Significance of reduced dimensionality in reaction kinetics: Impact of multi-site particles

Chemistry and Physics of Lipids

Volumn 101, Issue 1, 1999, Pages 37-44

  Nelsestuen, Gary L ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

Author keywords

Alkaline phosphatase; Beta lactamase; Enzyme kinetics; Periplasm; Surface catalysis

Indexed keywords

ALKALINE PHOSPHATASE; BETA LACTAMASE;

CATALYSIS; CYTOPLASM; DIFFUSION; ENZYME KINETICS; NONHUMAN; PRIORITY JOURNAL; REVIEW; SURFACE PROPERTY; VELOCITY;

EID: 0032819732     PISSN: 00093084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-3084(99)00053-5     Document Type: Article

References (20)

1. Adair G.S. The hemoglobin system. VI. The oxygen dissociation curve of hemoglobin. J. Biol. Chem. 63:1925;529.
2. Ames G.F.-L. Bacterial periplasmic transport systems: structure, mechanism and evolution. Ann. Rev. Biochem. 55:1986;397-425.
3. Andree H.A.M., Contino P.B., Repke D., Gentry R., Nemerson Y. Transport rate limited catalysis on macroscopic surfaces. The activation of factor X in a continuous flow enzyme reactor. Biochemistry. 33:1994;4368-4374.
4. Berg H.C., Purcell E.M. Physics of chemoreception. Biophys. J. 20:1977;193-219.
5. Billy D., Speijer H., Willems G., Hemker H.C., Lindhout T. Prothrombin activation by prothrombinase in a tubular flow reactor. J. Biol. Chem. 270:1995;1029-1034.
6. Delisi C. Role of diffusion regulation in receptor-ligand interactions. Methods Enzymol. 93:1983;95-109.
7. Gelb M.H., Jain M.K., Hanel A.M., Berg O.G. Interfacial. enzymology. of. glycerolipid. hydrolases: lessons. from. secreted. phospholipases A2. Ann. Rev. Biochem. 64:1995;653-688.
8. Jain M.K., Gelb M.H., Rogers J., Berg O.G. Kinetic basis for interfacial catalysis by phospholipase A2. Methods Enzymol. 249:1995;567-614.
9. Land B.R., Salpeter E.E., Salpeter M.M. Kinetic parameters for acetylcholine interaction in intact junction. Proc. Natl. Acad. Sci. USA. 78:1981;7200-7204.
10. Lu Y., Nelsestuen G.L. The prothrombinase reaction: mechanism switching between Michaelis-Menten and non-Michaelis-Menten behaviors. Biochemistry. 35:1996;8201-8209.
11. Martinez, M.B., 1995. An Investigation of Enzyme Kinetics at the Diffusional Limit. Enzymes in the Periplasm of Escherichia coli. PhD Thesis, University of Minnesota.
12. Martinez M.B., Flickinger M., Nelsestuen G.L. Accurate kinetic modeling of alkaline phosphatase in the Eschericia coli periplasm: implications for enzyme properties and substrate diffusion. Biochemistry. 35:1996;1179-1186.
13. McGee M.P., Li L.C., Xiong H. Diffusion control in blood coagulation. Activation of factor X by factors IXa/VIIIa assembled on human monocyte membranes. J. Biol. Chem. 267:1992;24333-24339.
14. Monod J., Wyman J., Changeux J.-P. J. Mol. Biol. 12:1965;88.
15. Nelsestuen G.L., Martinez M.B. Steady state enzyme velocities that are independent of [Enzyme}: an important behavior in many membrane and particle bound states. Biochemistry. 36:1997;9081-9086.
16. Nikaido H., Rosenberg E.Y., Foulds J. Porin channels in Escherichia coli: studies with β-lactams in intact cells. J. Bacteriol. 153:1982;232-240.
17. Rogers M.J., Strittmatter P. Evidence for random distribution and translational movement of cytochrome b5 in endoplasmic reticulum. J. Biol. Chem. 250:1974;5713-5718.
18. Rogers M.J., Strittmatter P. The interaction of NADH-cytochrome b5 reductase and cytochrome b5 bound to egg lecithin liposomes. J. Biol. Chem. 250:1975;5713-5718.
19. Segel I.H. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady State Enzyme Systems. 1975;Wiley, New York.
20. Voet D., Voet J.G. Biochemistry. 2nd edition:1995;Wiley, New York.