Enhancing enzymatic activity of penicillin G acylase by coexpressing pcm gene

Applied Microbiology and Biotechnology

Volumn 72, Issue 5, 2006, Pages 953-958

  Wang, Tianwen ^a   Zhu, Hu ^a   Ma, Xingyuan ^a   Fei, Zhuoya ^a   Ma, Yushu ^a   Wei, Dongzhi ^a  

^a EAST CHINA UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

PENICILLIN G ACYLASE; RECOMBINANT PLASMIDS;

ANTIBIOTICS; BIOTECHNOLOGY; CELLS; ESCHERICHIA COLI; GENES;

ENZYMES;

AMIDASE; ISOASPARTATE METHYLTRANSFERASE; METHYLTRANSFERASE; PENICILLIN G ACYLASE; UNCLASSIFIED DRUG;

ANTIBIOTICS; COLIFORM BACTERIUM; ENZYME ACTIVITY; GENE EXPRESSION; RECOMBINATION;

ALCALIGENES FAECALIS; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE EXPRESSION; GENE FUNCTION; GENE INDUCTION; HOST CELL; NONHUMAN; NUCLEOTIDE SEQUENCE;

ALCALIGENES FAECALIS; CLONING, MOLECULAR; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; PENICILLIN AMIDASE; PLASMIDS; RECOMBINANT PROTEINS;

ALCALIGENES FAECALIS; ESCHERICHIA COLI;

EID: 33749174590     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-006-0349-y     Document Type: Article

References (30)

1. Bradford MM (1976) A rapid and sensitive for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
2. Clark ED (2001) Protein refolding for industrial processes. Curr Opin Biotechnol 12:202-207
3. Clarke S (2003) Aging as war between chemical and biochemical processes: protein methylation and the recognition of age-damaged proteins for repair. Ageing Res Rev 2:263-285
4. Dirnbach E, Steel DG, Gafni A (1999) Proline isomerization is unlikely to be the cause of slow annealing and reactivation during the folding of alkaline phosphatase. J Biol Chem 274:4532-4536
5. Ellis RJ, Hemmingsen SM (1989) Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures. Trends Biochem Sci 14:339-342
6. Ermolenko DN, Zherdev AV, Dzantiev BB (2004) Antibodies as specific chaperones. Biochemistry (Mosc) 69:1233-1238
7. Fahnert B, Lilie H, Neubauer P (2004) Inclusion bodies: formation and utilisation. Adv Biochem Eng Biotechnol 89:93-142
8. Fu JC, Ding L, Clarke S (1991) Purification, gene cloning, and sequence analysis of an L-isoaspartyl protein carboxyl methyltransferase from Escherichia coli. J Biol Chem 266:14562-14572
9. Guise AD, West SM, Chaudhuri JB (1996) Protein folding in vivo and renaturation of recombinant proteins from inclusion bodies. Mol Biotechnol 6:53-64
10. Joshi BH, Puri RK (2005) Optimization of expression and purification of two biologically active chimeric fusion proteins that consist of human interleukin-13 and Pseudomonas exotoxin in Escherichia coli. Protein Expr Purif 39:189-198
11. Kern R, Malki A, Abdallah J, Liebart JC, Dubucs C, Yu MH, Richarme G (2005) Protein isoaspartate methyltransferase is a multicopy suppressor of protein aggregation in Escherichia coli. J Bacteriol 187:1377-1383
12. Kim SG, Kweon DH, Lee DH, Park YC, Seo JH (2005) Coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli. Protein Expr Purif 4:426-432
13. Kondo A, Kohda J, Endo Y, Shiromizu T, Kurokawa Y, Nishihara K, Yanagi H, Yura T, Fukuda H (2000) Improvement of productivity of active horseradish peroxidase in Escherichia coli by coexpression of Dsb proteins. J Biosci Bioeng 90:600-606
14. Lee S, Sowa ME, Choi JM, Tsai FT (2004) The ClpB/Hsp104 molecular chaperone - a protein disaggregating machine. J Struct Biol 146:99-105
15. Liang Y, Li W, Ma Q, Zhang Y (2005) Functional properties of PDIA from Aspergillus niger in renaturation of proteins. FEMS Microbiol Lett 245:363-368
16. Lin SY, Kondo F (2001) A simple classification method for residual antibiotics using E. coli cells transformed by the calcium chloride method and drug resistance plasmid DNA. Microbios 104:149-158
17. Liu Y, Zhao TJ, Yan YB, Zhou HM (2005) Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system. Protein Expr Purif 44:155-161
18. Merli S, Corti A, Cassani G (1995) Production of soluble tumor necrosis factor receptor type I in Escherichia coli: optimization of the refolding yields by a microtiter dilution assay. Anal Biochem 230:85-91
19. Middelberg AP (2002) Preparative protein refolding. Trends Biotechnol 20:437-443
20. Rupp K, Birnbach U, Lundstrom J, Van PN, Soling HD (1994) Effects of CaBP2, the rat analog of ERp72, and of CaBP1 on the refolding of denatured reduced proteins. Comparison with protein disulfide isomerase. J Biol Chem 269:2501-2507
21. Ryttersgaard C, Griffith SC, Sawaya MR, MacLaren DC, Clarke S, Yeates TO (2002) Crystal structure of human L-isoaspartyl methyltransferase. J Biol Chem 277:10642-10646
22. Schiene C, Fischer G (2000) Enzymes that catalyse the restructuring of proteins. Curr Opin Struct Biol 10:40-45
23. Singh SM, Panda AK (2005) Solubilization and refolding of bacterial inclusion body proteins. J Biosci Bioeng 99:303-310
24. Sorensen HP, Mortensen KK (2005) Advanced genetic strategies for recombinant protein expression in Escherichia coli. J Biotechnol 115:113-128
25. Sun QM, Chen LL, Cao L, Fang L, Chen C, Hua ZC (2005) An improved strategy for high-level production of human vasostatin120-180. Biotechnol Prog 21:1048-1052
26. Wang T, Zhu H, Ma X, Ma Y, Wei D (2006) Structure-based stabilization of an enzyme: the case of penicillin acylase from Alcaligenes faecalis. Prot Peptide Letters 13:177-183
27. Tsumoto K, Umetsu M, Kumagai I, Ejima D, Arakawa T (2003) Solubilization of active green Xuorescent protein from insoluble particles by guanidine and arginine. Biochem Biophys Res Commun 312:1383-1386
28. Wei C, Tang B, Zhang Y, Yang K (1999) Oxidative refolding of recombinant prochymosin. Biochem J 340:345-351
29. Weibezahn J, Schlieker C, Tessarz P, Mogk A, Bukau B (2005) Novel insights into the mechanism of chaperone-assisted protein disaggregation. Biol Chem 386:739-744
30. Weir MP, Sparks J (1987) Purification and renaturation of recombinant human interleukin-2. Biochem J 245:85-91