Functional role of a non-active site residue Trp23 on the enzyme activity of Escherichia coli thioesterase I/protease I/lysophospholipase L1

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 10, 2009, Pages 1467-1473

  Lee, Li Chiun ^a   Chou, Yi Li ^b   Chen, Hong Hwa ^b   Lee, Ya Lin ^c   Shaw, Jei Fu ^a,b,d  

^a INSTITUTE OF PLANT AND MICROBIAL BIOLOGY   (Taiwan)

^b NATIONAL CHENG KUNG UNIVERSITY   (Taiwan)

^c TAIWAN AGRICULTURAL RESEARCH INSTITUTE   (Taiwan)

^d NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

Author keywords

Aromatic aromatic interaction; Enzyme kinetics; Hydrogen bond; Protein structure; Tryptophan

Indexed keywords

ALANINE; BRINASE; LYSOPHOSPHOLIPASE; LYSOPHOSPHOLIPASE L1; MUTANT PROTEIN; PHENYLALANINE; THIOESTERASE 1; THIOL ESTER HYDROLASE; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; BIOCHEMISTRY; CATALYSIS; CONTROLLED STUDY; CROSS LINKING; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ESCHERICHIA COLI; HYDROGEN BOND; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN FUNCTION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; THREE DIMENSIONAL IMAGING; TURNOVER TIME;

AMINO ACID SUBSTITUTION; BASE SEQUENCE; BINDING SITES; DNA PRIMERS; DNA, BACTERIAL; ENZYME STABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROGEN BONDING; KINETICS; LYSOPHOSPHOLIPASE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PEPTIDE HYDROLASES; PERIPLASMIC PROTEINS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; THERMODYNAMICS; THIOLESTER HYDROLASES; TRYPTOPHAN;

ESCHERICHIA COLI;

EID: 69449102331     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.06.008     Document Type: Article

References (41)

