2024年4月11日发(作者：)

代谢物与ogt催化结构域结合

英文回答：

The catalytic domain of OGT (O-linked N-

acetylglucosamine transferase) interacts with several

metabolites, including UDP-GlcNAc (uridine diphosphate N-

acetylglucosamine), the sugar donor substrate for O-GlcNAc

transfer, and acetyl-CoA (acetyl coenzyme A), the cofactor

for O-GlcNAc modification. These metabolites bind to

specific sites on the OGT catalytic domain and are

essential for its enzymatic activity.

UDP-GlcNAc binds to a highly conserved cleft in the OGT

catalytic domain, which is formed by residues from both the

Rossmann-like and the catalytic domains. The binding of

UDP-GlcNAc induces conformational changes in the OGT

catalytic domain, which are necessary for the transfer of

GlcNAc to the protein substrate.

Acetyl-CoA binds to a distinct site on the OGT

catalytic domain, which is located near the active site.

The binding of acetyl-CoA is essential for the transfer of

the acetyl group to the GlcNAc residue on the protein

substrate.

In addition to UDP-GlcNAc and acetyl-CoA, the OGT

catalytic domain can also interact with other metabolites,

such as NAD+ (nicotinamide adenine dinucleotide) and ATP

(adenosine triphosphate). These metabolites may modulate

the activity of OGT or play a role in its regulation.

中文回答：

OGT（O-连接的N-乙酰葡萄糖胺转移酶）催化结构域与多种代

谢物结合，包括UDP-GlcNAc（尿苷二磷酸N-乙酰葡萄糖胺），O-

GlcNAc转移的糖供体底物，和乙酰辅酶A（辅酶A），O-GlcNAc修

饰的辅因子。这些代谢物与OGT催化结构域上的特定位点结合，是

OGT酶活性的必需品。

UDP-GlcNAc与OGT催化结构域中的一个高度保守的裂隙结合，

该裂隙由Rossmann样结构域和催化结构域的残基形成。UDP-GlcNAc

的结合诱导OGT催化结构域构象变化，这是将GlcNAc转移到蛋白质

底物所必需的。

乙酰辅酶A与OGT催化结构域上的一个不同位点结合，该位点

位于活性位点附近。乙酰辅酶A的结合对于将乙酰基转移到蛋白质

底物上的GlcNAc残基至关重要。

除了UDP-GlcNAc和乙酰辅酶A之外，OGT催化结构域还可以与

其他代谢物相互作用，例如NAD+（烟酰胺腺嘌呤二核苷酸）和ATP

（三磷酸腺苷）。这些代谢物可以调节OGT的活性或在调节OGT中

发挥作用。