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http://purl.uniprot.org/citations/8373353http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8373353http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8373353http://www.w3.org/2000/01/rdf-schema#comment"The 1.54 kb cDNA for ancrod, a thrombin-like enzyme, was cloned from a lambda ZAP cDNA library derived from the venom glands of Calloselasma (Agkistrodon) rhodostoma. The cDNA sequence reveals that ancrod is synthesized as a pre-zymogen of 258 amino acids, including a putative secretory peptide of 18 amino acids and a proposed zymogen peptide of 6 amino-acid residues. The amino-acid sequence of the predicted active form of the enzyme exhibits a high degree of sequence similarity to those of mammalian serine proteases (trypsin and pancreatic kallikrein) and other thrombin-like enzymes (batroxobin and flavoxobin). Key amino-acid residues (His43, Asp88, Ser182 and Asp176) that are thought to be involved in the substrate cleavage and in the substrate-binding reaction are conserved. Ancrod contains 13 cysteine residues. Based on alignment with the amino-acid sequences of trypsin and batroxobin, six disulphide bridges can be predicted to be present in the ancrod protein. The existence of a free cysteine, which changes the common sequence surrounding the Ser182 active site from Gly-Asp-Ser-Gly-Gly-Pro to Cys-Asp-Ser-Gly-Gly-Pro, is unusual for a serine protease."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.org/dc/terms/identifier"doi:10.1042/bj2940387"xsd:string
http://purl.uniprot.org/citations/8373353http://purl.org/dc/terms/identifier"doi:10.1042/bj2940387"xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/author"Shih C.-M."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/author"Shih C.-M."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/author"Au L.-C."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/author"Au L.-C."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/author"Teh G.-W."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/author"Teh G.-W."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/author"Chang K.-J."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/author"Chang K.-J."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/author"Chou J.-S."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/author"Chou J.-S."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/author"Lin S.-B."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/author"Lin S.-B."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/pages"387-390"xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/pages"387-390"xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/title"Molecular cloning and sequence analysis of the cDNA for ancrod, a thrombin-like enzyme from the venom of Calloselasma rhodostoma."xsd:string
http://purl.uniprot.org/citations/8373353http://purl.uniprot.org/core/title"Molecular cloning and sequence analysis of the cDNA for ancrod, a thrombin-like enzyme from the venom of Calloselasma rhodostoma."xsd:string