Направленный мутагенез пенициллинацилазы из Escherichia coli для изменения каталитических свойств и стабильности (1105631), страница 26
Текст из файла (страница 26)
Catalytic antibodies and their applications. // Curr. Opin.Biotechnol. 2005. Т. 16. № 6. С. 631–6.75. Tanaka F. Catalytic antibodies as designer proteases and esterases. // Chem. Rev. 2002. Т. 102.№ 12. С. 4885–906.76. Gabor E.M., Janssen D.B. Increasing the synthetic performance of penicillin acylase PAS2 bystructure-inspired semi-random mutagenesis. // Protein Eng. Des. Sel. 2004. Т. 17. № 7. С.
571–9.77. Škrob F., Bečka S., Plháčková K., Fotopulosová V., Kysl k P. Novel penicillin G acylase fromAchromobacter sp. CCM 4824 // Enzyme Microb. Technol. 2003. Т. 32. № 6. С. 738–744.78. Barends T.R.M., Polderman-Tijmes J.J., Jekel P.A., Williams C., Wybenga G., Janssen D.B.,Dijkstra B.W. Acetobacter turbidans alpha-amino acid ester hydrolase: how a single mutationimproves an antibiotic-producing enzyme. // J. Biol. Chem. 2006.
Т. 281. № 9. С. 5804–10.79. Torres-Guzmán R., delaMata I., Torres-Bacete J., Arroyo M., Castillón M.P., Acebal C.Substrate specificity of penicillin acylase from Streptomyces lavendulae. // Biochem. Biophys. Res.Commun. 2002. Т. 291. № 3. С. 593–7.80. Wen Y., Shi X., Yuan Z., Zhou P. Expression, purification, and characterization of His-taggedpenicillin G acylase from Kluyvera citrophila in Escherichia coli.
// Protein Expr. Purif. 2004. Т. 38.№ 1. С. 24–8.81. Chiang C., Bennett R.E. Purification and properties of penicillin amidase from Bacillusmegaterium. // J. Bacteriol. 1967. Т. 93. № 1. С. 302–8.17582. Jager S., Jekel P., Janssen D. Hybrid penicillin acylases with improved properties for synthesisof β-lactam antibiotics // Enzyme Microb.
Technol. 2007. Т. 40. № 5. С. 1335–1344.83. Cheng T., Chen M., Zheng H., Wang J., Yang S., Jiang W. Expression and purification ofpenicillin G acylase enzymes from four different micro-organisms, and a comparative evaluation oftheir synthesis/hydrolysis ratios for cephalexin. // Protein Expr. Purif.
2006. Т. 46. № 1. С. 107–13.84. Verhaert R.M., Riemens A.M., VanderLaan J.M., VanDuin J., Quax W.J. Molecular cloning andanalysis of the gene encoding the thermostable penicillin G acylase from Alcaligenes faecalis. //Appl. Environ. Microbiol. 1997.
Т. 63. № 9. С. 3412–8.85. Svedas V., Guranda D., VanLangen L., VanRantwijk F., Sheldon R. Kinetic study of penicillinacylase from Alcaligenes faecalis. // FEBS Lett. 1997. Т. 417. № 3. С. 414–8.86. Cai G., Zhu S., Yang S., Zhao G., Jiang W. Cloning, Overexpression, and Characterization of aNovel Thermostable Penicillin G Acylase from Achromobacter xylosoxidans : Probing theMolecular Basis for Its High Thermostability // 2004. Т. 70.
№ 5. С. 2764–2770.87. Torres L.L., Ferreras E.R., Cantero A., Hidalgo A., Berenguer J. Functional expression of apenicillin acylase from the extreme thermophile Thermus thermophilus HB27 in Escherichia coli. //Microb. Cell Fact. 2012. Т. 11. С.
