γ-Glutamyl transpeptidase from Bacillus pumilus KS 12: Decoupling autoprocessing from catalysis and molecular characterization of N-terminal region

Enzyme and Microbial Technology

Volumn 50, Issue 3, 2012, Pages 159-164

  Murty, N Apurva Ratan ^a   Tiwary, Ekta ^a   Sharma, Richa ^a   Nair, Neha ^a   Gupta, Rani ^a  

^a UNIVERSITY OF DELHI   (India)

Author keywords

Bacillus pumilus KS 12; Chaperone; Decoupling; Gamma glutamyl transpeptidase; N terminal truncation

Indexed keywords

BACILLUS PUMILUS; CHAPERONE; DECOUPLING; GAMMA GLUTAMYL TRANSPEPTIDASE; N-TERMINAL TRUNCATION;

AFFINITY CHROMATOGRAPHY; BACILLI; BACTERIOLOGY; CLONING; ESCHERICHIA COLI; PH EFFECTS;

ENZYME ACTIVITY;

BACTERIAL ENZYME; GAMMA GLUTAMYLTRANSFERASE;

AFFINITY CHROMATOGRAPHY; ARTICLE; BACILLUS LICHENIFORMIS; BACILLUS PUMILUS; CATALYSIS; CONTROLLED STUDY; DECOUPLING AUTOPROCESSING; ENZYME ACTIVITY; ENZYME MECHANISM; ESCHERICHIA COLI; MOLECULAR WEIGHT; NONHUMAN; SEQUENCE ANALYSIS; THERMOSTABILITY;

AMINO ACID SEQUENCE; BACILLUS; BIOTECHNOLOGY; CATALYSIS; CHROMATOGRAPHY, AFFINITY; CLONING, MOLECULAR; DIMERIZATION; ESCHERICHIA COLI; GAMMA-GLUTAMYLTRANSFERASE; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA;

BACILLUS LICHENIFORMIS; BACILLUS PUMILUS;

EID: 84856505571     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2011.08.005     Document Type: Article

References (27)

