Snake venom glutaminyl cyclase

Toxicon

Volumn 48, Issue 3, 2006, Pages 278-286

  Pawlak, Joanna ^a   Manjunatha Kini, R ^a  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

Glutaminyl cyclase; Pyroglutamic acid; Snake venom; Three finger toxins

Indexed keywords

COMPLEMENTARY DNA; ENZYME; GLUTAMINYL CYCLASE; SNAKE VENOM; TOXIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; BRAIN; CONTROLLED STUDY; DNA SEQUENCE; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYLOGENY; PRIORITY JOURNAL; PROTEIN EXPRESSION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RNA ISOLATION;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; COLUBRIDAE; DNA PRIMERS; DNA, COMPLEMENTARY; GUANYLATE CYCLASE; MOLECULAR SEQUENCE DATA; PROTEIN PROCESSING, POST-TRANSLATIONAL; SEQUENCE HOMOLOGY, AMINO ACID; SEQUENCE HOMOLOGY, NUCLEIC ACID; SNAKE VENOMS;

BOIGA; BOIGA DENDROPHILA; BOIGA IRREGULARIS; COLUBRIDAE; SERPENTES;

EID: 33747021920     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2006.05.013     Document Type: Article

References (35)

1. Aird S.D., Yates III J.R., Martino P.A., Shabanowitz J., Hunt D.F., and Kaiser I.I. The amino acid sequence of the acidic subunit B-chain of crotoxin. Biochim. Biophys. Acta 1040 (1990) 217-224
2. Bieber A.L., Becker R.R., McParland R., Hunt D.F., Shabanowitz J., Yates III J.R., Martino P.A., and Johnson G.R. The complete sequence of the acidic subunit from Mojave toxin determined by Edman degradation and mass spectrometry. Biochim. Biophys. Acta 1037 (1990) 413-421
3. Blobel G., and Dobberstein B. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol. 67 (1975) 835-851
4. Busby Jr. W.H., Quackenbush G.E., Humm J., Youngblood W.W., and Kizer J.S. An enzyme(s) that converts glutaminyl-peptides into pyroglutamyl-peptides. Presence in pituitary, brain, adrenal medulla, and lymphocytes. J. Biol. Chem. 262 (1987) 8532-8536
5. Chi C.W., Wang S.Z., Xu L.G., Wang M.Y., Lo S.S., and Huang W.D. Structure-function studies on the bradykinin potentiating peptide from Chinese snake venom (Agkistrodon halys Pallas). Peptides 6 Suppl 3 (1985) 339-342
6. Deshimaru M., Ogawa T., Nakashima K., Nobuhisa I., Chijiwa T., Shimohigashi Y., Fukumaki Y., Niwa M., Yamashina I., Hattori S., and Ohno M. Accelerated evolution of crotalinae snake venom gland serine proteases. FEBS Lett. 397 (1996) 83-88
7. Fischer W.H., and Spiess J. Identification of a mammalian glutaminyl cyclase converting glutaminyl into pyroglutamyl peptides. Proc. Natl. Acad. Sci. USA 84 (1987) 3628-3632
8. Fry B.G. From genome to "venome": molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins. Genome Res. 15 (2005) 403-420
9. Fry B.G., Lumsden N.G., Wuster W., Wickramaratna J.C., Hodgson W.C., and Kini R.M. Isolation of a neurotoxin (alpha-colubritoxin) from a nonvenomous colubrid: evidence for early origin of venom in snakes. J. Mol. Evol. 57 (2003) 446-452
10. Fry B.G., Wuster W., Ryan Ramjan S.F., Jackson T., Martelli P., and Kini R.M. Analysis of Colubroidea snake venoms by liquid chromatography with mass spectrometry: evolutionary and toxinological implications. Rapid Commun. Mass Spectrom. 17 (2003) 2047-2062
11. Hinke S.A., Pospisilik J.A., Demuth H.U., Mannhart S., Kuhn-Wache K., Hoffmann T., Nishimura E., Pederson R.A., and McIntosh C.H. Dipeptidyl peptidase IV (DPIV/CD26) degradation of glucagon. Characterization of glucagon degradation products and DPIV-resistant analogs. J. Biol. Chem. 275 (2000) 3827-3834
12. Huang K.F., Liu Y.L., Cheng W.J., Ko T.P., and Wang A.H. Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation. Proc. Natl. Acad. Sci. USA 102 (2005) 13117-13122
13. Junqueira-de-Azevedo I.L., Ching A.T., Carvalho E., Faria F., Nishiyama Jr. M.Y., Ho P.L., and Diniz M.R. Lachesis muta (Viperidae) cDNAs reveal diverging pitviper molecules and scaffolds typical of cobra (Elapidae) venoms: implications in snake toxin repertoire evolution. Genetics 173 (2006) 877-889
