메뉴 건너뛰기




Volumn 59, Issue 9, 2011, Pages 4519-4526

A novel L-amino acid oxidase from Trichoderma harzianum ETS 323 associated with antagonism of Rhizoctonia solani

Author keywords

Biocontrol; Flavoprotein; L amino acid oxidase; Rhizoctonia solani; Trichoderma harzianum

Indexed keywords

AMINO ACID SEQUENCE; ANTAGONISTIC EFFECTS; BINDING MOTIF; BIOCONTROL AGENT; BIOLOGICAL FUNCTIONS; EXTRACELLULAR PROTEINS; FLAVOPROTEIN; HOMODIMERIC PROTEINS; IN-VITRO ASSAYS; L-AMINO ACID OXIDASE; L-PHENYLALANINE; MONOMERIC FORMS; PHYTOPATHOGENS; RHIZOCTONIA SOLANI; SUBSTRATE SPECIFICITY; TRICHODERMA; TRICHODERMA HARZIANUM;

EID: 79955695549     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf104603w     Document Type: Article
Times cited : (36)

References (25)
  • 1
    • 0001820032 scopus 로고
    • Trichoderma: Application, mode of action and potential as a biocontrol agent of soilborne plant pathogenic fungi
    • Chet I., Ed.; Wiley: New York
    • Chet, I. Trichoderma: application, mode of action and potential as a biocontrol agent of soilborne plant pathogenic fungi. In InnoVatiVe Approaches to Plant Disease Control; Chet, I., Ed.; Wiley: New York, 1987; pp 137-160.
    • (1987) InnoVatiVe Approaches to Plant Disease Control , pp. 137-160
    • Chet, I.1
  • 3
    • 34447118987 scopus 로고    scopus 로고
    • Mycoparasitism studies of Trichoderma harzianum strains against Rhizoctonia solani: Evaluation of coiling and hydrolytic enzyme production
    • DOI 10.1007/s10529-007-9372-z
    • Almeida, F. B.; Cerqueira, F. M.; Nascimento, R. N.; Ulhoa, C. J.; Lima, A. L. Mycoparasitism studies of Trichoderma harzianum strains against Rhizoctonia solani: Evaluation of coiling and hydrolytic enzyme production. Biotechnol. Lett. 2007, 29, 1189-1193. (Pubitemid 47035012)
    • (2007) Biotechnology Letters , vol.29 , Issue.8 , pp. 1189-1193
    • Almeida, F.B.D.R.1    Cerqueira, F.M.2    Silva, R.D.N.3    Ulhoa, C.J.4    Lima, A.L.5
  • 4
    • 0034120004 scopus 로고    scopus 로고
    • Colony growth, in vitro antagonism and secretion of extracellular enzymes in cold-tolerant strains of Trichoderma species
    • DOI 10.1017/S0953756299001653
    • Antal, Z.; Manczinger, L.; Szakács, G.; Tengerdy, R. P.; Ferenczy, L. Colony growth, in vitro antagonism and secretion of extracellular enzymes in cold tolerant strains of Trichoderma species. Mycol. Res. 2000, 104, 545-549. (Pubitemid 30411317)
    • (2000) Mycological Research , vol.104 , Issue.5 , pp. 545-549
    • Antal, Zs.1    Manczinger, L.2    Szakacs, Gy.3    Tengerdy, R.P.4    Ferenczy, L.5
  • 5
    • 51649107641 scopus 로고    scopus 로고
    • Proteomic study of biocontrol mechanisms of Trichoderma harzianum ETS 323 in response to Rhizoctonia solani
    • Tseng, S. C.; Liu, S. Y.; Yang, H. H.; Lo, C. T.; Peng, K. C. Proteomic study of biocontrol mechanisms of Trichoderma harzianum ETS 323 in response to Rhizoctonia solani. J. Agric. Food Chem. 2008, 56, 6914-6922.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 6914-6922
    • Tseng, S.C.1    Liu, S.Y.2    Yang, H.H.3    Lo, C.T.4    Peng, K.C.5
  • 6
    • 33646110520 scopus 로고    scopus 로고
    • Isolation and characterization of an apoptotic and platelet aggregation inhibiting L-amino acid oxidase from Vipera berus berus (common viper) venom
    • Samel, M.; Vija, H.; Rönnholm, G.; Siigur, J.; Kalkkinen, N.; Siigur, E. Isolation and characterization of an apoptotic and platelet aggregation inhibiting L-amino acid oxidase from Vipera berus berus (common viper) venom. Biochim. Biophys. Acta 2006 1764, 707-714.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 707-714
    • Samel, M.1    Vija, H.2    Rönnholm, G.3    Siigur, J.4    Kalkkinen, N.5    Siigur, E.6
