Primary Structure of a Coagulant Enzyme, Bilineobin, from Agkistrodon bilineatus Venom

Nikai, Toshiaki; Ohara, A.; Komori, Yumiko; Fox, James W.; Sugihara, Hisayoshi

doi:10.1006/abbi.1995.1208

Cited by 50 publications

(29 citation statements)

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“…The absence of free thiols in SVTLEs led to the assumption that all 12 cysteines are linked in disulfide bonds. These pairings were confirmed experimentally on bilineobin from Agkistrodon bilineatus and contortrixobin from A. contortrix contortrix [12,50]. Therefore, SVTLE disulfide bridges are predicted to be the pairs of cysteine residues 22-157, 42-58, 91-250, 136-201, 168 -182 and 191 -220 and as found in the crystallographic structure of TSV-PA -the only crystal structure of a venom serine protease currently available [51].…”

Section: Common Features Of Svtlessupporting

confidence: 58%

Snake venom thrombin-like enzymes: from reptilase to now

Castro

Zingali

Albuquerque

et al. 2004

Cellular and Molecular Life Sciences (CMLS)

172

123

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The snake venom thrombin-like enzymes (SVTLEs) comprise a number of serine proteases functionally and structurally related to thrombin. Until recently, only nine complete sequences of this subgroup of the serine protease family were known. Over the past 5 years, the primary structure of several SVTLEs has been characterized, and now this family includes several members. Of particular interest is their possible use in pathologies such as thrombosis. The aim of the present review is to summarize the state of the art concerning the evolutionary, structural and biological features of the SVTLEs.

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Section: Common Features Of Svtlessupporting

confidence: 58%

Snake venom thrombin-like enzymes: from reptilase to now

Castro

Zingali

Albuquerque

et al. 2004

Cellular and Molecular Life Sciences (CMLS)

172

123

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“…The molecular mass of AH143 is similar to other thrombin-like enzymes already studied (6,13). In addition, molecular mass and enzymatic activities -including plasma clotting, amidolytic activity and not inhibition by heparin -characterize AH143 Since AH143 is not inhibited by heparin, it can be used in quantitative determination of fibrinogen as well as in plasma of patients under heparin treatment and in the laboratory for routine assays of coagulation factors (4).…”

Section: Discussionmentioning

confidence: 70%

“…Analyses of AH143 activity in various conditions of temperature and pH were carried out in accordance with Nikai et al (13). The temperature under which the purification was performed was based on the observation that the enzyme solution was stable at 4°C (4, 7).…”

Section: Discussionmentioning

confidence: 99%

Purification and partial characterization of a coagulant serine protease from the venom of the Iranian snake Agkistrodon halys

Ghorbanpur

Mirakabadi

Zokaee

et al. 2009

J. Venom. Anim. Toxins incl. Trop. Dis

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ABSTRACT:Agkistrodon halys is one of several dangerous snake species in Iran. Among the most important signs and symptoms in patients envenomated by this snake is disseminated intravascular coagulation. A thrombin-like enzyme, called AH143, was isolated from Agkistrodon halys venom by gel filtration on a Sephadex G-50 column, ion-exchange chromatography on a DEAE-Sepharose and high performance liquid chromatography (HPLC) on a C18 column. In the final stage of purification, 0.82 mg of purified enzyme was obtained from 182.5 mg of venom. The purified enzyme showed a single protein band by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), under reducing conditions, and its molecular mass was found to be about 30 kDa. AH143 revealed clotting activity in human plasma, which was not inhibited by EDTA or heparin. This enzyme still demonstrated coagulation activity when exposed to variations in temperature and pH ranging, respectively, from 30 to 40°C and from 7.0 to 8.0. It also displayed proteolytic activities on synthetic substrate. The purified enzyme did not show any effect on casein. We concluded that the venom of the Iranian snake Agkistrodon halys contains about 0.45% single procoagulant protein which appears to be a thrombin-like enzyme.

