Cite

[1] Carriger JF, Rand GM, Gardinali PR, Perry WB, Tompkins MS, Fernandez AM. Pesticides of potential ecological concern in sediment from South Florida Canals: An ecological risk prioritization for aquatic arthropods. Soil Sediment Contam. 2006;15:21-45. DOI: 10.1080/15320380500363095.10.1080/15320380500363095Search in Google Scholar

[2] Hussain S, Siddique T, Saleem M, Arshad M, Khalid A. Impact of pesticides on soil microbial diversity, enzymes and biochemical reactions. Adv Agron. 2009;102:159-200. DOI: 10.1016/S0065-2113(09)01005-0.10.1016/S0065-2113(09)01005-0Search in Google Scholar

[3] Hussain S, Arshad M, Saleem M, Khalid A. Biodegradation of α- and β-endosulfan by soil bacteria. Biodegradation. 2007;18:731-740. DOI 10.1007/s10532-007-9102-1.10.1007/s10532-007-9102-1Search in Google Scholar

[4] Hussain S, Arshad M, Saleem M, Zahir Z.A. Screening of soil fungi for in vitro degradation of endosulfan. World J Microbiol Biotechnol. 2007;23:939-945. DOI 10.1007/s11274-006-9317-z.10.1007/s11274-006-9317-zSearch in Google Scholar

[5] Megharaj M, Boul HL, Thiele JH. Effects of DDT and its metabolites onsoil algae and enzymatic activity. Biol Fertil Soils. 1999;29:130-134. http://link.springer.com/article/10.1007/s003740050534#page-1.10.1007/s003740050534Search in Google Scholar

[6] Whalen JK. Managing soil biota-mediated decomposition and nutrient mineralization in sustainable agroecosystems. Adv Agron. 2010; ID 384604. DOI: 10.1155/2014/384604.10.1155/2014/384604Search in Google Scholar

[7] Bandick AK, Dick RP. Field management effects on enzyme activities. Soil Biol Biochem. 1999;31:1471-1479. DOI: 10.1016/S0038-0717(99)00051-6.10.1016/S0038-0717(99)00051-6Search in Google Scholar

[8] MacDonald AG, Tipton KF. Fifty-five years of enzyme classification: advances and difficulties. FEBS Journal. 2014;281:583-592. DOI: 10.1111/febs.12530.10.1111/febs.1253024103004Search in Google Scholar

[9] van Alten DMF, Komander D, Synstad B, Gaseidnes S, Peter MG, Eijsink VGF. Structural insights into the catalytic mechanism of a family 18 exo-chitinase. Proc Natl Acad Sci USA. 2001;98:8979-8984. DOI: 10.1073/pnas.151103798.10.1073/pnas.1511037985535911481469Search in Google Scholar

[10] Brás N, Cerqueira N, Ramos MJ, Fernandes PA. Glycosidases - A Mechanistic Overview. In: Chuan-Fa Chang, editor. Carbohydrates - Comprehensive Studies on Glycobiology and Glycotechnology. Rijeka: InTech; 2012; 117-134. DOI: 10.5772/52019.10.5772/52019Search in Google Scholar

[11] Harman GE, Hayes CK, Lorito M, Broadway RM, diPietro A, Peterbauer C, Tronsmo A, Chitinolytic enzymes of Trichoderma harzianum: purification of chitobiosidase and endochitinase. Mol Plant Pathol. 1993;83:313-318. http://www.apsnet.org/publications/phytopathology/backissues/Documents/1993Articles/Phyto83n03_313.PDF.10.1094/Phyto-83-313Search in Google Scholar

[12] Beier S, Bertilsson S. Bacterial chitin degradation-mechanisms and ecophysiological strategies. Front Microbiol. 2013;4:143. DOI: 10.3389/fmicb.2013.00149.10.3389/fmicb.2013.00149368244623785358Search in Google Scholar