  • 7
    • 0037145809 scopus 로고    scopus 로고
    • Antimicrobial action of achacin is mediated by L-amino acid oxidase activity
    • DOI 10.1016/S0014-5793(02)03608-6, PII S0014579302036086
    • Ehara, T.; Kitajima, S.; Kanzawa, N.; Tamiya, T.; Tsuchiya, T. Antimicrobial action is mediated by L-amino acid oxidase activity. FEBS Lett. 2002, 531, 509-512. (Pubitemid 35336077)
    • (2002) FEBS Letters , vol.531 , Issue.3 , pp. 509-512
    • Ehara, T.1    Kitajima, S.2    Kanzawa, N.3    Tamiya, T.4    Tsuchiya, T.5
  • 8
    • 26844491279 scopus 로고    scopus 로고
    • Cloning, characterization and expression of escapin, a broadly antimicrobial FAD-containing L-amino acid oxidase from ink of the sea hare Aplysia californica
    • DOI 10.1242/jeb.01795
    • Yang, H.; Johnson, P.M.; Ko, K. C.; Kamio,M.; Germann,M.W.; Derby, C. D.; Tai, P. C. Cloning, characterization and expression of escapin, a broadly antimicrobialFAD-containing L-amino acid oxidase from ink the sea hare Aplysia californica. J. Exp. Biol. 2005, 208, 3609-3622. (Pubitemid 41463281)
    • (2005) Journal of Experimental Biology , vol.208 , Issue.18 , pp. 3609-3622
    • Yang, H.1    Johnson, P.M.2    Ko, K.-C.3    Kamio, M.4    Germann, M.W.5    Derby, C.D.6    Tai, P.C.7
  • 9
    • 0014944573 scopus 로고
    • L-Amino acid oxidase, a bactericidal system
    • Skarnes, R. C. L-Amino acid oxidase, a bactericidal system. Nature 1970, 225, 1072-1073.
    • (1970) Nature , vol.225 , pp. 1072-1073
    • Skarnes, R.C.1
  • 10
    • 0036234815 scopus 로고    scopus 로고
    • Snake L-amino acid oxidases
    • Du, X. Y.; Clemetson, K. J. Snake L-amino acid oxidases. Toxicon 40: 659-665.
    • Toxicon , vol.40 , pp. 659-665
    • Du, X.Y.1    Clemetson, K.J.2
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 14644432391 scopus 로고    scopus 로고
    • Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243
    • DOI 10.1128/JB.187.6.2084-2092.2005
    • Nishizawa, T.; Aldrich, C. C.; Sherman, D. H. Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243. J. Bacteriol. 2005, 187, 2084-2092. (Pubitemid 40316239)
    • (2005) Journal of Bacteriology , vol.187 , Issue.6 , pp. 2084-2092
    • Nishizawa, T.1    Aldrich, C.C.2    Sherman, D.H.3
  • 14
    • 0033970608 scopus 로고    scopus 로고
    • New sequence motifs in flavoproteins: Evidence for common ancestry and tools to predict structure
    • DOI 10.1002/(SICI)1097-0134(20000101)38:1<95::AID-PROT10>3.0.CO;2-A
    • Vallon, O. New sequence motifs in Flavoproteins: Evidence for common ancestry and tools to predict structure. Proteins 2000, 38, 95-114. (Pubitemid 30020606)
    • (2000) Proteins: Structure, Function and Genetics , vol.38 , Issue.1 , pp. 95-114
    • Vallon, O.1
  • 15
    • 0034724181 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of apoxin I, a snake venom- derived apoptosis-inducing factor with L-amino acid oxidase activity
    • DOI 10.1021/bi992416z
    • Torii, S.; Yamane, K.; Mashima, T.; Haga, N.; Yamamoto, K.; Fox, J. W.; Naito, M.; Tsuruo, T. Molecular cloning and functional analysis of apoxin I, a snake venom-derived apoptosis inducing factor with L-amino acid oxidase activity. Biochemistry 2000, 39, 3197-3205. (Pubitemid 30169988)
    • (2000) Biochemistry , vol.39 , Issue.12 , pp. 3197-3205
    • Torii, S.1    Yamane, K.2    Mashima, T.3    Haga, N.4    Yamamoto, K.5    Fox, J.W.6    Naito, M.7    Tsuruo, T.8
  • 17
    • 0025784241 scopus 로고
    • Antibacterial effects of different snake venoms: Purification and characterization of antibacterial proteins from Pseudechis australis (Australian king brown or mulga snake) venom
