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Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases.

Zhu Z, Liang Z, Zhang T, Zhu Z, Xu W, Teng M, Niu L
J Biol Chem 280 10524-9 (2005)
Cited: 27 times
EuropePMC logo PMID: 15632114

Abstract

We deduced that Agkistrodon actus venom serine proteinases I and II, previously isolated from the venom of A. acutus (Zhu, Z., Gong, P., Teng, M., and Niu, L. (2003) Acta Crystallogr. Sect. D Biol. Crystallogr. 59, 547-550), are encoded by two almost identical genes, with only the single substitution Asp for Asn at residue 62. Amidolytic assays indicated that they possess slightly different enzymatic properties. Crystal structures of A. actus venom serine proteinases I and II were determined at resolution of 2.0 and 2.1 A with the identification of trisaccharide (NAG(301)-FUC(302)-NAG(303)) and monosaccharide (NAG(301)) residues in them, respectively. The substrate binding sites S3 of the two proteinases appear much shallower than that of Trimeresurus stejnegeri venom plasminogen activator despite the overall structural similarity. Based on structural analysis, we showed that these Asn(35)-linked oligosaccharides collide spatially with some inhibitors, such as soybean trypsin inhibitor, and would therefore hinder their inhibitory binding. Difference of the carbohydrates in both the proteinases might also lead to their altered catalytic activities.

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  1. Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis. Kang TS, Georgieva D, Genov N, Murakami MT, Sinha M, Kumar RP, Kaur P, Kumar S, Dey S, Sharma S, Vrielink A, Betzel C, Takeda S, Arni RK, Singh TP, Kini RM. FEBS J. 278 4544-4576 (2011)