105.88. Prieto I., Martin J., Arche R., Fern P., Prez-aranda A., I J.L.B. Penicillin acylase mutants withaltered site-directed activity from Kluyvera citrophila // Appl. Microbiol. 1990. С. 553–559.89. Wang J., Zhang Q., Huang H., Yuan Z., Ding D., Yang S., Jiang W. Increasing syntheticperformance of penicillin G acylase from Bacillus megaterium by site-directed mutagenesis. // Appl.Microbiol.
Biotechnol. 2007. Т. 74. № 5. С. 1023–30.90. Forney L.J., Wong D.C. Alteration of the catalytic efficiency of penicillin amidase fromEscherichia coli. // Appl. Environ. Microbiol. 1989. Т. 55. № 10. С. 2556–60.91. Roa A., Garcia J.L., Salto F., Cortes E. Changing the substrate specificity of penicillin G acylasefrom Kluyvera citrophila through selective pressure. // Biochem. J.
1994. Т. 303. С. 869–75.92. Niersbach H., Kohne A., Tischer W., Weber M., Wedekind F., Plapp R. Improvement of thecatalytic properties of penicillin G acylase from Escherichia coli ATCC 11105 by selection of a newsubstrate specificity // Appl. Microbiol. Biotechnol. 1995.
Т. 43. № 4. С. 679–684.93. Zhou Z., Zhang A., Wang J., Chen M., Li R., Yang S., Yuan Z. Improving the Specific SyntheticActivity of a Penicillin G Acylase Using DNA Family Shuffling // Acta Biochim. Biophys. Sin.(Shanghai). 2003. Т. 35. № 6.
С. 573–579.94. Flores G., Soberón X., Osuna J. Production of a fully functional , permuted single-chainpenicillin G acylase // Protein Sci. 2004. Т. 13. С. 1677–1683.17695. Oliver G., Valle F., Rosetti F., Gómez-Pedrozo M., Santamaría P., Gosset G., Bolivar F. Acommon precursor for the two subunits of the penicillin acylase from Escherichia coli ATCC11105.// Gene. 1985. Т.
40. № 1. С. 9–14.96. Williams J., Zuzel T. Penicillin G acylase (E.C.3.4.1.11) substrate specificity modification by invitro mutagenesis // J Cell Biochem. 1985. № 9B. С. 99.97. Martín J., Prieto I., Barbero J.L., Pérez-Gil J., Mancheño J.M., Arche R. Thermodynamicprofiles of penicillin G hydrolysis catalyzed by wild-type and Met->Ala168 mutant penicillinacylases from Kluyvera citrophila. // Biochim. Biophys. Acta. 1990. Т. 1037.
№ 2. С. 133–9.98. Alkema W.B., Dijkhuis A.J., Vries E. de, Janssen D.B. The role of hydrophobic active-siteresidues in substrate specificity and acyl transfer activity of penicillin acylase // Eur. J. Biochem.2002. Т. 269. № 8. С. 2093–2100.99. Alkema W.B., Hensgens C.M.., Snijder H.J., Keizer E., Dijkstra B.W., Janssen D.B. Structuraland kinetic studies on ligand binding in wild-type and active-site mutants of penicillin acylase. //Protein Eng.
Des. Sel. 2004. Т. 17. № 5. С. 473–80.100. Шаповалова И.В., Алкема В.Б.Л., Ямскова О.В., де Врис Э., Гуранда Д.Ф., Янссен Д.Б.,Швядас В.К. Мутация остатка bF71 в структуре пенициллинацилазы из Escherichia coliприводит к улучшению энантиоселективности и каталитических свойств // Acta Naturae. 2009.Т. 3. С.
65–70.101. Шаповалова И.В. Характеристика новых мутантных форм пенициллинацилазы изEscherichia coli // Кандидатская диссертация, Москва. 2007.102. Yang S., Zhou L., Tang H., Pan J., Wu X., Huang H., Yuan Z. Rational design of a more stablepenicillin G acylase against organic cosolvent // J. Mol. Catal. B Enzym. 2002. Т. 18. № 4-6. С.285–290.103. Yuryev R., Kasche V., Ignatova Z., Galunsky B. Improved A. faecalis penicillin amidasemutant retains the thermodynamic and pH stability of the wild type enzyme. // Protein J.