14. Kini R.M. Molecular moulds with multiple missions: functional sites in three-finger toxins. Clin. Exp. Pharmacol. Physiol 29 (2002) 815-822
15. 2 enzymes. J. Mol. Evol. 48 (1999) 125-132
16. Liao Y.D., Wang S.C., Leu Y.J., Wang C.F., Chang S.T., Hong Y.T., Pan Y.R., and Chen C. The structural integrity exerted by N-terminal pyroglutamate is crucial for the cytotoxicity of frog ribonuclease from Rana pipiens. Nucleic Acids Res. 31 (2003) 5247-5255
17. Mackessy S.P. Biochemistry and pharmacology of colubrid snake venoms. J. Toxicol.-Toxin Rev. 21 (2002) 43-83
18. Mackessy S.P., Sixberry N.M., Heyborne W.H., and Fritts T. Venom of the Brown Treesnake, Boiga irregularis: ontogenetic shifts and taxa-specific toxicity. Toxicon 47 (2006) 537-548
19. Mebs D. Enzymes in snake venoms: an overview. In: Bailey T.D. (Ed). Enzymes from Snake Venom (1998), Alaken Inc., Fort Collins, CO 1-10
20. Mebs D., and Claus I. Amino acid sequences and toxicities of snake venom components. In: Harvey A.L. (Ed). Snake Toxins (1991), Pergamon Press Inc, NY 425-447
21. 2 isozyme genes. Proc. Natl. Acad. Sci. USA 92 (1995) 5605-5609
22. 2 isozyme-encoding genes. Gene 172 (1996) 267-272
23. Oberg K.A., Ruysschaert J.M., Azarkan M., Smolders N., Zerhouni S., Wintjens R., Amrani A., and Looze Y. Papaya glutamine cyclase, a plant enzyme highly resistant to proteolysis, adopts an all-beta conformation. Eur. J. Biochem. 258 (1998) 214-222
24. Ohno M., Menez R., Ogawa T., Danse J.M., Shimohigashi Y., Fromen C., Ducancel F., Zinn-Justin S., Le Du M.H., Boulain J.C., Tamiya T., and Menez A. Molecular evolution of snake toxins: is the functional diversity of snake toxins associated with a mechanism of accelerated evolution?. Prog. Nucleic Acid Res. Mol. Biol. 59 (1998) 307-364
25. Pohl T., Zimmer M., Mugele K., and Spiess J. Primary structure and functional expression of a glutaminyl cyclase. Proc. Natl. Acad. Sci USA 88 (1991) 10059-10063
26. Reza A., Swarup S., and Kini R.M. Two parallel prothrombin activator systems in Australian rough-scaled snake, Tropidechis carinatus. Structural comparison of venom prothrombin activator with blood coagulation factor X. Thromb. Haemost. 93 (2005) 40-47
27. Rudd P.M., Joao H.C., Coghill E., Fiten P., Saunders M.R., Opdenakker G., and Dwek R.A. Glycoforms modify the dynamic stability and functional activity of an enzyme. Biochemistry 33 (1994) 17-22
28. Schilling S., Hoffmann T., Rosche F., Manhart S., Wasternack C., and Demuth H.U. Heterologous expression and characterization of human glutaminyl cyclase: evidence for a disulfide bond with importance for catalytic activity. Biochemistry 41 (2002) 10849-10857
29. Song I., Chuang C.Z., and Bateman Jr. R.C. Molecular cloning, sequence analysis and expression of human pituitary glutaminyl cyclase. J. Mol. Endocrinol. 13 (1994) 77-86
30. Sykes P.A., Watson S.J., Temple J.S., and Bateman Jr. R.C. Evidence for tissue-specific forms of glutaminyl cyclase. FEBS Lett. 455 (1999) 159-161
31. Takeya H., Arakawa M., Miyata T., Iwanaga S., and Omori-Satoh T. Primary structure of H2-proteinase, a non-hemorrhagic metalloproteinase, isolated from the venom of the habu snake, Trimeresurus flavoviridis. J. Biochem. (Tokyo) 106 (1989) 151-157
32. Tsetlin V. Snake venom alpha-neurotoxins and other 'three-finger' proteins. Eur. J. Biochem. 264 (1999) 281-286
33. Van Coillie E., Proost P., Van I A., Struyf S., Polfliet M., De I M., Harvey D.J., Van Damme J., and Opdenakker G. Functional comparison of two human monocyte chemotactic protein-2 isoforms, role of the amino-terminal pyroglutamic acid and processing by CD26/dipeptidyl peptidase IV. Biochemistry 37 (1998) 12672-12680
34. Von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14 (1986) 4683-4690
35. Wang C., Eufemi M., Turano C., and Giartosio A. Influence of the carbohydrate moiety on the stability of glycoproteins. Biochemistry 35 (1996) 7299-7307