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  4. BJ-48, a novel thrombin-like enzyme from the Bothrops jararacussu venom with high selectivity for Arg over Lys in P1: Role of N-glycosylation in thermostability and active site accessibility. Silva-Junior FP, Guedes HL, Garvey LC, Aguiar AS, Bourguignon SC, Di Cera E, Giovanni-De-Simone S. Toxicon 50 18-31 (2007)
  5. Glycosylated trypsin-like proteases from earthworm Eisenia fetida. Wu JX, Zhao XY, Pan R, He RQ. Int. J. Biol. Macromol. 40 399-406 (2007)
  6. Molecular characterization of BjussuSP-I, a new thrombin-like enzyme with procoagulant and kallikrein-like activity isolated from Bothrops jararacussu snake venom. Sant'Ana CD, Bernardes CP, Izidoro LF, Mazzi MV, Soares SG, Fuly AL, Zingali RB, Magro AJ, Braz AS, Fontes MR, Stábeli RG, Sampaio SV, Soares AM. Biochimie 90 500-507 (2008)
  7. Molecular cloning of novel serine proteases and phospholipases A2 from green pit viper (Trimeresurus albolabris) venom gland cDNA library. Rojnuckarin P, Muanpasitporn C, Chanhome L, Arpijuntarangkoon J, Intragumtornchai T. Toxicon 47 279-287 (2006)
  8. Purification and functional characterisation of rhinocerase, a novel serine protease from the venom of Bitis gabonica rhinoceros. Vaiyapuri S, Harrison RA, Bicknell AB, Gibbins JM, Hutchinson G. PLoS ONE 5 e9687 (2010)
  9. Bothrops protease A, a unique highly glycosylated serine proteinase, is a potent, specific fibrinogenolytic agent. Paes Leme AF, Prezoto BC, Yamashiro ET, Bertholim L, Tashima AK, Klitzke CF, Camargo AC, Serrano SM. J. Thromb. Haemost. 6 1363-1372 (2008)
  10. Cloning of serine protease cDNAs from Crotalus durissus terrificus venom gland and expression of a functional Gyroxin homologue in COS-7 cells. Yonamine CM, Prieto-da-Silva AR, Magalhães GS, Rádis-Baptista G, Morganti L, Ambiel FC, Chura-Chambi RM, Yamane T, Camillo MA. Toxicon 54 110-120 (2009)
  11. Purification, characterization and gene cloning of Da-36, a novel serine protease from Deinagkistrodon acutus venom. Zheng Y, Ye FP, Wang J, Liao GY, Zhang Y, Fan QS, Lee WH. Toxicon 67 1-11 (2013)
  12. Structural models of the snake venom factor V activators from Daboia russelli and Daboia lebetina. Segers K, Rosing J, Nicolaes GA. Proteins 64 968-984 (2006)
  13. Crystal structure and activating effect on RyRs of AhV_TL-I, a glycosylated thrombin-like enzyme from Agkistrodon halys snake venom. Zeng F, Shen B, Zhu Z, Zhang P, Ji Y, Niu L, Li X, Teng M. Arch. Toxicol. 87 535-545 (2013)
  14. N-glycome profiling of Bothrops jararaca newborn and adult venoms. Zelanis A, Serrano SM, Reinhold VN. J Proteomics 75 774-782 (2012)
  15. Molecular cloning of serine proteases from elapid snake venoms. Jin Y, Lee WH, Zhang Y. Toxicon 49 1200-1207 (2007)
  16. Shedaoenase, a novel fibrinogenase from the venom of Agkistrodon shedaoenthesis Zhao. Jiao HM, Yang LX, Lu B, Wu YQ, Zhou YC. Acta Biochim. Biophys. Sin. (Shanghai) 37 835-842 (2005)
  17. Correlation between the glycan variations and defibrinogenating activities of acutobin and its recombinant glycoforms. Wang YM, Tsai IH, Chen JM, Cheng AC, Khoo KH. PLoS ONE 9 e100354 (2014)
  18. Expression of a new serine protease from Crotalus durissus collilineatus venom in Pichia pastoris and functional comparison with the native enzyme. Boldrini-França J, Santos Rodrigues R, Santos-Silva LK, de Souza DL, Gomes MS, Cologna CT, de Pauw E, Quinton L, Henrique-Silva F, de Melo Rodrigues V, Arantes EC. Appl. Microbiol. Biotechnol. 99 9971-9986 (2015)
  19. High-level expression, purification, and enzymatic characterization of truncated human plasminogen (Lys531-Asn791) in the methylotrophic yeast Pichia pastoris. Liu R, Zhao B, Zhang Y, Gu J, Yu M, Song H, Yu M, Mo W. BMC Biotechnol. 15 50 (2015)
  20. Serine protease isoforms in Gloydius intermedius venom: Full sequences, molecular phylogeny and evolutionary implications. Yang ZM, Yu H, Liu ZZ, Pei JZ, Yang YE, Yan SX, Zhang C, Zhao WL, Wang ZZ, Wang YM, Tsai IH. J Proteomics 164 19-32 (2017)
  21. Cloning of cDNAs and molecular characterisation of C-type lectin-like proteins from snake venoms. Feng J, Chen T, Zhou M, Shaw C. Toxicon 60 1363-1369 (2012)
  22. Cloning, expression, purification and bioactivity evaluation of a thrombin-like enzyme from Deinagkistrodon acutus venom gland library. Li A, Zhang C, Wang J, Wang J, Jiang H, Li J, Ma X, Zhang W, Lu Y. Biotechnol. Lett. 40 93-102 (2018)
  23. Isolation and characterisation of a kallikrein-like enzyme from Agkistrodon halys pallas snake venom. Zhang Y, Xu W, Ma B, Huang K, Song M, Zhang N, Zhang Y, Wang Y, Dai Y, Luo Y. J. Sci. Food Agric. 92 1497-1503 (2012)
  24. Comprehensive Study of the Proteome and Transcriptome of the Venom of the Most Venomous European Viper: Discovery of a New Subclass of Ancestral Snake Venom Metalloproteinase Precursor-Derived Proteins. Leonardi A, Sajevic T, Pungerčar J, Križaj I. J. Proteome Res. 18 2287-2309 (2019)
  25. Limited proteolysis of fibrinogen by fibrinogenase from Echis multisquamatis venom. Chernyshenko VO. Protein J. 34 130-134 (2015)


Related citations provided by authors (1)

  1. Purification, N-terminal sequencing, partial characterization, crystallization and preliminary crystallographic analysis of two glycosylated serine proteinases from Agkistrodon acutus venom.. Zhu Z, Gong P, Teng M, Niu L Acta Crystallogr D Biol Crystallogr 59 547-50 (2003)

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