LYS-49 phospholipase A2 homologs from venoms of deinagkistrodon acutus and trimeresurus mucrosquamatus have identical protein sequence

Wang, Ying‐Ming; Wang, Jim-Hon; Pan, Fu-Ming; Tsai, Inn-Ho

doi:10.1016/0041-0101(95)00161-1

Cited by 17 publications

(8 citation statements)

References 24 publications

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“…The data-collection and reduction statistics are listed in Table 2. Sequence of the N-terminal amino-acid residues of acutohaemolysin aligned with the N-terminal sequences of Lys49-type PLA 2 s from other snake venoms: Lys49-type PLA 2 (Fan et al, 1999), ACLMT (Selistre de Araujo et al, 1996), AppK49 (Maraganore & Heinrikson, 1986), Basper II (Francis et al, 1991), TMK49 (Liu et al, 1991), TFBP I and II (Liu et al, 1990), TGRK49 (Nakashima et al, 1995 and D. acutus K49 (Wang et al, 1996). The bold characters represent the conserved residues among snakevenom PLA 2 s. ² R merge = i |hI(h)i À I(h) i |/ i I(h) i , where I(h) i is the intensity of the ith observation of re¯ection h and hI(h)i is the mean intensity of re¯ection h. ³ The completeness is the ratio of the number of the observed re¯ections to the number of possible re¯ections.…”

Section: Crystallization Papersmentioning

confidence: 96%

Characterization, crystallization and preliminary X-ray diffraction analysis of acutohaemolysin, a haemolytic toxin fromAgkistrodon acutusvenom

Huang

Zhu

et al. 2000

Acta Crystallogr D Biol Cryst

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Acutohaemolysin, a phospholipase A(2) (PLA(2)) from the venom of the snake Agkistrodon acutus, has been isolated and purified to homogeneity by anion-exchange chromatography on a DEAE-Sepharose column followed by cation-exchange chromatography on a CM-Sepharose column. It is an alkaline protein with an isoelectric point of 10.5 and is comprised of a single polypeptide chain of 13 938 Da. Its N-terminal amino-acid sequence shows very high similarity to Lys49-type PLA(2) proteins from other snake venoms. Although its PLA(2) enzymatic activity is very low, acutohaemolysin has a strong indirect haemolytic activity and anticoagulant activity. Acutohaemolysin crystals with a diffraction limit of 1.60 A were obtained by the hanging-drop vapour-diffusion method. The crystals belong to the space group C2, with unit-cell parameters a = 45.30, b = 59.55, c = 46.13 A, beta = 117.69 degrees. The asymmetric unit contains one molecule.

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Section: Crystallization Papersmentioning

confidence: 96%

Characterization, crystallization and preliminary X-ray diffraction analysis of acutohaemolysin, a haemolytic toxin fromAgkistrodon acutusvenom

Huang

Zhu

et al. 2000

Acta Crystallogr D Biol Cryst

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“…Residues identical to those in the top line is denoted with a dot; gaps are marked with hyphens. Abbreviations are: TMV, T. mucrosquamatus venom and DAV, D. acutus venom [29].…”

Section: Purification and Characterization Of Pla 2 Smentioning

confidence: 99%

Phospholipases A₂ from Callosellasma rhodostoma venom gland

Tsai

Wang

et al. 2000

European Journal of Biochemistry

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Callosellasma rhodostoma (Malayan pitviper) is a monotypic Asian pitviper of medical importance. Three acidic phospholipases A 2 (PLA 2 s) and one basic PLA 2 -homolog were purified from its venom while 10 cDNAs encoding distinct PLA 2 s were cloned from venom glands of a Thailand specimen of this species. Complete amino-acid sequences of the purified PLA 2 s were successfully deduced from their cDNA sequences. Among the six un-translated PLA 2 cDNAs, two apparently result from recombination of its Lys49-PLA 2 gene with its Asp49-PLA 2 genes. The acidic PLA 2 s inhibit platelet-aggregation, while the noncatalytic PLA 2 -homolog induces local edema. This basic PLA 2 -homolog contains both Asp49 and other, unusual substitutions unique for the venom Lys49-PLA 2 subtype (e.g. Leu5, Trp6, Asn28 and Arg34). Three-dimensional modelling of the basic protein revealed a heparin-binding region, and an abnormal calcium-binding pocket, which may explain its low catalytic activity. Oxidation of up to six of its Met residues or coinjection with heparin reduced its edemainducing activity but methylation of its active site His48 did not. The distinct Arg/Lys-rich and Met-rich region at positions 10±36 of the PLA 2 homolog presumably are involved in its heparin-binding and the cell membraneinterference leading to edema and myotoxicity.

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“…The sequence data for CRV-H1E6, CRV-S1E6a, and CRV-S1E6b have been deposited in the GenBank database with the accession numbers AF104067, AF104068, and AF104069, respectively. Refer to (35,36) for other sequences. Single-letter codes of amino acids are used.…”

Section: Figmentioning

confidence: 99%

Differential Expression and Geographic Variation of the Venom Phospholipases A2 of Calloselasma rhodostoma and Trimeresurus mucrosquamatus

Tsai

Chen

Wang

et al. 2001

Archives of Biochemistry and Biophysics

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LYS-49 phospholipase A2 homologs from venoms of deinagkistrodon acutus and trimeresurus mucrosquamatus have identical protein sequence

Cited by 17 publications

References 24 publications

Characterization, crystallization and preliminary X-ray diffraction analysis of acutohaemolysin, a haemolytic toxin fromAgkistrodon acutusvenom

Characterization, crystallization and preliminary X-ray diffraction analysis of acutohaemolysin, a haemolytic toxin fromAgkistrodon acutusvenom

Phospholipases A₂ from Callosellasma rhodostoma venom gland

Differential Expression and Geographic Variation of the Venom Phospholipases A2 of Calloselasma rhodostoma and Trimeresurus mucrosquamatus

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LYS-49 phospholipase A2 homologs from venoms of deinagkistrodon acutus and trimeresurus mucrosquamatus have identical protein sequence

Cited by 17 publications

References 24 publications

Characterization, crystallization and preliminary X-ray diffraction analysis of acutohaemolysin, a haemolytic toxin fromAgkistrodon acutusvenom

Characterization, crystallization and preliminary X-ray diffraction analysis of acutohaemolysin, a haemolytic toxin fromAgkistrodon acutusvenom

Phospholipases A2 from Callosellasma rhodostoma venom gland

Differential Expression and Geographic Variation of the Venom Phospholipases A2 of Calloselasma rhodostoma and Trimeresurus mucrosquamatus

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Product

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About

Phospholipases A₂ from Callosellasma rhodostoma venom gland