Atp is a (+) allosteric effector, and ctp is a (−) allosteric effector of the enzyme atcase. both of these heterotropic effectors bind to the regulatory subunits on atcase. the substrates of atcase, aspartate and carbamoyl phosphate, bind the enzyme active site with positive cooperativity (i. e., they exert a “+” homotropic effect on activity). as the concentrations of the substrates change from values where [s]≪km to values where [s] is saturating ([s]≫km), how will the binding constants for each of the two allosteric effectors change? in other words, does atp bind atcase with higher affinity when [s] is low or high? does ctp bind atcase with higher affinity when [s] is low or high?

Iwannasay c is the most accurate

Ihope you find the answer

Answertraveling around a circular trackexplanation"traveling around a circular track" is the best answer as you could be traveling around a circular track at a constant speed. your velocity would therefore have the same magnitude but will always be constantly direction. since acceleration is the rate of change of velocity, the rate of change will only involve the direction of velocity and not the magnitude.wrong choices: "an object at rest" does not accelerate at all"increasing speed while traveling around a curve" means that the acceleration will not be constant due to only change in direction; it will be constant due to both magnitude and direction"an object in free fall" does not necessarily change direction