[13] Kielak AM, Cretoiu MS, Semenov AV, Sorensen SJ, van Elsas JD. Bacterial chitinolytic communities respond to chitin and pH alteration in soil. Appl Environ Microbiol. 2013;79:263-272. DOI: 10.1128/AEM.02546-12.10.1128/AEM.02546-12353612123104407Search in Google Scholar

[14] Hamid R, Khan MA, Ahmad M, Ahmad MM, Abdin MZ, Musarrat J, Javed S. Chitinases: An update. J Pharm BioAllied Sci. 2013;5:21-29. DOI: 10.4103/0975-7406.106559.10.4103/0975-7406.106559361233523559820Search in Google Scholar

[15] Metcalfe AC, Krsek M, Gooday GW, Prosser JI, Wellington EMH. Molecular analysis of a bacterial chitinolytic community in an upland pasture. Appl Environ Microbiol. 2002;68:5042-5050. DOI: 10.1128/AEM.68.10.5042-5050.2002.10.1128/AEM.68.10.5042-5050.200212639512324355Search in Google Scholar

[16] Suzuki K, Sugawara N, Suzuki M, Uchiyama T, Katouno F, Nikaidou N, Watanabe T. Chitinases A, B, and C1 of Serratia marcescens 2170 produced by recombinant Escherichia coli: enzymatic properties and synergism on chitin degradation. Biosci Biotechnol Biochem. 2002;66:1075-1083. DOI: 10.1271/bbb.66.1075.10.1271/bbb.66.107512092818Search in Google Scholar

[17] Sato Y, Araki Y. Identification of inducers for chitinase B (ChiB) production in Bacillus cereus CH and estimation of its induction mechanism. J Environ Biotechnol. 2008;8:119-121. http://www.jseb.jp/jeb/08-02/08-02-119.pdf.Search in Google Scholar

[18] Lombard V, Golaconda RH, Drula E, Coutinho PM, Henrissat B. The carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Res. 2014;42:D490-D495. DOI: 10.1093/nar/gkt1178.10.1093/nar/gkt1178396503124270786Search in Google Scholar

[19] Hsieh YC, Wu YJ, Chiang TY, Kuo CY, Shrestha KL, Chao CF, et al. Crystal structures of Bacillus cereus NCTU2 chitinase complexes with chitooligomers reveal novel substrate binding for catalysis: a chitinase without chitin binding and insertion domains. J Biol Chem. 2010;285:31603-31615. DOI: 10.1074/jbc.M110.149310.10.1074/jbc.M110.149310295123420685646Search in Google Scholar

[20] Van Aalten DMF, Synstad B, Brurberg MB, Hough E, Riise BW, Eijsink VGH, et al. Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-Å resolution. Proc Natl Acad Sci USA. 2000;97:5842-5847. DOI: 10.1073/pnas.97.11.5842.10.1073/pnas.97.11.58421852110823940Search in Google Scholar

[21] Papanikolau Y, Prag G, Tavlas G, Vorgias CE, Oppenheim AB, Petratos K. High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis. Biochemistry. 2001;40:11338-11343. DOI: 10.1021/bi010505h.10.1021/bi010505h11560481Search in Google Scholar

[22] Kezuka Y, Ohishi M, Itoh Y, Watanabe J, Mitsutomi M, Watanabe T, et al. Structural studies of a two-domain chitinase from Streptomyces griseus HUT6037. J Mol Biol. 2006;358:472-484. DOI: 10.1016/j.jmb.2006.02.013.10.1016/j.jmb.2006.02.01316516924Search in Google Scholar

[23] Howell VM, Cardinal JW, Richardson AL, Gimm O, Robinson BG, Marsh DJ. Rapid mutation screening for HRPT2 and MEN1 mutations associated with familial and sporadic primary hyperparathyroidism. J Mol Diagn. 2006;8:559-566. DOI: 10.2353/jmoldx.2006.060015.10.2353/jmoldx.2006.060015187616817065424Search in Google Scholar

[24] Suzuki S, Nakanishi E, Ohira T, Kawachi R, Nagasawa H, Sakuda S. Chitinase inhibitor allosamidin is a signal molecule for chitinase production in its producing streptomyces. J Antibiot. 2006:59;402-409. DOI: 10.1038/ja.2006.57.10.1038/ja.2006.5717025016Search in Google Scholar

