Properties of the N,N'-dicyclohexylcarbodiimide resistant ATPase of Streptococcus cremoris.
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.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D002234:Carbodiimides / Q000494:pharmacology*; D002412:Cations; D002462:Cell Membrane / Q000201:enzymology; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology*; D007700:Kinetics; D013291:Streptococcus / Q000201:enzymology*; D013816:Thermodynamics
D002234:Carbodiimides; D002412:Cations; D004024:Dicyclohexylcarbodiimide; D000251:Adenosine Triphosphatases