The hybrid enzymes from α-aspartyl dipeptidase and L-aspartase

Biochemical and Biophysical Research Communications

Volumn 331, Issue 1, 2005, Pages 107-112

  Sheng, Yongjie ^a   Li, Shuang ^a   Gou, Xiaojun ^a   Kong, Xiangduo ^a   Wang, Xiaoping ^a   Sun, Yanhong ^a   Zhang, Jin ^a  

^a BEIJING UNIVERSITY OF POSTS AND TELECOMMUNICATIONS   (China)

Author keywords

Gene random deletion; Hybrid enzyme; In vitro selection; l Aspartase; Aspartyl dipeptidase

Indexed keywords

ALPHA ASPARTYL DIPEPTIDASE; ASPARTATE AMMONIA LYASE; DIPEPTIDASE; HYBRID PROTEIN; MONOMER; TETRAMER; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SYNTHESIS; GENE DELETION; HYBRID; HYBRIDIZATION; IN VITRO SELECTION; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; THERMOSTABILITY; WILD TYPE;

EID: 17544377784     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.03.140     Document Type: Article

References (23)

1. K. Hakansson, A.H. Wang, and C.G. Miller The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad Proc. Natl. Acad. Sci. USA 97 2000 14097 14102
2. T.H. Carter, and C.G. Miller Aspartate-specific peptidases in Salmonella typhimurium: mutants deficient in peptidase E J. Bacteriol. 159 1984 453 459
3. C.A. Conlin, K. Hakensson, A. Liljas, and C.G. Miller Cloning and nucleotide sequence of the cyclic AMP receptor protein-regulated Salmonella typhimurium pepE gene and crystallization of its product, an alpha-aspartyl dipeptidase J. Bacteriol. 176 1994 166 172
4. C.L. James, and R.E. Viola Production and characterization of bifunctional enzymes. Substrate channeling in the aspartate pathway Biochemistry 41 2002 3726 3731
5. M.M. Jayasekera, W. Shi, G.K. Farber, and R.E. Viola Evaluation of functionally important amino acids in l-aspartate ammonia-lyase from Escherichia coli Biochemistry 36 1997 9145 9150
6. X.D. Kong, Y. Liu, X.J. Gou, S.Z. Zhu, H.Y. Zhang, X.P. Wang, and J. Zhang Directed evolution of alpha-aspartyl dipeptidase from Salmonella typhimurium Biochem. Biophys. Res. Commun. 289 2001 137 142
7. L.J. Wang, X.D. Kong, H.Y. Zhang, X.P. Wang, and J. Zhang Enhancement of the activity of l-aspartase from Escherichia coli W by directed evolution Biochem. Biophys. Res. Commun. 276 2000 346 349
8. H.Y. Zhang, Z.Q. Li, and J. Zhang Enzymatic generation of mutant libraries in vitro for random mutagenesis of the aspartase gene Chin. Sci. Bull. 37 1992 598 601
9. H.Y. Zhang, J. Zhang, L. Lin, W.Y. Du, and J. Lu Enhancement of the stability and activity of aspartase by random and site-directed mutagenesis Biochem. Biophys. Res. Commun. 192 1993 15 21
10. X.D. Kong, Z.Q. L, X.J. Gou, S.Z. Zhu, H.Y. Zhang, X.P. Wang, and J. Zhang A monomeric l-aspartase obtained by in vitro selection J. Biol. Chem. 277 2002 24289 24293
11. M. Ostermeier, J.H. Shim, and S.J. Benkovic A combinatorial approach to hybrid enzymes independent of DNA homology Nat. Biotechnol. 17 1999 1205 1209
12. S. Lutz, M. Ostermeier, G.L. Moore, C.D. Maranas, and S.J. Benkovic Creating multiple-crossover DNA libraries independent of sequence identity Proc. Natl. Acad. Sci. USA 98 2001 11248 11253
13. M. Ostermeier, A.E. Nixon, and S.J. Benkovie Incremental truncation as a strategy in the engineering of novel biocatalysts Bioorg. Med. Chem. 7 1999 2139 2144
14. S. Lutz, M. Ostermeier, and S.J. Benkovic Rapid generation of incremental truncation libraries for protein engineering using alpha-phosphothioate nucleotides Nucleic Acids. Res. 29 2001 E16
15. V. Sieber, C.A. Martinez, and F.H. Arnold Libraries of hybrid proteins from distantly related sequences Nat. Biotechnol. 19 2001 456 460
16. W.M. Coco, W.E. Levinson, M.J. Crist, H.J. Hektor, A. Darzins, P.T. Pienkos, C.H. Squires, and D.J. Monticello DNA shuffling method for generating highly recombined genes and evolved enzymes Nat. Biotechnol. 19 2001 354 359
17. H. Murakami, T. Hohsaka, and M. Sisido Random insertion and deletion of arbitrary number of bases for codon-based random mutation of DNAs Nat. Biotechnol. 20 2002 76 81
18. D. Zha, A. Eipper, and M.T. Reetz Assembly of designed oligonucleotides as an efficient method for gene recombination: a new tool in directed evolution Chem. Biochem. 4 2003 34 39
19. A. Sigh, and K. Hayashi Construction of chimeric β-glucosidases with improved enzymatic properties J. Biol. Chem. 270 1995 21928 21933
20. C.L. Tsou Conformational flexibility of enzyme active sites Science 262 1993 380 381
21. A. Fontana Rigidity of thermophilic enzymes A. Ballesteros In stability and stabilization of biocatalysts 1998 Elsevier Science Amsterdam 277 294
22. X.D. Kong, S.Z. Zhu, X.J. Gou, X.P. Wang, H.Y. Zhang, and J. Zhang A circular RNA-DNA enzyme obtained by in vitro selection Biochem. Biophys. Res. Commun. 292 2002 1111 1115
23. A. Gershenson, J.A. Schauerte, L. Giver, and F.H. Arnold Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases Biochemistry 39 2000 4658 4665