Kinetics and Mechanism of a Reaction Catalyzed by PST-01 Protease from Pseudomonas aeruginosa PST-01

Biotechnology and Bioengineering

Volumn 86, Issue 3, 2004, Pages 365-373

  Bobe, Lulian M ^a   Abdelmoez, Wael ^a   Ogino, Hiroyasu ^a   Yasuda, Masahiro ^a   Ishimi, Kosaku ^a   Ishikawa, Haruo ^a  

^a Osaka Prefecture University   (Japan)

Author keywords

Enzyme kinetics; Initial reaction rate; Organic solvent stable enzyme; Peptide synthesis; PST 01 protease

Indexed keywords

BIOMEDICAL ENGINEERING; HYDROLYSIS; REACTION KINETICS; SUBSTRATES; SYNTHESIS (CHEMICAL);

BUFFER SOLUTIONS; HYDROLYTIC REACTION;

BIOTECHNOLOGY;

AMIDE; AMINO ACID DERIVATIVE; CARBOXYBENZOYLALANINE; CARBOXYBENZOYLALANYLLEUCINAMINE; DIMETHYL SULFOXIDE; LEUCINE; PROTEINASE; UNCLASSIFIED DRUG;

AQUEOUS SOLUTION; ARTICLE; CONCENTRATION RESPONSE; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SUBSTRATE; HYDROLYSIS; NONHUMAN; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS AERUGINOSA PST 01;

CATALYSIS; CHROMATOGRAPHY, GEL; DIPEPTIDES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOPEPTIDASES; HYDROLYSIS; KINETICS; MOLECULAR WEIGHT; PSEUDOMONAS AERUGINOSA; SOLVENTS; SUBSTRATE SPECIFICITY;

PSEUDOMONAS; PSEUDOMONAS AERUGINOSA;

EID: 2342419734     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.20052     Document Type: Article

References (29)

