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Limited proteolysis as a structural probe of the soluble alpha-glycerophosphate oxidase from Streptococcus sp.
Charrier V, Luba J, Parsonage D, Claiborne A. Charrier V, et al. Among authors: parsonage d. Biochemistry. 2000 May 2;39(17):5035-44. doi: 10.1021/bi992499j. Biochemistry. 2000. PMID: 10819968
As reported previously [Parsonage, D., Luba, J., Mallett, T. C., and Claiborne, A. (1998) J. Biol. Chem. 273, 23812-23822], the flavoprotein alpha-glycerophosphate oxidases (GlpOs) from a number of enterococcal and streptococcal sources contain a conserved 50-52 res …
As reported previously [Parsonage, D., Luba, J., Mallett, T. C., and Claiborne, A. (1998) J. Biol. Chem. 273, 23812-23822], th …
Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron-reduced enzyme forms.
Crane EJ 3rd, Parsonage D, Poole LB, Claiborne A. Crane EJ 3rd, et al. Among authors: parsonage d. Biochemistry. 1995 Oct 31;34(43):14114-24. doi: 10.1021/bi00043a016. Biochemistry. 1995. PMID: 7578008
The combined rapid-reaction and steady-state data are best accommodated by a limiting type of ternary complex mechanism very similar to that proposed previously [Parsonage, D., Miller, H., Ross, R.P., & Claiborne, A. (1993) J. Biol. Chem. 268, 3161-3167]....
The combined rapid-reaction and steady-state data are best accommodated by a limiting type of ternary complex mechanism very similar to that …
75 results