[25] Rao FV, Houston DR, Boot RG, Aerts JM, Hodkinson M, Adams DJ, et al. Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinases. Chem Biol. 2005;12:65-76. DOI: 10.1016/j.chembiol.2004.10.013.10.1016/j.chembiol.2004.10.01315664516Search in Google Scholar

[26] Saguez J, Vincent C, Giordanengo P. Chitinase inhibitors and chitin mimetics for crop protection. Pest Technol. 2008;2:81-86. https://www.u-picardie.fr/PCP/data/pub/2008-Saguez%20et%20al.Pest%20Technology.pdfSearch in Google Scholar

[27] Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, et al. The Protein Data Bank. Nucleic Acids Res. 2000;28:235-240. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC102472/pdf/gkd090.pdf.10.1093/nar/28.1.23510247210592235Search in Google Scholar

[28] MacDonald JM, Tarling CA, Taylor EJ, Dennis RJ, Myers DS, Knapp S, et al. Chitinase inhibition by chitobiose and chitotriose thiazolines. Angew Chem Int Ed Engl. 2010;49:2599-2602. DOI: 10.1002/anie.200906644.10.1002/anie.20090664420209544Search in Google Scholar

[29] Van Aalten DMF, Komander D, Synstad B, Gseidnes S, Peter MG, Eijsink VGH. Structural insights into the catalytic mechanism of a family 18 exo-chitinase. Proc Natl Acad Sci USA. 2001;98:8979-8984. DOI:10.1073/pnas.151103798.10.1073/pnas.1511037985535911481469Search in Google Scholar

[30] Kolstad G, Synstad B, Eijsink VGH, Van Aalten DMF. Structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 Å resolution. Acta Crystallogr D Biol Crystallogr. 2002;58:377-379. DOI: 10.1107/S0907444901018972.10.1107/S090744490101897211807282Search in Google Scholar

[31] Vaaje-Kolstad G, Houston DR, Rao FV, Peter MG, Synstad B, Van Aalten DMF, et al. Structure of the D142N mutant of the family 18 chitinase ChiB from Serratia marcescens and its complex with allosamidin. Biochim Biophys Acta. 2004;1696:103-111. DOI:10.1016/j.bbapap.2003.09.014.10.1016/j.bbapap.2003.09.01414726210Search in Google Scholar

[32] Vaaje-Kolstad G, Vasella A, Peter MG, Netter C, Houston DR, Westereng B, et al. Interactions of a family 18 chitinase with the designed inhibitor HM508 and its degradation product, chitobiono-delta-lactone. J Biol Chem. 2004; 279:3612-3619. DOI 10.1074/jbc.M310057200.10.1074/jbc.M31005720014597613Search in Google Scholar

[33] Houston DR, Synstad B, Eijsink VGH, Stark MJ, Eggleston I, Van Aalten DMF. Structure-based exploration of cyclic dipeptide chitinase inhibitors. J Med Chem. 2004;47:5713-5720. DOI: 10.1021/jm049940a.10.1021/jm049940a15509170Search in Google Scholar

[34] Pettersen EF, Goddard TD, Huang CC, Couch GS, Greeblatt DM, Meng EC, et al. UCSF Chimera - A visualization system for exploratory research and analysis. J Comput Chem. 2004;25:1605-1612. DOI: 10.1002/jcc.20084.10.1002/jcc.2008415264254Search in Google Scholar

[35] Larkin MA, Blackshields G, Brown NP, Chenna R, McGettigan PA, McWilliam H, et al. ClustalW and ClustalX version 2.0. BMC Bioinf. 2007;23:2947-2948. DOI: 10.1093/bioinformatics/btm404.10.1093/bioinformatics/btm40417846036Search in Google Scholar

