Enhanced preference for π-bond containing substrates is correlated to Pro110 in the substrate-binding tunnel of Escherichia coli thioesterase I/protease I/lysophospholipase L1

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1774, Issue 8, 2007, Pages 959-967

  Lee, Li Chiun ^a   Liaw, Yen Chywan ^b   Lee, Ya Lin ^c   Shaw, Jei Fu ^a,d,e  

^a NATIONAL TAIWAN OCEAN UNIVERSITY   (Taiwan)

^b INSTITUTE OF MOLECULAR BIOLOGY   (Taiwan)

^c FU JEN CATHOLIC UNIVERSITY   (Taiwan)

^d INSTITUTE OF PLANT AND MICROBIAL BIOLOGY   (Taiwan)

^e NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

Author keywords

bond; Enzyme kinetics; Proline substituent; Substrate specificity; Substrate binding tunnel

Indexed keywords

AROMATIC COMPOUND; BRINASE; LEUCINE; LYSOPHOSPHOLIPASE; LYSOPHOSPHOLIPASE L1; PROLINE; THIOL ESTER HYDROLASE; THIOL ESTER HYDROLASE I; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL BOND; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION;

AMINO ACID SUBSTITUTION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; LEUCINE; LYSOPHOSPHOLIPASE; MUTATION, MISSENSE; PERIPLASMIC PROTEINS; PROLINE; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; TRIGLYCERIDES;

ESCHERICHIA COLI;

EID: 34547459487     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.05.012     Document Type: Article

References (24)

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. 1 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. 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
10. 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
11. 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
12. 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., D 56 (2000) 756-757
13. 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 center of SGNH-hydrolases through a conserved hydrogen bond network. J. Mol. Biol. 330 (2003) 539-551
14. 1 are governed by its switch loop movement. Biochemistry 44 (2005) 1971-1979
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. Lee Y.L., SU M.S., Huang T.H., and Shaw J.F. C-terminal His-tagging results in substrate specificity changes of the thioesterase I from Escherichia coli. J. Am. Oil Chem. Soc. 76 (1999) 1113-1118
17. Vallejos C.E. Enzyme activity staining. In: Tanksley S.D., and Orton T.J. (Eds). Isozymes in Plant Genetics and Breeding vol. 1A (1983), Elsevier B.V., Amsterdam 496-516
18. 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
19. Tiss A., Carriere F., and Verger R. Effects of gum Arabic on lipase interfacial binding and activity. Anal. Biochem. 294 (2001) 36-43
20. Kishimoto T., Soda Y., Matsuyama Y., and Mizuno K. An enzymatic assay for lysophosphatidylcholine concentration in human serum and plasma. Clin. Biochem. 35 (2002) 411-416
21. Schneider T.R. A genetic algorithm for the identification of conformationally invariant regions in protein molecules. Acta Crystallogr., D 58 (2002) 195-208
22. Bhattacharyya R., and Chakrabarti P. Stereospecific interactions of proline residues in protein structures and complexes. J. Mol. Biol. 331 (2003) 925-940
23. 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
24. Yuan Z., Bailey T.L., and Teasdale R.D. Prediction of protein B-factor profiles. Proteins 58 (2005) 905-1012