Novel penicillin G acylase from Achromobacter sp. CCM 4824
作者： František Škrob , Stanislav Bečka , Kamila Plháčková , Vladana Fotopulosová , Pavel Kyslı́k
DOI: 10.1016/S0141-0229(03)00036-X
关键词:
摘要: Abstract A novel penicillin G acylase from the bacterial strain Achromobacter sp. CCM 4824 was characterized. The specific activity of purified enzyme 27.6 U mg −1 protein (6-nitro-3-phenylacetylamidobenzoic acid, NIPAB as substrate). consists two dissimilar subunits α and β with a molecular mass 27.0 62.4 kDa, respectively. isoelectric point about pH 8.8. N-terminal amino acid sequence subunit (SNMWIVGRDHAKDARSILLN) internal (YGYGYAVAQDRLFQMEMAR) exhibited significant similarity acylases. K m values for were 1.9±0.1 4.5±0.2 μM, turnover rates k cat 29±1 19±1 s , maximal hydrolytic found at 7.5 temperature 60 °C. In contrast to published substrate specificities acylases, an almost two-fold ampicillin, amoxicillin cephalexin compared G.
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sci-hub.se 参考文章(31)
Apolinary Szewczuk, Małgorzata Robak, Penicillin amidase from Proteus rettgeri. Acta Biochimica Polonica. ,vol. 28, pp. 275- 284 ,(1981)
T.A. Savidge, M. Cole, [54b] Penicillin acylase (bacterial) Methods in Enzymology. ,vol. 43, pp. 705- 721 ,(1975) , 10.1016/0076-6879(75)43136-6
R M Verhaert, A M Riemens, J M van der Laan, J van Duin, W J Quax, Molecular cloning and analysis of the gene encoding the thermostable penicillin G acylase from Alcaligenes faecalis Applied and Environmental Microbiology. ,vol. 63, pp. 3412- 3418 ,(1997) , 10.1128/AEM.63.9.3412-3418.1997
Alexey L. Margolin, Vytas K. Švedas, Ilya V. Berezin, Substrate specificity of penicillin amidase from E. coli Biochimica et Biophysica Acta. ,vol. 616, pp. 283- 289 ,(1980) , 10.1016/0005-2744(80)90145-X
Miroslav Konstantinović, Nada Marjanović, Goran Ljubijankić, Vladimir Glišin, The penicillin amidase of Arthrobacter viscosus (ATCC 15294). Gene. ,vol. 143, pp. 79- 83 ,(1994) , 10.1016/0378-1119(94)90608-4
Vytas Švedas, Dorel Guranda, Luuk van Langen, Fred van Rantwijk, Roger Sheldon, Kinetic study of penicillin acylase from Alcaligenes faecalis FEBS Letters. ,vol. 417, pp. 414- 418 ,(1997) , 10.1016/S0014-5793(97)01289-1
Roberto Fernández-Lafuente, Odette Hernández-Jústiz, Cesar Mateo, Marco Terreni, Gloria Fernández-Lorente, Miguel A Moreno, Jorge Alonso, Jose L García-López, Jose M Guisan, None, Biotransformations catalyzed by multimeric enzymes: stabilization of tetrameric ampicillin acylase permits the optimization of ampicillin synthesis under dissociation conditions. Biomacromolecules. ,vol. 2, pp. 95- 104 ,(2001) , 10.1021/BM000072I
Ana Roa, Maria P Castillon, Martin L Goble, Richard Virden, Jose L Garcia, None, New Insights on the Specificity of Penicillin Acylase Biochemical and Biophysical Research Communications. ,vol. 206, pp. 629- 636 ,(1995) , 10.1006/BBRC.1995.1089
W.L. Baker, Co‐existence of β‐lactamase and penicillin acylase in bacteria; detection and quantitative determination of enzyme activities Journal of Applied Microbiology. ,vol. 73, pp. 14- 22 ,(1992) , 10.1111/J.1365-2672.1992.TB04963.X
S. G. Senthilvel, J. S. Pai, Purification of penicillin acylase of Bacillus megaterium Biotechnology Techniques. ,vol. 10, pp. 611- 614 ,(1996) , 10.1007/BF00157371