Effect of length of molecular recognition moiety on enzymatic activity switching

Journal of Bioscience and Bioengineering

Volumn 116, Issue 4, 2013, Pages 433-437

  Oshiba, Yuhei ^a   Tamaki, Takanori ^a   Ohashi, Hidenori ^a   Hirakawa, Hidehiko ^b   Yamaguchi, Satoshi ^b   Nagamune, Teruyuki ^b   Yamaguchi, Takeo ^a  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

Author keywords

Biotin PEG derivatives; Conjugation; P450cam; Poly(ethylene glycol); Site specific

Indexed keywords

ACTIVE SITE; BIOTIN-PEG; CONFORMATIONAL CHANGE; CONJUGATION; ENZYMATIC ACTIVITIES; P450CAM; SITE-SPECIFIC; THIOL GROUPS;

AMINO ACIDS; GLYCOPROTEINS;

POLYETHYLENE GLYCOLS;

3MD PROTEIN; AVIDIN; BIOTIN; CYSTEINE; MACROGOL; MUTANT PROTEIN; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CHEMICAL REACTION; CONTROLLED STUDY; DRUG CONJUGATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME MODIFICATION; ENZYME SPECIFICITY; MOLECULAR RECOGNITION; MOLECULE; MUTANT; NONHUMAN; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN EXPRESSION;

BIOTIN-PEG DERIVATIVES; CONJUGATION; P450CAM; POLY(ETHYLENE GLYCOL); SITE SPECIFIC;

AVIDIN; BIOTIN; CAMPHOR 5-MONOOXYGENASE; CATALYTIC DOMAIN; CYSTEINE; MUTAGENESIS, SITE-DIRECTED; POLYETHYLENE GLYCOLS;

EID: 84883277609     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2013.04.003     Document Type: Article

References (32)

