PMID: 2957254Jan 1, 1987

Properties of the N,N'-dicyclohexylcarbodiimide resistant ATPase of Streptococcus cremoris

The International Journal of Biochemistry
M A Rimpiläinen

Abstract

1. The specific activity of the membrane-bound ATPase of Streptococcus cremoris HA was 1.30 mumol Pi/mg protein/min. 2. Km for ATP as substrate was 0.8 mM. 3. The pH optimum was 8.0 at +37 degrees C. 4. The ATPase was maximally activated with Mg2+/ATP molar ratio of 1:2. 5. Cations activated the enzyme in order: Mg2+ greater than Co2+ greater than Mn2+ greater than Zn2+ greater than Ca2+ greater than K+ greater than Na+. 6. The enzyme was inhibited by oligomycin (27-77%), sodium azide (13-33%) and ouabain (15-22%). N,N'-dicyclohexylcarbodiimide had no effect on the enzyme activity.

References

Jan 1, 1979·Annual Review of Biochemistry·J A DownieG B Cox
Apr 1, 1976·Journal of General Microbiology·T W Ritchey, H W Seely
Nov 25, 1970·Biochemical and Biophysical Research Communications·A Abrams, C Baron
Dec 1, 1982·European Journal of Biochemistry·S F BiketovV L Tsuprun
Sep 1, 1983·Antonie van Leeuwenhoek·W N Konings, R Otto

Citations

Jan 1, 1988·The International Journal of Biochemistry·M A RimpiläinenR I Forsén
Mar 15, 2005·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·Prislaine P MagalhãesPietro Ciancaglini

Related Concepts

DNA-dependent ATPase
Carbodiimides
Cations
Plasma Membrane
Dicyclohexylcarbodiimide
Streptococcus
Thermodynamics

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