthesis of substrates
dc.subject	Substrate specificity
dc.subject	Thiol-dependent serine proteinase
dc.title	Enzymatic properties of thiol-dependent serine proteinase of Bacillus intermedius 3-19
dc.type	Article
dc.relation.ispartofseries-issue	1
dc.relation.ispartofseries-volume	62
dc.collection	Публикации сотрудников КФУ
dc.relation.startpage	49
dc.source.id	SCOPUS00062979-1997-62-1-SID0030642217

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