The answer would be <span>insulin-dependent diabetes mellitus.</span>
Answer:
The rate of reaction when the enzyme is saturated with substrate is the maximum rate of reaction, Vmax. ... This is usually expressed as the Km (Michaelis constant) of the enzyme, an inverse measure of affinity. For practical purposes, Km is the concentration of substrate which permits the enzyme to achieve half Vmax.
Explanation: lmk if this helps
Answer:
the answer is chloroplasts
Explanation:
Answer:
Enzyme A acts as a catalyst by lowering the activation energy the reaction needs in order to take place this would in turn lower the reaction time of the reaction lading to a faster reaction. when conditions around the enzyme change this may lead to the breaking of hydrogen bonds causing the active site to change in shape, this change would would lead to the substrate no longer being able to fit which would lower the rate of reaction.
Explanation:
Answer:
While ATP itself doesn't just generate energy from being present it for the most part does that probably seems confusing so I will clarify. ATP is a highly unstable molecule and without the assistants of anything its bonds will break. So you start with ADP once chemiosmosis is complete specifically the phosphorylation portion of it, Adenosine diphosphate because adenosine triphosphate. Basically a phosphate molecule is shoved on to ADP making ATP this last molecule is easily broken off, as I previously explained, releasing energy.
A simple explanation is what follows. When ATP loses a phosphate molecule becoming ADP energy is released.
