منابع مشابه
Synthetic human prion protein octapeptide repeat binds to the proteinase K active site.
Proteinase K is widely used in tests for the presence of infectious prion protein causing fatal spongiform encephalopathies. To investigate possible interactions between the enzyme and the functionally important N-terminal prion domain, we crystallized mercury-inhibited proteinase K in the presence of the synthetic peptides GGGWGQPH and HGGGW. The octapeptide sequence is identical to that of a ...
متن کاملCharacterization of the active site of human multicatalytic proteinase.
The activity of multicatalytic proteinase against synthetic substrates and the kinetics of its inhibition by a range of class-specific inhibitors have been investigated. The enzyme was found to have a broader pH activity profile than previously noted, being active against succinyl-Ala-Ala-Phe-7-amino-4-methylcoumarin optimally at pH 4.5 and against benzyloxycarbonyl-Gly-Gly-Arg-7-amino-4-methyl...
متن کاملA herpesvirus maturational proteinase, assemblin: identification of its gene, putative active site domain, and cleavage site.
A herpesvirus proteinase activity has been identified and partially characterized by using the cloned enzyme and substrate genes in transient transfection assays. Evidence is presented that the proteinase gene of cytomegalovirus strain Colburn encodes a 590-amino acid protein whose N-terminal 249 residues contain the proteolytic activity and two domains that are highly conserved in the homologo...
متن کاملActive Site-directed Inhibition by Optically Pure Epoxyalkyl Cellobiosides Reveals Differences in Active Site Geometry
1,31,4-@-~-Glucan 4-glucanohydrolases (EC 3.2.1.73) from Bacillus subtilis and barley (Hordeum vulgare) with identical substrate specificities but unrelated primary structures have been probed with (R,S)epoxyalkyl (-propyl, -butyl, -pentyl) 8-cellobiosides and with optically pure (3s)and (3R)-3,4-cellobiosides as active site-directed inhibitors. The optimal aglycon length for inactivation diff...
متن کاملActive site geometry of glucose-1-phosphate uridylyltransferase.
Glucose-1-phosphate uridylyltransferase, or UGPase, catalyzes the production of UDP-glucose from glucose-1-phosphate and UTP. Because of the biological role of UDP-glucose in glycogen synthesis and in the formation of glycolipids, glycoproteins, and proteoglycans, the enzyme is widespread in nature. Recently this laboratory reported the three-dimensional structure of UGPase from Escherichia col...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1986
ISSN: 0014-5793
DOI: 10.1016/0014-5793(86)80307-6