    • Stiles, B. G.; Sexton, F. W.; Weinstein, S. A. Antibacterial effects of different snake venoms: purification and characterization of antibacterial proteins from Pseudechis australis (Australian king brown or mulga snake) venom. Toxicon 1991, 29, 1129-1141.
    • (1991) Toxicon , vol.29 , pp. 1129-1141
    • Stiles, B.G.1    Sexton, F.W.2    Weinstein, S.A.3
  • 18
    • 0037145809 scopus 로고    scopus 로고
    • Antimicrobial action of achacin is mediated by L-amino acid oxidase activity
    • DOI 10.1016/S0014-5793(02)03608-6, PII S0014579302036086
    • Ehara, T.; Kitajima, S.; Kanzawa, N.; Tamiya, T.; Tsuchiya, T. Antimicrobial action is mediated by L-amino acid oxidase activity. FEBS Lett. 2002, 531, 509-512. (Pubitemid 35336077)
    • (2002) FEBS Letters , vol.531 , Issue.3 , pp. 509-512
    • Ehara, T.1    Kitajima, S.2    Kanzawa, N.3    Tamiya, T.4    Tsuchiya, T.5
  • 19
    • 33845626586 scopus 로고    scopus 로고
    • Identification of an antibacterial protein as L-amino acid oxidase in the skin mucus of rockfish Sebastes schlegeli
    • DOI 10.1111/j.1742-4658.2006.05570.x
    • Kitani, Y.; Tsukamoto, C.; Zhang, G.; Nagai, H.; Ishida, M.; Ishizaki, S.; Shimakura, K.; Shiomi, K.; Nagashima, Y. Identification of an antibacterial protein as L-amino acid oxidase in the skin mucus of rockfish Sebastes schlegeli. FEBS J. 2007, 274 (1), 125-36. (Pubitemid 44952903)
    • (2007) FEBS Journal , vol.274 , Issue.1 , pp. 125-136
    • Kitani, Y.1    Tsukamoto, C.2    Zhang, G.3    Nagai, H.4    Ishida, M.5    Ishizaki, S.6    Shimakura, K.7    Shiomi, K.8    Nagashima, Y.9
  • 20
    • 0030570468 scopus 로고    scopus 로고
    • Identification of the snake venom substance that induces apoptosis
    • Suhr, S. M.; Kim, D. S. Identification of the snake venom substance that induces apoptosis. Biochem. Biophys. Res. Commun. 1996, 224, 134-139.
    • (1996) Biochem. Biophys. Res. Commun. , vol.224 , pp. 134-139
    • Suhr, S.M.1    Kim, D.S.2
  • 21
    • 0030910602 scopus 로고    scopus 로고
    • Apoxin I, a novel apoptosis-inducing factor with L-amino acid oxidase activity purified from western diamondback rattlesnake venom
    • DOI 10.1074/jbc.272.14.9539
    • Torii, S.; Naito, M.; Tsuruo, T. Apoxin I, a novel apoptosisinducing factor with L-amino acid oxidase activity purified from western diamondback rattlesnake venom. J. Biol. Chem. 1997, 272, 9539-9542. (Pubitemid 27154972)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.14 , pp. 9539-9542
    • Torii, S.1    Naito, M.2    Tsuruo, T.3
  • 22
    • 77649187050 scopus 로고    scopus 로고
    • Biochemical functional and structural characterization of Akbu- LAAO: A novel snake venom L-amino acid oxidase from Agkistrodon blomhoffii ussurensis
    • Sun, M. Z.; Guo, C.; Tian, Y.; Chen, D.; Greenaway, F. T.; Liu, S. Biochemical, functional and structural characterization of Akbu- LAAO: A novel snake venom L-amino acid oxidase from Agkistrodon blomhoffii ussurensis. Biochimie 2010, 92, 343-349.
    • (2010) Biochimie , vol.92 , pp. 343-349
    • Sun, M.Z.1    Guo, C.2    Tian, Y.3    Chen, D.4    Greenaway, F.T.5    Liu, S.6
  • 23
    • 0034792723 scopus 로고    scopus 로고
    • Inhibition of human platelet aggregation by L-amino acid oxidase purified from Naja naja kaouthia venom
    • DOI 10.1016/S0041-0101(01)00133-7, PII S0041010101001337
    • Sakurai, Y.; Takatsuka, H.; Yoshioka, A.; Matsui, T.; Suzuki, M.; Titani, K.; Fujimura, Y. Inhibition of human platelet aggregation by L-amino acid oxidase purified from Naja naja kaouthia venom. Toxicon 2002, 39, 1827-1833. (Pubitemid 32971821)
    • (2001) Toxicon , vol.39 , Issue.12 , pp. 1827-1833
    • Sakurai, Y.1    Takatsuka, H.2    Yoshioka, A.3    Matsui, T.4    Suzuki, M.5    Titani, K.6    Fujimura, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.