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“…Like physiological tissue type plasminogen activator (t-PA), TSV-PA specifically cleaves the Arg 561 -Val 562 plasminogen bond to generate two-chain plasmin, a key enzyme in fibrinolysis (2,3). Sequence homology with trypsin and other venom serine proteinases (4) indicates that TSV-PA belongs to the family of serine proteinases (5). Trypsin-like serine proteinases, which cleave the peptide bond following arginine or lysine, display very different substrate and inhibitor specificities.…”

Section: 10246 -10255)mentioning

confidence: 99%

Trimeresurus stejnegeri Snake Venom Plasminogen Activator

Zhang¹,

Wisner²,

Maroun³

et al. 1997

Journal of Biological Chemistry

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The specific plasminogen activator from Trimeresurus stejnegeri venom (TSV-PA) is a serine proteinase presenting 23% sequence identity with the proteinase domain of tissue type plasminogen activator, and 63% with batroxobin, a fibrinogen clotting enzyme from Bothrops atrox venom that does not activate plasminogen. TSV-PA contains six disulfide bonds and has been successfully overexpressed in Escherichia coli (Zhang, Y., Wisner, A., Xiong, Y. L., and Bon, C. (1995) J. Biol. Chem. 270, 10246 -10255).To identify the functional domains of TSV-PA, we focused on three short peptide fragments of TSV-PA showing important sequence differences with batroxobin and other venom serine proteinases. Molecular modeling shows that these sequences are located in surface loop regions, one of which is next to the catalytic site. When these sequences were replaced in TSV-PA by the equivalent batroxobin residues none generated either fibrinogen-clotting or direct fibrinogenolytic activity. Two of the replacements had little effect in general and are not critical to the specificity of TSV-PA for plasminogen. Nevertheless, the third replacement, produced by the conversion of the sequence DDE 96a-98 to NVI, significantly increased the K m for some tripeptide chromogenic substrates and resulted in undetectable plasminogen activation, indicating the key role that the sequence plays in substrate recognition by the enzyme.The plasminogen activator from Trimeresurus stejnegeri venom (TSV-PA) 1 is a 234-residue single chain glycoprotein with an apparent molecular weight of 33 kDa (1). Like physiological tissue type plasminogen activator (t-PA), TSV-PA specifically cleaves the Arg 561 -Val 562 plasminogen bond to generate two-chain plasmin, a key enzyme in fibrinolysis (2, 3). Sequence homology with trypsin and other venom serine proteinases (4) indicates that TSV-PA belongs to the family of serine proteinases (5). Trypsin-like serine proteinases, which cleave the peptide bond following arginine or lysine, display very different substrate and inhibitor specificities. They were among the first enzymes to be studied extensively (6). In particular, the role of the "specificity pocket" in determining the "primary", or P1, 2 specificity of the enzyme has long been recognized (7). The existence and critical importance of other additional structural determinants of proteinase specificity have also been established (8), but both their location and their role remain unknown.The sequence of TSV-PA exhibits a high degree of identity (60 -66%) with other snake venom proteinases, such as Vipera russelli venom factor V activator (9), batroxobin from Bothrops atrox venom (10), and Agkistrodon contortrix venom protein C activator (11), which present considerable differences in their substrate specificities. For example, TSV-PA, which efficiently activates plasminogen, does not clot or degrade fibrinogen and does not activate or degrade factor X, prothrombin, and protein C (1). On the other hand, batroxobin, which shows a thrombinlike activity (12), does not a...

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Primary Structure of a Coagulant Enzyme, Bilineobin, from Agkistrodon bilineatus Venom

Cited by 50 publications

References 0 publications

Snake venom thrombin-like enzymes: from reptilase to now

Snake venom thrombin-like enzymes: from reptilase to now

Purification and partial characterization of a coagulant serine protease from the venom of the Iranian snake Agkistrodon halys

Trimeresurus stejnegeri Snake Venom Plasminogen Activator

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