1. Suzuki H., Yamada C., Kato K. Gamma-glutamyl compounds and their enzymatic production using bacterial gamma-glutamyltranspeptidase. Amino Acid 2007, 32:333-340.
2. Gong M., How B. Prominent role of γ-glutamyl-transpeptidase on the growth of Helicobacter pylori. World J Gastroenterol 2004, 10:2994-2996.
3. McGovern K.J., Blanchard T.G., Gutierrez J.A., Czinn S.J., Krakowka S., Youngman P. γ-Glutamyltransferase is a Helicobacter pylori virulence factor but is not essential for colonization. Infect Immun 2001, 69:4168-4173.
4. Boanca G., Sand A., Barycki J.J. Uncoupling the enzymatic and autoprocessing activities of Helicobacter pylori γ-glutamyltranspeptidase. J Biol Chem 2006, 281:19029-19037.
5. Yao Y.F., Weng Y.M., Hu H.Y., Ku K.L., Lin L.L. Expression optimization and biochemical characterization of a recombinant gamma-glutamyltranspeptidase from Escherichia coli novablue. J Protein Chem 2006, 25:431-441.
6. Kimura K., Tran L.S.P., Uchida I., Itoh Y. Characterization of Bacillus subtilis - γ-glutamyltransferase and its involvement in the degradation of capsule poly-c-glutamate. Microbiology 2004, 150:4115-4123.
7. Lin L.L., Chou P.R., Hua Y.W., Hsu W.H. Overexpression, one-step purification and biochemical characterization of a recombinant γ-glutamyltranspeptidase from Bacillus licheniformis. Appl Microbiol Biotechnol 2006, 73:103-112.
8. Castellano I., Merlino A., Rossi M., Cara F.L. Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: an enzyme specialized in hydrolase activity. Biochemie 2010, 92:464-474.
9. Castellano I., Salle A.D., Merlino A., Rossi M., Cara F.L. Gene, gene cloning and protein expression of γ-glutamyl transpeptidases from Thermus thermophilus and Deinococcus radiodurans: comparison of molecular and structural properties with mesophilic counterparts. Extremophiles 2011, 15:259-270.
10. Altschul S.F., Gish W., Miller W., Myers E.W., Lipman D.J. Basic local alignment search tool. J Mol Biol 1990, 215:403-410.
11. Gasteiger J.E., Gattiker A., Hoogland C., Ivanyi I., Appel D., Bairoch A. ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res 2003, 31:3784-3788.
12. Bendtsen D., Nielsen H., Von Heijne G., Brunak S. Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 2004, 340:783-795.
13. Corpet F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res 1998, 16:10881-11089.
14. Gouet P., Courcelle E., Stuart D.I., Metoz F. ESPript: multiple sequence alignments in PostScript. Bioinformatics 1998, 15:305-308.
15. Tiwary E., Gupta R. Subtilisin-γ-glutamyl transpeptidase: a novel combination as ungual enhancer for prospective topical application. J Pharm Sci 2010, 99:4866-4873.
16. Hsu W.H., Ong P.L., Chen S.C., Lin L.L. Contribution of Ser463 residue to the enzymatic and autoprocessing activity of Escherichia coli γ-glutamyl transpeptidase. Indian J Biochem Biophys 2009, 46:281-288.
17. Okada T., Suzuki H., Wada K., Kumagai H., Fukuyama K. Crystal structures of coli γ-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate. Proc Natl Acad Sci 2006, 103:6471-6476.
18. Ong P.L., Yao Y.F., Weng Y.H., Hsu W.H., Lin L.L. Residues Arg114 and Arg337 are critical for the proper function of Escherichia coli γ-glutamyltranspeptidase. Biochem Biophys Res Commun 2008, 366:294-300.
19. Okada T., Suzuki H., Wada K., Kumagai H., Fukuyama K. Crystal structure of the γ-glutamyltranspeptidase precursor protein from Escherichia coli: structural changes upon autocatalytic processing and implications for the maturation mechanism. J Biol Chem 2007, 282:2433-2439.
20. Morrow A.L., Williams K., Sand A., Boanca G., Barycki J.J. Characterization of Helicobacter pylori γ-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis. J Biol Chem 2007, 282:534-541.
21. Wada K., Irie M., Suzuki H., Fukuyama K. Crystal structure of the halotolerant γ-glutamyltranspeptidase from Bacillus subtilis in complex with glutamate reveals a unique architecture of the solvent-exposed catalytic pocket. FEBS J 2010, 277:1000-1009.
22. Lin L.L., Yang L.Y., Hu H.Y., Lo H.F. Influence of N-terminal truncations on the functional expression of Bacillus licheniformis γ-glutamyltranspeptidase in recombinant Escherichia coli. Curr Microbiol 2008, 57:603-608.
23. Moallic C., Dabonne S., Colas B., Sine J.P. Identification and characterization of a gamma-glutamyl transpeptidase from a thermo-alcalophile strain of Bacillus pumilus. Protein J 2006, 25:391-397.
24. Suzuki H., Kumagai H., Tochikura T. γ-Glutamyltranspeptidase from Escherichia coli K-12: formation and localization. J Bacteriol 1986, 168:1332-1335.
25. Chang H.P., Liang W.C., Lyu R.C., Chi M.C., Wang T.F., Su K.L., et al. Effects of C terminal truncation on autocatalytic processing of Bacillus licheniformis γ-glutamyl transpeptidase. Biochemistry 2010, 75:919-929.
26. Duggleby H.J., Tolley S.P., Hill C.P., Dodson E.J., Dodson G., Moody P.C. Penicillin acylase has a single-amino-acid catalytic centre. Nature 1995, 373:264-268.
27. Oinonen C., Tikkanen R., Rouvinen J., Peltonen L. Three-dimensional structure of human lysosomal aspartylglucosaminidase. Nat Struct Biol 1995, 2:1102-1108.