[36] Marti-Renon MA, Capriotti E, Shindyalov IN, Bourne PE. Structure Comparison and Alignment. In: Gu J, Bourne PE, editors. Structural Bioinformatics. Hoboken, New Jersey: John Wiley & Sons; 2009. http://www.sdsc.edu/pb/papers/c16.pdf.Search in Google Scholar

[37] Le Guilloux V, Schmidtke P, Tuffery P. Fpocket: An open source platform for ligand pocket detection. BMC Bioinf. 2009;10:168. DOI:10.1186/1471-2105-10-168.10.1186/1471-2105-10-168270009919486540Search in Google Scholar

[38] Irwin JJ, Shoichet BK. Zinc - a free database of commercially available compounds for virtual screening. J Chem Inf Model. 2005;45:177-182. DOI: 10.1021/ci049714.10.1021/ci049714+136065615667143Search in Google Scholar

[39] Grosdidier A, Zoete V, Michielin O. SwissDock - a protein-small molecule docking web service based on EADock DSS. Nucleic Acids Res. 2011;39:W270-W277. DOI:10.1093/nar/gkr366.10.1093/nar/gkr366312577221624888Search in Google Scholar

[40] Schneidman-Duhovny D, Inbar Y, Nussinov R, Wolfson HJ. PatchDock and SymmDock: servers for rigid and symmetric docking. Nucleic Acids Res. 2005;33:W363-367. DOI:10.1093/nar/gki481.10.1093/nar/gki481116024115980490Search in Google Scholar

[41] Grosdidier A, Zoete V, Michielin O. EADock: A multiobjective evolutionary framework for the docking of small molecules into protein active site. Proteins: Struct Funct Bioinf. 2007;67:1010-1025. DOI: 10.1002/prot.21367.10.1002/prot.2136717380512Search in Google Scholar

[42] Andrusier N, Nussinov R, Wolfson HJ. FireDock: fast interaction refinement in molecular docking. Proteins. 2007;69:139-59. DOI: 10.1002/prot.21495.10.1002/prot.2149517598144Search in Google Scholar

[43] Firoz A, Malik A, Afzal O, Jha V. ContPro: A web tool for calculating amino acid contact distances in protein from 3D-structures at different distance threshold. Bioinformation. 2010;5:55-57. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3039989/.10.6026/97320630005055303998921346863Search in Google Scholar

[44] Vlădoiu DL, Filimon MN, Ostafe V, Isvoran A. Assessment of pesticides interactions with Bacillus pasteurii urease. A computational study. Rom J Phys. 2015;60:583-592. http://www.nipne.ro/rjp/2015_60_3-4/0583_0592.pdf.Search in Google Scholar

[45] Singh G, Wright D. Effect of herbicides on nodulation, symbiotic nitrogen fixation, growth and yield of pea (Pisum sativum). J Agric Sci. 1999;133:21-30. DOI: 10.1017/S0021859699006735.10.1017/S0021859699006735Search in Google Scholar

[46] Ismail BS, Jokha Y, Omar O. Effects of glufosinate-ammonium on microbial population and enzyme activities in soils. Microbios. 1995;83:185-190.Search in Google Scholar

[47] Filimon MN, Voia SO, Popescu R, Bordean DM, Vladoiu DL, Mituletu M, et al. The effect of chlorsulfuron and MCPB-Na on the enzymatic activity of microorganisms. J Serb Chem Soc. 2014;79:1075-1084. DOI: 10.2298/JSC140115031F.10.2298/JSC140115031FSearch in Google Scholar

[48] Antonious GF. Impact of soil management and two botanical insecticides on urease and invertase activity. J Environ Sci Health B. 2003;38:479-488. DOI: 10.1081/PFC-120021667.10.1081/PFC-12002166712856929Search in Google Scholar

[49] Demanou J, Monkiedje A, Njine T, Foto SM, Nola M, Serges H, et al. Changes in soil chemical properties and microbial activities in response to the fungicide Ridomil gold plus copper. Int J Environ Res Public Health. 2004;1:26-34. DOI: 10.3390/ijerph2004010026.10.3390/ijerph200401002616696178Search in Google Scholar

eISSN:
1898-6196
Language:
English