1. Pacaud M., and Uriel J. Isolation and some properties of a proteolytic enzyme from Escherichia coli (protease I). Eur. J. Biochem. 23 (1971) 435-442
2. Albright F.R., White D.A., and Lennarz W.J. Studies on enzymes involved in the catabolism of phospholipids in Escherichia coli. J. Biol. Chem. 248 (1973) 3968-3977
3. Doi O., and Nojima S. Lysophospholipase of Escherichia coli. J. Biol. Chem. 250 (1975) 5208-5214
4. Pacaud M., Sibilli L., and LeBras G. Protease I from Escherichia coli. Eur. J. Biochem. 69 (1976) 141-151
5. Karasawa K., Kudo I., Kobayashi T., Homma H., Chiba N., Mizushima H., et al. Lysophospholipase L1 from Escherichia coli K-12 overproducer. J. Biochem. 109 (1991) 288-293
6. Ichihara S., Matsubara Y., Kato C., Akasaka K., and Mizushima S. Molecular cloning, sequencing, and mapping of the gene encoding protease I and characterization of proteinase and proteinase-defective Escherichia coli mutants. J. Bacteriol. 175 (1993) 1032-1037
7. Cho H., and Cronan J.E. Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme. J. Biol. Chem. 268 (1993) 9238-9245
8. Cho H., and Cronan J.E. "Protease I" of Escherichia coli functions as a thioesterase in vivo. J. Bacteriol. 176 (1994) 1793-1795
9. Lin T.H., Chen C., Haung R.F., Lee Y.L., Shaw J.F., and Huang T.H. Multinuclear NMR resonance assignments and the secondary structure of Escherichia coli thioesterase/protease I: a member of a new subclass of lipolytic enzymes. J. Biomol. NMR 11 (1998) 363-380
10. Huang Y.T., Liaw Y.C., Gorbatyuk V.Y., and Huang T.H. Backbone dynamics of Escherichia coli thioesterase/protease I: evidence of a flexible active-site environment for a serine protease. J. Mol. Biol. 307 (2001) 1075-1090
11. Lo Y.C., Lee Y.L., Shaw J.F., and Liaw Y.C. Crystallization and preliminary X-ray crystallographic analysis of thioesterase I from Escherichia coli. Acta Crystallogr. sect. D. 56 (2000) 756-757
12. Lo Y.C., Lin S.C., Shaw J.F., and Liaw Y.C. Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic centre of SGNH-hydrolases through a conserved hydrogen bond network. J. Mol. Biol. 330 (2003) 539-551
13. 1 are governed by its switch loop movement. Biochemistry 44 (2005) 1971-1979
14. Lee L.C., Lee Y.L., Leu R.J., and Shaw J.F. Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterase I/protease I/phospholipase L1. Biochem. J. 397 (2006) 69-76
15. Tyukhtenko S.I., Litvinchuk A.V., Chang C.F., Lo Y.C., Lee S.J., Shaw J.F., Liaw Y.C., and Huang T.H. Sequential structural changes of Escherichia coli thioesterase/protease I in the serial formation of Michaelis and tetrahedral complexes with diethyl p-nitrophenyl phosphate. Biochemistry 42 (2003) 8289-8297
16. Ordentlich A., Barak D., Kronman C., Ariel N., Segall Y., Velan B., and Shafferman A. Contribution of aromatic moieties of tyrosine 133 and of the anionic subsite tryptophan 86 to catalytic efficiency and allosteric modulation of acetylcholinesterase. J. Biol. Chem. 270 (1995) 2082-2091
17. MacMillan F., Budiman K., Angerer H., and Michel H. The role of tryptophan 272 in the Paracoccus denitrificans cytochrome c oxidase. FEBS Lett. 580 (2006) 1345-1349
18. Ridder A., Skupjen P., Unterreitmeier S., and Langosch D. Tryptophan supports interaction of transmembrane helices. J. Mol. Biol. 354 (2005) 894-902
19. Stollar E.J., Gelpi J.L., Velankar S., Golovin A., Orozco M., and Luisi B.F. Unconventional interactions between water and heterocyclic nitrogens in protein structures. Proteins 57 (2004) 1-8
20. Monien B.H., Krishnasamy C., Olson S.T., and Desai U.R. Importance of tryptophan 49 of antithrombin in heparin binding and conformational activation. Biochemistry 44 (2005) 11660-11668
21. Mulky A., Sarafianos S.G., Jia Y., Arnold E., and Kappes J.C. Identification of amino acid residues in the human immunodeficiency virus type-1 reverse transcriptase tryptophan-repeat motif that are required for subunit interaction using infectious virions. J. Mol. Biol. 349 (2005) 673-684
22. Kaneda K., Sekiguchi J., and Shida T. Role of the tryptophan residue in the vicinity of the catalytic centre of exonuclease III family AP endonucleases: AP site recognition mechanism. Nucleic Acids Res. 34 (2006) 1552-1563
23. Murthy S.N., Iismaa S., Begg G., Freymann D.M., Graham R.M., and Lorand L. Conserved tryptophan in the core domain of transglutaminase is essential for catalytic activity. Proc. Natl. Acad. Sci. 99 (2002) 2738-2742
24. Kochhar S., and Dua R.D. An active centre tryptophan residue in liquefying alpha-amylase from Bacillus amyloliquefaciens. Biochem. Biophys. Res. Commun. 126 (1985) 966-973
25. Lee Y.L., Chen J.C., and Shaw J.F. The thioesterase of Escherichia coli has arylesterase activity and shows stereospecificity for protease substrates. Biochem. Biophys. Res. Commun. 231 (1997) 452-456
26. Tanksley S.D., and Orton T.T. Isozymes in Plant Genetics and Breeding, Part A (1983), Elsevier Science Publishers, East Linn 500-501
27. Blank A., Sugiyama R.H., and Dekker C. Activity staining of nucleolytic enzymes after sodium dodecyl sulfate-polyacrylamide gel electrophoresis: use of aqueous isopropanol to remove detergent from gels. Anal. Biochem. 120 (1982) 267-275
28. Wallace A.C., Laskowski R.A., and Thornton J.M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8 (1995) 127-134
29. Levitt M., and Perutz M.F. Aromatic rings act as hydrogen bond acceptors. J. Mol. Biol. 201 (1988) 751-754
30. Gervasio F.L., Chelli R., Procacci P., and Schettino V. The nature of intermolecular interactions between aromatic amino acid residues. Proteins 48 (2002) 117-125
31. Thomas K.A., Smith G.M., Thomas T.B., and Feldmann R.J. Electronic distributions within protein phenylalanine aromatic rings are reflected by the three-dimensional oxygen atom environments. Proc. Natl. Acad. Sci. 79 (1982) 4843-4847
32. Mecozzi S., West A.P., and Dougherty D.A. Cation-π interactions in aromatics of biological and medicinal interest: electrostatic potential surfaces as a useful qualitative guide. Proc. Natl. Acad. Sci. 93 (1996) 10566-10571
33. Wales T.E., and Engen J.R. Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom. Rev. 25 (2006) 158-170
34. Pal D., and Chakrabarti P. Non-hydrogen bond interactions involving the methionine sulfur atom. J. Biomol. Struct. Dyn. 19 (2001) 115-128
35. Brandl M., Weiss M.S., Jabs A., Suhnel J., and Hilgenfeld R. C-H...pi-interactions in proteins. J. Mol. Biol. 307 (2001) 357-377
36. Hunter C.A., Singh J., and Thornton J.M. Pi-pi interaction: the geometry and energetics of phenylalanine-phenylalanine interactions in proteins. J. Mol. Biol. 218 (1991) 837-846
37. Tatko C.D., and Waters M.L. Investigation of the nature of the methionine-pi interaction in beta-hairpin peptide model system. Protein Sci. 13 (2004) 2515-2522
38. Eriksson A.E., Baase W.A., Zhang X.J., Heinz D.W., Blaber M., Baldwin E.P., and Matthews B.W. Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. Science 255 (1992) 178-183
39. Lee J., Lee K., and Shin S. Theoretical studies of the response of a protein structure to cavity-creating mutations. Biophys. J. 78 (2000) 1665-1671
40. Fagain C.O. Understanding and increasing protein stability. Biochim. Biophys. Acta. 1252 (1995) 1-14
41. Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105-132