Roles of lysine-69 in dimerization and activity of trimeresurus flavoviridis venom aspartate-49-phospholipase A2

Journal of Molecular Recognition

Volumn 9, Issue 1, 1996, Pages 23-30

  Nakamura, Shinji ^a   Nakai, Makoto ^a   Nakashima, Kin Ichi ^a   Ogawa, Tomohisa ^a   Shimohigashi, Yasuyuki ^a   Ohno, Motonori ^a   Kihara, Hiroshi ^b   Yamane, Takashi ^c   Ashida, Tamaichi ^c  

^a KYUSHU UNIVERSITY   (Japan)

^b TAKARA SHUZO CO LTD   (Japan)

^c NAGOYA UNIVERSITY   (Japan)

Author keywords

2,4,6 trinitrobenzenesulfonate; Aspartate 49 phospholipase A2; Conformational displacement; Lysine residues; Subunit interaction

Indexed keywords

ASPARTIC ACID; CALCIUM; ENZYME INHIBITOR; LYSINE; PHOSPHOLIPASE A; SNAKE VENOM; TRIMERESURUS VENOMS; TRINITROBENZENESULFONIC ACID;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; ENZYMOLOGY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; KINETICS; METABOLISM; MOLECULAR GENETICS; MOLECULAR WEIGHT; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SNAKE;

AMINO ACID SEQUENCE; ANIMALS; ASPARTIC ACID; CALCIUM; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CROTALID VENOMS; DIMERIZATION; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME INHIBITORS; KINETICS; LYSINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PHOSPHOLIPASES A; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; TRIMERESURUS; TRINITROBENZENESULFONIC ACID;

EID: 0029693985     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1352(199601)9:1<23::AID-JMR235>3.0.CO;2-P     Document Type: Article

References (36)

1. 2 at 2.5 Å. Access to a shielded catalytic center. J. Biol. Chem. 260, 9742-9749.
2. 2 neurotoxins, agkistrodotoxin and crotoxin. Toxicon 29, 441-451.
3. Crestfield, A. M., Moore, S. and Stein, W. H. (1963). The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J. Biol. Chem. 238, 622-627.
4. 2 from snake venom to human secreted forms. J. Mol. Evol. 31, 228-238.
5. 2. J. Mol. Biol. 124, 53-60.
6. 2 at 1.7 Å resolution. J. Mol. Biol. 147, 97-123.
7. 2. J. Mol. Biol. 168, 163-179.
8. 2. Secondary-structure prediction, circular dichroism and relative interface hydrophobicity. Eur. J. Biochem. 137, 537-544.
9. Edman, P. (1970). In Protein Sequence Determination: Sequence Determination, ed. by S. B. Needleman, pp. 211-255, Springer-Verlag, Berlin.
10. Fields, R. (1972). The rapid determination of amino groups with TNBS. Methods Enzymol. 25, 464-468.
11. 2+-binding ligand. Eur. J. Biochem. 113, 283-288.
12. 2. Arch. Biochem. Biophys. 284, 352-359.
13. 2 isozyme from Trimeresurus gramineus (green habu snake) venom. Toxicon 30, 1331-1341.
14. 2 variant in Heloderma suspectum (Gila monster) venom. Eur. J. Biochem. 186, 23-33.
15. 2 based upon structural determinants. J. Biol. Chem. 252, 4913-4921.
16. Ishimaru, K., Kihara, H. and Ohno, M. (1980). Purification and properties of phospholipase A from venom of Trimeresurus flavoviridis (habu snake). J. Biochem. (Tokyo) 88, 443-451.
17. 2 on phospholipid analogues. A reevaluation of the minimal substrate requirements. Biochemistry 29, 6094-6102.
18. Levy, H. M., Leber, P. D. and Ryan, E. M., (1963). Inactivation of myosin by 2,4-dinitrophenol and protection by adenostne triphosphate and other phosphate compounds. J. Biol. Chem. 238, 3654-3659.
19. 2 from Bungarus fasciatus (banded krait) venom. Toxicon 28, 1457-1468.
20. 2 with low activity, from Trimeresurus flavoviridis venom. J. Biochem. (Toyko) 107, 400-408.
21. 2. J. Biol. Chem. 261, 4797-4804.
22. 2. J. Biochem. (Tokyo) 100, 883-893.
23. 2 from the venom of Trimeresurus gramineus (green habu snake). Toxicon 29, 157-166.
24. 2, and consequent revision of the amino acid sequence. J. Biochem. (Tokyo) 108, 816-821.
25. 2 and its fragment with calcium ion. J. Biochem. (Tokyo) 96, 1183-1191.
26. 2 from bovine pancreas and Crotalus atrox venom. J. Biol. Chem. 260, 11627-11634.
27. 2 upon active site ligand binding. J. Mol. Recogn. 1, 124-129.
28. 2 from the venom of Agkistrodon piscivorus piscivorus. J. Biol. Chem. 267, 22645-22657.
29. 2. Monomer-dimer equilibrium. J. Am. Chem. Soc. 97, 1205-1208.
30. 2 from the venom of australien king brown snake, Pseudechis australis. Toxicon 28, 329-339.
31. 2 via substrate level acylation of lysine 56. J. Biol. Chem. 264, 10041-10047.
32. 2. Role of histidine and calcium ion in the catalytic mechanism. Biochemistry 19, 743-750.
33. 2 at 2.2 A resolution. Nature 352, 79-82.
34. 2 in a complex with a transition-state analogue. Science 250, 1560-1563.
35. 2. J. Biochem. (Tokyo) 103, 156-161.
36. 2 with low activity, from the venom of Trimeresurus flavoviridis (habu snake). Toxicon 28, 43-54.