1. Deschrevel B, Vincent J, Thellier M. 1993. Kinetic study of the chymotrypsin-catalyzed hydrolysis and synthesis of a peptide bond in a monophasic aqueous/organic reaction medium. Arch Biochem Biophys 304:45-52.
2. Ferdinand W. 1966. The interpretation of non-hyperbolic rate curve for two-substrate enzymes. A possible mechanism for phosphofructokinase. Biochem J 98:278-283.
3. Froom HJ. 1975. Initial rate enzyme kinetics. New York: Springer-Verlag. p 149-150.
4. Gaertner H, Puigserver A. 1989. Kinetics and specificity of serine proteases in peptide synthesis catalyzed in organic solvents. Eur J Biochem 181:207-213.
5. Inouye K, Watanabe K, Morihara K, Tochino K, Kanaya T, Emura J, Sakakibara S. 1979. Enzyme-assisted semisynthesis of human insulin. J Am Chem Soc 101:751-752.
6. Ishikawa H, Maeda T, Hikita H, Miyatake K. 1988. The computerized derivation of rate equations for enzyme reactions on the basis of the pseudo-steady-state assumption and the rapid equilibrium assumption. Biochem J 251:175-181.
7. Isowa Y, Ohmori M, Ichikawa T, Mori K, Nonaka Y, Kihara K, Oyama K, Satoh H, Nishimura S. 1979. The thermolysin-catalyzed condensation reactions of N-substituted aspartic and glutamic acids with phenylalanine alkyl esters. Tetrahedron Lett 28:2611-2612.
8. Jakubke HD, Kuhl P, Konnecke A. 1985. Basic principles of protease-catalyzed peptide bond formation. Angew Chem Int Ed Engl 24:85-93.
9. Khmelnitsky YL, Levashov AV, Klyachko NL, Martinek K. 1988. Engineering biocatalytic systems in organic media with low water content. Enzyme Microb Technol 10:710-724.
10. Klibanov AM. 1986. Enzymes that work in organic solvents. CHEMTECH 16:354-359.
11. Kullmann W. 1980. Proteases as catalysts of enzymic synthesis of opioid peptides. J Biol Chem 255:8234-8238.
12. Kunugi S, Yoshida M. 1996. Kinetics of a thermolysin-catalyzed peptide formation in acetonitrile-water. Bull Chem Soc Jpn 69:805-809.
13. Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage. Nature (London) 227:680-685.
14. Lee SB. 1995. Enzyme reaction kinetics in organic solvents: a theoretical kinetic model and comparison with experimental observations. J Ferment Bioeng 79:479-484.
15. Nakanishi K, Kimura Y, Matsuno R. 1986. Kinetics and equilibrium of enzymatic synthesis of peptides in aqueous/organic biphasic systems. Thermolysin-catalyzed synthesis of N-(benzyloxycarbonyl)-L-aspartyl-L-phenylalanine methyl esters. Eur J Biochem 161:541-549.
16. Nakanishi K, Matsuno R. 1986. Kinetics of enzymatic synthesis of peptides in aqueous/organic biphasic systems. Thermolysin-catalyzed synthesis of N-(benzyloxycarbonyl)-L-phenylalanyl-L-phenylalanine methyl esters. Eur J Biochem 161:533-540.
17. Ogino H, Yasui K, Shiotani T, Ishihara T, Ishikawa H. 1995. Organic solvent-tolerant bacterium which secrets an organic solvent-stable proteolytic enzyme. Appl Environ Microbiol 61:4258-4262.
18. Ogino H, Yamada M, Watanabe F, Ichinose H, Yasuda M, Ishikawa H. 1999a. Peptide synthesis catalyzed by organic solvent-stable protease from Pseudomonas aeruginosa PST-01 in monophasic aqueous-organic solvent systems. J Biosci Bioeng 88:513-518.
19. Ogino H, Watanabe F, Yamada M, Nakagawa S, Hirose T, Noguchi A, Yasuda M, Ishikawa H. 1999b. Purification and characterization of organic solvent-stable protease from organic solvent-tolerant Pseudomonas aeruginosa PST-01. J Biosci Bioeng 87:61-68.
20. Ogino H, Gemba Y, Yamada M, Shizuka M, Yasuda M, Ishikawa H. 2000. The synthetic rate of dipeptide catalyzed by organic solvent-stable protease from Pseudomonas aeruginosa PST-01 in the presence of water-soluble organic solvents. Biochem Eng J 5:219-223.
21. Ogino H, Ishikawa H. 2001. Enzymes which are stable in the presence of organic solvents. J Biosci Bioeng 91:109-116.
22. Oka T, Morihara K. 1978. Peptide bond synthesis catalyzed by α-chymotrypsin. J Biochem 84:1277-1283.
23. Riechmann L, Kasche V. 1986. Reaction mechanism, specificity and pH-dependence of peptide synthesis catalyzed by the metalloproteinase thermolysin. Biochim Biophys Acta 872:269-276.
24. 2. Biocatal Biotransform 17:417-429.
25. Schwartz A, Wandrey C, Steinke D, Kula MR. 1992. A two-step enzymatic synthesis of dipeptides. Biotechnol Bioeng 39:132-140.
26. Segel IH. 1993. Enzyme kinetics: behavior and analysis of rapid equilibrium and steady-state enzyme systems. New York: John Wiley & Sons, Inc. p 657-659.
27. Tsuzuki H, Oka T, Morihara K. 1980 Coupling between Cbz-Arg-OH and Leu-X catalyzed by trypsin and papain. J Biochem 88:669-675.
28. Wayne SI, Fruton JS. 1983. Thermolysin-catalyzed peptide bond synthesis. Proc Natl Acad Sci USA 80:3241-3244.
29. Wolff EC, Shirmer EW, Folk JE. 1962. The kinetics of carboxypeptidase B activity I. Kinetic parameters. J Biol Chem 237:3094-3099.