Insulin causes decrease in activity’ of which enzyme-
Insulin promotes glucose uptake in muscle and adipose tissue by increasing the translocation of GLUT4 transporters. But the question is about enzymes. So, maybe it's about enzymes involved in glycogen synthesis or breakdown. Insulin inhibits gluconeogenesis and glycogenolysis, right? That means enzymes involved in breaking down glycogen or producing glucose would be affected.
Wait, glycogen phosphorylase is the enzyme that breaks down glycogen into glucose-1-phosphate. In the liver, when insulin is present, it would decrease the activity of glycogen phosphorylase to prevent the breakdown of glycogen, thereby lowering blood glucose. So insulin inhibits glycogen phosphorylase. That makes sense because when insulin is active, the body is in an anabolic state, storing glucose as glycogen, not breaking it down.
Let me check the options. The correct answer here is probably glycogen phosphorylase. The other options might be enzymes that insulin actually activates. For example, insulin activates glycogen synthase to promote glycogen synthesis. So if the options included glycogen synthase, that's not the answer. Another enzyme could be hormone-sensitive lipase, which is inhibited by insulin to prevent lipolysis. But the question is about enzymes in the context of glucose metabolism, so maybe the answer is glycogen phosphorylase.
So the core concept is insulin's role in regulating glucose metabolism by inhibiting glycogen breakdown. The correct answer is glycogen phosphorylase. The other options would be enzymes that insulin activates or that are unrelated. For example, if an option was glucokinase, that's activated by insulin. Or if it was protein kinase B, which is part of the insulin signaling pathway. So the incorrect options would be enzymes that insulin activates or those not directly related to glycogen breakdown.
**Core Concept**
Insulin regulates glucose homeostasis by modulating enzymes involved in glycogen metabolism. It inhibits glycogen phosphorylase to suppress glycogenolysis in the liver, reducing blood glucose levels during the fed state.
**Why the Correct Answer is Right**
Insulin decreases glycogen phosphorylase activity via activation of the PI3K/Akt pathway. This enzyme catalyzes the rate-limiting step in glycogenolysis by cleaving glucose from glycogen. By inhibiting it, insulin prevents excessive glucose release into the bloodstream, aligning with its anabolic role postprandially.
**Why Each Wrong Option is Incorrect**
**Option A:** *Glycogen synthase* is activated by insulin, promoting glycogen synthesis.
**Option B:** *Hepatic glucokinase* is upregulated by insulin, enhancing glucose phosphorylation and storage.
**Option C:** *Protein kinase B (Akt)* is activated by insulin signaling, not inhibited.
**Clinical Pearl / High-Yield Fact**
Remember "insulin = anabolic brake on catabolism": it inhibits glycogen phosphorylase (glycogenolysis), hormone-sensitive lipase (lipolysis), and gluconeogenic enzymes. Always correlate enzyme function with insulin’s metabolic effects.
**Correct