1. Heredia K.L., Bontempo D., Ly T., Byers J.T., Halstenberg S., Maynard H.D. In situ preparation of protein - "Smart" polymer conjugates with retention of bioactivity. J.Am. Chem. Soc. 2005, 127:16955-16960.
2. Li M., De P., Gondi S.R., Sumerlin B.S. Responsive polymer-protein bioconjugates prepared by RAFT polymerization and copper-catalyzed azide-alkyne click chemistry. Macromol. Rapid Commun. 2008, 29:1172-1176.
3. De P., Li M., Gondi S.R., Sumerlin B.S. Temperature-regulated activity of responsive polymer-protein conjugates prepared by grafting-from via RAFT polymerization. J.Am. Chem. Soc. 2008, 130:11288-11289.
4. Grover G.N., Alconcel S.N.S., Matsumoto N.M., Maynard H.D. Trapping of thiol-terminated acrylate polymers with divinyl sulfone to generate well-defined semitelechelic Michael acceptor polymers. Macromolecules 2009, 42:7657-7663.
5. Lecolley F., Tao L., Mantovani G., Durkin I., Lautru S., Haddleton D. M.: a new approach to bioconjugates for proteins and peptides ("pegylation") utilising living radical polymerisation. Chem. Commun. 2004, 2026-2027.
6. So T., Ueda T., Abe Y., Nakamata T., Imoto T. Situation of monomethoxypolyethylene glycol covalently attached to lysozyme. J.Biochem. 1996, 119:1086-1093.
7. Stayton P.S., Shimoboji T., Long C., Chilkoti A., Chen G.H., Harris J.M., Hoffman A.S. Control of protein-ligand recognition using a stimuli-responsive polymer. Nature 1995, 378:472-474.
8. Salmaso S., Bersani S., Pennadam S.S., Alexander C., Caliceti P. Avidin bioconjugate with a thermoresponsive polymer for biological and pharmaceutical applications. Int. J. Pharm. 2007, 340:20-28.
9. Ziegler M., Xiao R., Penefsky H.S. Close Proximity of Cys64 and Cys140 in the δ-Subunit of Escherichia coli F1-ATPase. J.Biol. Chem. 1994, 269:4233-4239.
10. Deiters A., Cropp T.A., Mukherji M., Chin J.W., Anderson J.C., Schultz P.G. Adding amino acids with novel reactivity to the genetic code of Saccharomyces cerevisiae. J.Am. Chem. Soc. 2003, 125:11782-11783.
11. Nakata E., Koshi Y., Koga E., Katayama Y., Hamachi I. Double-modification of lectin using two distinct chemistries for fluorescent ratiometric sensing and imaging saccharides in test tube or in cell. J.Am. Chem. Soc. 2005, 127:13253-13261.
12. Abuchowski A., Mccoy J.R., Palczuk N.C., Vanes T., Davis F.F. Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase. J.Biol. Chem. 1977, 252:3582-3586.
13. Gaertner H.F., Puigserver A. J.: Increased activity and stability of poly(ethylene glycol)-modified trypsin. Enzyme Microb. Technol. 1992, 14:150-155.
14. Gauthier M.A., Klok H.A. Polymer-protein conjugates: an enzymatic activity perspective. Polym. Chem. 2010, 1:1352-1373.
15. Oshiba Y., Tamaki T., Yamaguchi S., Hirakawa H., Nagamune T., Yamaguchi T. Molecular recognition moiety and its target biomolecule interact in switching enzyme activity. J. Biosci. Bioeng. 2013, 115:639-644.
16. Busby W.F., Ackermann J.M., Crespi C.L. Effect of methanol, ethanol, dimethyl sulfoxide, and acetonitrile on in vitro activities of cDNA-expressed human cytochromes P-450. Drug Metab. Dispos. 1999, 27:246-249.
17. Furge L.L., Guengerich F.P. Cytochrome P450 enzymes in drug metabolism and chemical toxicology. Biochem. Mol. Biol. Educ. 2006, 34:66-74.
18. Veronese F.M. Peptide and protein PEGylation: a review of problems and solutions. Biomaterials 2001, 22:405-417.
19. Depp V., Alikhani A., Grammer V., Lele B.S. Native protein-initiated ATRP: a viable and potentially superior alternative to PEGylation for stabilizing biologics. Acta Biomater. 2009, 5:560-569.
20. Sevrioukova I.F., Hazzard J.T., Tollin G., Poulos T.L. Laser flash induced electron transfer in P450cam monooxygenase: putidaredoxin reductase-putidaredoxin interaction. Biochemistry 2001, 40:10592-10600.
21. Sevrioukova I.F., Garcia C., Li H.Y., Bhaskar B., Poulos T.L. Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida. J.Mol. Biol. 2003, 333:377-392.
22. Dunn A.R., Dmochowski I.J., Bilwes A.M., Gray H.B., Crane B.R. Probing the open state of cytochrome P450cam with ruthenium-linker substrates. Proc. Natl. Acad. Sci. USA 2001, 98:12420-12425.
23. Hays A.M.A., Dunn A.R., Chiu R., Gray H.B., Stout C.D., Goodin D.B. Conformational states of cytochrome P450cam revealed by trapping of synthetic molecular wires. J.Mol. Biol. 2004, 344:455-469.
24. Yao H., McCullough C.R., Costache A.D., Pullela P.K., Sem D.S. Structural evidence for a functionally relevant second camphor binding site in P450cam: Model for substrate entry into a P450 active site. Proteins: Struct. Funct. Bioinf. 2007, 69:125-138.
25. DeSantis G., Jones J.B. Chemical modification of enzymes for enhanced functionality. Curr. Opin. Biotechnol. 1999, 10:324-330.
26. Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes: I. Evidence for its hemoprotein nature. J.Biol. Chem. 1964, 239:2370-2378.
27. Gunsalus I.C., Wagner G.C. Bacterial P-450cam methylene monooxygenase components: cytochrome m, putidaredoxin, and putidaredoxin reductase. Methods Enzymol. 1978, 52:166-188.
28. Sevrioukova I.F., Poulos T.L. Putidaredoxin reductase, a new function for an old protein. J.Biol. Chem. 2002, 277:25831-25839.
29. Manna S.K., Mazumdar S. Reversible inactivation of cytochrome P450 by alkaline earth metal ions: auxiliary metal ion induced conformation change and formation of inactive P420 species in CYP101. J.Inorg. Biochem. 2008, 102:1312-1321.
30. Wells A.V., Li P.S., Champion P.M., Martinis S.A., Sligar S.G. Resonance raman investigations of Escherichia coli-Expressed Pseudomonas putida Cytochrome P450 and P420. Biochemistry 1992, 31:4384-4393.
31. Tian W.D., Wells A.V., Champion P.M., Diprimo C., Gerber N., Sligar S.G. Measurements of CO geminate recombination in cytochromes P450 and P420. J.Biol. Chem. 1995, 270:8673-8679.
32. Martinis S.A., Blanke S.R., Hager L.P., Sligar S.G., Hoa G.H.B., Rux J.J., Dawson J.H. Probing the heme iron coordination structure of pressure-induced cytochrome P420cam. Biochemistry 1996, 35:14530-14536.