L-Amino acid oxidase from Naja naja oxiana venom

被引：53
作者：
Samel, Mari [1 ]
Tonismagi, Kulli [1 ]
Ronnholm, Gunilla [2 ,3 ]
Vija, Heiki [1 ]
Siigur, Jueri [1 ]
Kalkkinen, Nisse [2 ,3 ]
Siigur, Ene [1 ]
机构：
[1] NICPB, EE-12618 Tallinn, Estonia
[2] Univ Helsinki, Inst Biotechnol, Prot Chem Res Grp, FIN-00014 Helsinki, Finland
[3] Univ Helsinki, Inst Biotechnol, Core Facil, FIN-00014 Helsinki, Finland
来源：
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 2008年 / 149卷 / 04期
关键词：
snake venom; Naja naja oxiana; L-amino acid oxidase; platelet aggregation; antibacterial activity; partial sequencing;
D O I：
10.1016/j.cbpb.2007.11.008
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
A new L-amino acid oxidase (LAAO) was isolated from the Central Asian cobra Naja naja oxiana venom by size exclusion, ion exchange and hydrophobic chromatography. The N-terminal sequence and the internal peptide sequences share high similarity with other snake venom L-amino acid oxidases, especially with those isolated from elapid venoms. The enzyme is stable at low temperatures (-20 degrees C, -70 degrees C) and loses its activity by heating at 70 degrees C. Specific substrates for the isolated protein are L-phenylalanine, L-tryptophan, L-methionine and L-leucine. The enzyme has antibacterial activity inhibiting the growth of Gram-positive (Bacillus subtilis) and Gram-negative (Escherichia coli) bacteria. N. naja oxiana LAAO dose-dependently inhibited ADP- or collagen-induced platelet aggregation with IC50 of 0.094 mu M and 0.036 mu M, respectively. The antibacterial and anti-aggregating activity was abolished by catalase. (c) 2007 Elsevier Inc. All rights reserved.
引用
收藏
页码：572 / 580
页数：9
相关论文
共 47 条
[1]   Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah) [J].
Ahn, MY ;
Lee, BM ;
Kim, YS .
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 1997, 29 (06) :911-919
[2]   Isolation, structural, and functional characterization of an apoptosis-inducing L-amino acid oxidase from leaf-nosed viper (Eristocophis macmahoni) snake venom [J].
Ali, SA ;
Stoeva, S ;
Abbasi, A ;
Alam, JM ;
Kayed, R ;
Faigle, M ;
Neumeister, B ;
Voelter, W .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2000, 384 (02) :216-226
[3]   Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].
Altschul, SF ;
Madden, TL ;
Schaffer, AA ;
Zhang, JH ;
Zhang, Z ;
Miller, W ;
Lipman, DJ .
NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402
[4]  
Bergmeyer HU, 1983, METHOD ENZYMAT AN, V2, P149
[5]   Cloning and biochemical characterization of APIT, a new L-amino acid oxidase from Aplysia punctata [J].
Butzke, D ;
Hurwitz, R ;
Thiede, B ;
Goedert, S ;
Rudel, T .
TOXICON, 2005, 46 (05) :479-489
[6]   Snake venom L-amino acid oxidases [J].
Du, XY ;
Clemetson, KJ .
TOXICON, 2002, 40 (06) :659-665
[7]   Antimicrobial action of achacin is mediated by L-amino acid oxidase activity [J].
Ehara, T ;
Kitajima, S ;
Kanzawa, N ;
Tamiya, T ;
Tsuchiya, T .
FEBS LETTERS, 2002, 531 (03) :509-512
[8]   Molecular approaches for structural characterization of Bothrops L-amino acid oxidases with antiprotozoal activity:: cDNA cloning, comparative sequence analysis, and molecular modeling [J].
Franca, Suzelei C. ;
Kashima, Simone ;
Roberto, Patricia G. ;
Marins, Mozart ;
Ticli, Fabio K. ;
Pereira, Jose Odair ;
Astolfi-Filho, Spartaco ;
Stabeli, Rodrigo G. ;
Magro, Angelo J. ;
Fontes, Marcos R. M. ;
Sampaio, Suely V. ;
Soares, Andreimar M. .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2007, 355 (02) :302-306
[9]   ACTIVATION OF BOVINE FACTOR-V BY AN ACTIVATOR PURIFIED FROM THE VENOM OF NAJA-NAJA-OXIANA [J].
GERADS, I ;
TANS, G ;
YUKELSON, LY ;
ZWAAL, RFA ;
ROSING, J .
TOXICON, 1992, 30 (09) :1065-1079
[10]   AMINO-ACID SEQUENCE OF NEUROTOXIN-1 FROM NAJA-NAJA-OXIANA VENOM [J].
GRISHIN, EV ;
SUKHIKH, AP ;
SLOBODYAN, LN ;
OVCHINNIKOV, YA ;
SOROKIN, VM .
FEBS LETTERS, 1974, 45 (01) :118-121
12345