2010. Т.29. № 3. С. 181–7.104. Guncheva M., Ivanov I., Galunsky B., Stambolieva N., Kaneti J. Kinetic studies and molecularmodelling attribute a crucial role in the specificity and stereoselectivity of penicillin acylase to thepair ArgA145-ArgB263. // Eur. J.
Biochem. 2004. Т. 271. № 11. С. 2272–9.105. Polizzi K.M., Chaparro-Riggers J.F., Vazquez-Figueroa E., Bommarius A.S. Structure-guidedconsensus approach to create a more thermostable penicillin G acylase. // Biotechnol. J. 2006. Т. 1.№ 5.
С. 531–6.106. Serra I., Cecchini D.A., Ubiali D., Manazza E.M., Albertini A.M., Terreni M. Coupling of SiteDirected Mutagenesis and Immobilization for the Rational Design of More Efficient Biocatalysts :The Case of Immobilized 3G3K PGA from E . coli // European J. Org. Chem. 2009. С. 1384–1389.177107.
Scaramozzino F., Estruch I., Rossolillo P., Terreni M., Albertini A.M. Improvement ofCatalytic Properties of Escherichia coli Penicillin G Acylase Immobilized on Glyoxyl Agarose byAddition of a Six-Amino-Acid Tag Improvement of Catalytic Properties of Escherichia coliPenicillin G Acylase Immobilized on Glyoxyl Agarose by // Appl. Environ. Microbiol. 2005. Т.
71.№ 12. С. 8937–40.108. Cecchini D., Pavesi R., Sanna S., Daly S., Xaiz R., Pregnolato M., Terreni M. Efficientbiocatalyst for large-scale synthesis of cephalosporins, obtained by combining immobilization andsite-directed mutagenesis of penicillin acylase. // Appl. Microbiol. Biotechnol. 2012.109. Smith G.P., Petrenko V. Phage Display // Chem. Rev.
1997. Т. 97. № 2. С. 391–410.110. Shi Y.-F., Soumillion P., Ueda M. Effects of catalytic site mutations on active expression ofphage fused penicillin acylase. // J. Biotechnol. 2010. Т. 145. № 2. С. 139–42.111. Stratagene. QuikChange ® Site-Directed Mutagenesis Kit // Mutagenesis. 2010. С. 1–18.112. Dominy C.N., Andrews D.W. Site-directed mutagenesis by inverse PCR. // Methods Mol. Biol.2003. Т. 235. С. 209–23.113. Ясная А.
Клонирование и экспрессия в E.coli пенициллинацилаз для получениямутантных форм с улучшенными свойствами // Кандидатская диссертация, Москва. 2009.114. An Y., Ji J., Wu W., Lv A., Huang R., Wei Y. A rapid and efficient method for multiple-sitemutagenesis with a modified overlap extension PCR. // Appl. Microbiol. Biotechnol. 2005. Т. 68. №6. С. 774–8.115. http://products.invitrogen.com/ivgn/product/S33102.116. Keilmann C., Wanner G., Böck A. Molecular basis of the exclusive low-temperature synthesisof an enzyme in E. coli: penicillin acylase. // Biol Chem Hoppe Seyler. 1993.
Т. 374. С. 983–92.117. Rajendhran J., Gunasekaran P. Recent biotechnological interventions for developing improvedpenicillin G acylases. // J. Biosci. Bioeng. 2004. Т. 97. № 1. С. 1–13.118. Lindsay C., Pain R. The folding and solution conformation of penicillin G acylase // Eur. J.Biochem.
![](https://s.studizba.com/z.php?f=/templates/si/i/noavatar.png&w=100&h=100&t=1"){kind=avatar}
