Purification and characterization of a new l-amino acid oxidase from Daboia russellii siamensis venom

Zhong, Shaobin; Jin, Yang; Wu, Jianbo; Jia, Yongxing; Xu, Gelin; Wang, Gen-Chun; Xiong, Ya; Lu, Qiumin

doi:10.1016/j.toxicon.2009.06.004

Cited by 48 publications

(46 citation statements)

References 38 publications

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“…This is probably due to the high purity of the isolated LAAO enzyme. A recent study on Siamese Russell's viper (Daboia russellii siamensis) compared the MIC of king cobra LAAO enzyme with other LAAOs, the MIC of the Siamese Russell's viper LAAO enzyme against Staphylococcus aureus ATCC 25923, Pseudomonas aeruginosa ATCC 27853 and Escherichia coli ATCC 25922 was 9.0 μg/mL, 144.0 μg/mL and 288.0 μg/mL, all of which were higher than the MIC of king cobra LAAO (32).…”

Section: Mic Of King Cobra Venom Laao Enzymementioning

confidence: 98%

Purification and antibacterial activities of an L-amino acid oxidase from king cobra (Ophiophagus hannah) venom

Phua¹,

Vejayan²,

Ambu³

et al. 2012

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

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Some constituents of snake venom have been found to display a variety of biological activities. The antibacterial property of snake venom, in particular, has gathered increasing scientific interest due to antibiotic resistance. In the present study, king cobra venom was screened against three strains of Staphylococcus aureus [including methicillin-resistant Staphylococcus aureus (MRSA)], three other species of gram-positive bacteria and six gram-negative bacteria. King cobra venom was active against all the 12 bacteria tested, and was most effective against Staphylococcus spp. (S. aureus and S. epidermidis). Subsequently, an antibacterial protein from king cobra venom was purified by gel filtration, anion exchange and heparin chromatography. Mass spectrometry analysis confirmed that the protein was king cobra L-amino acid oxidase (Oh-LAAO). SDS-PAGE showed that the protein has an estimated molecular weight of 68 kDa and 70 kDa under reducing and non-reducing conditions, respectively. The minimum inhibitory concentrations (MIC) of Oh-LAAO for all the 12 bacteria were obtained using radial diffusion assay method. Oh-LAAO had the lowest MIC value of 7.5 µg/mL against S. aureus ATCC 25923 and ATCC 29213, MRSA ATCC 43300, and S. epidermidis ATCC 12228. Therefore, the LAAO enzyme from king cobra venom may be useful as an antimicrobial agent.

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Section: Mic Of King Cobra Venom Laao Enzymementioning

confidence: 98%

Purification and antibacterial activities of an L-amino acid oxidase from king cobra (Ophiophagus hannah) venom

Phua¹,

Vejayan²,

Ambu³

et al. 2012

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

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“…Such high competence for a negatively charged amino acid is unusual. The Lao-enzymes from other eukaryotes oxidize glutamate only slowly or not at all (relative activities 0-17 %) (Bender & Krebs, 1950;Zhong et al, 2009), while the highly agile Lao of the actinobacterium Rhodococcus opacus achieved a relative activity of 44 % (Geueke & Hummel, 2002). Interestingly, this apparent shift in relative substrate utilization in Lao1 of H. cylindrosporum did not cause gross discrimination against other L-amino acids, since significant activities were also The amino acids that displayed more than 2 % relative activity are shown.…”

Section: Stability and Catalytic Properties Of Recombinant Lao1mentioning

confidence: 99%

l-Amino acid oxidase of the fungus Hebeloma cylindrosporum displays substrate preference towards glutamate

et al. 2012

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Catabolism of amino acids is a central process in cellular nitrogen turnover, but only a few of the mechanisms involved have been described from basidiomycete fungi. This study identified one such mechanism, the L-amino acid oxidase (Lao1) enzyme of Hebeloma cylindrosporum, by 2D gel separation and MS. We determined genomic DNA sequences of lao1 and part of its upstream gene, a putative pyruvate decarboxylase (pdc2), and cloned the cDNA of lao1. The two genes were also identified and annotated from the genome of Laccaria bicolor. The lao1 and pdc2 gene structures were conserved between the two fungi. The intergenic region of L. bicolor possessed putative duplications not detected in H. cylindrosporum. Lao1 sequences possessed dinucleotide-binding motifs typical for flavoproteins. Lao1 was less than 23 % identical to Lao sequences described previously. Recombinant Lao1 of H. cylindrosporum was expressed in Escherichia coli, purified and refolded with SDS to gain catalytic activity. The enzyme possessed broad substrate specificity: 37 L-amino acids or derivatives served as effective substrates. The highest activities were recorded with L-glutamate, but positively charged and aromatic amino acids were also accepted. Michaelis constants for six amino acids varied from 0.5 to 6.7 mM. We have thus characterized a novel type of Lao-enzyme and its gene from the basidiomycete fungus H. cylindrosporum.

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“…Hydrogen peroxide not alone is responsible for these biological activities of SVLAAOs; that is, other mechanisms are probably triggered and cause a potent biological response [19]. Some studies have been conducted to determine the true mode of action of LAAOs in the induction of edema, that revealed that the action of these compounds is related to the stimulation and release of inflammatory mediators such as histamine, prostaglandin, kinins, and serotonin [25].…”

Section: A Potent Biochemical Analoguementioning

confidence: 99%

“…King cobra venom was most efficient against Escherichia coli and was least effective against Pseudomonas aeruginosa [34]. A recent study describe that the minimum inhibitory concentrations (MIC)of the Siamese Russell's viper LAAO enzyme against Staphylococcus aureus ATCC 25923, Pseudomonas aeruginosa ATCC 27853 and Escherichia coli ATCC 25922 higher than the MIC of king cobra LAAO [19]. It is also shown antiviral effect which has been well explored.…”

Section: A Potent Pharmacological Agentmentioning

confidence: 99%

A Novel Biochemical and Pharmacological Agent: L-Amino Acid Oxidase With Correlation to Cancer Management: An Overview

Murti¹,

Sethi²,

Nadeem³

et al. 2014

iosrphr

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Purification and characterization of a new l-amino acid oxidase from Daboia russellii siamensis venom

Cited by 48 publications

References 38 publications

Purification and antibacterial activities of an L-amino acid oxidase from king cobra (Ophiophagus hannah) venom

Purification and antibacterial activities of an L-amino acid oxidase from king cobra (Ophiophagus hannah) venom

l-Amino acid oxidase of the fungus Hebeloma cylindrosporum displays substrate preference towards glutamate

A Novel Biochemical and Pharmacological Agent: L-Amino Acid Oxidase With Correlation to Cancer Management: An Overview

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