Structure and Function of PAPOLG: A Key Enzyme in DNA and RNA Biosynthesis

Target Name: PAPOLG

NCBI ID: G64895

Structure and Function of PAPOLG: A Key Enzyme in DNA and RNA Biosynthesis

Polynucleotide adenylyltransferase gamma (PAPOLG) is a enzyme that plays a crucial role in the biosynthesis of DNA and RNA in all living organisms. PAPOLG is a member of the nucleotide transporter family 1 (Ntap) and is responsible for transporting the nucleotides GDP, GTP, and CTP from the cytoplasm to the nuclear envelope and vice versa.

PAPOLG is a key enzyme in the cell division cycle and is involved in the regulation of DNA replication, transcription, and repair. It is a protein that consists of 256 amino acids and has a calculated molecular mass of 31 kDa. PAPOLG has a unique structure that consists of a catalytic domain and a nucleotide-binding domain.

The catalytic domain of PAPOLG is the active site where the enzyme carries out its catalytic activity. It consists of a Rossmann-fold, a parallel beta-sheet, and a transmembrane region. The Rossmann-fold is the core of the catalytic domain and is responsible for the binding of nucleotides. The parallel beta-sheet is responsible for the overall structural stability of the domain and is involved in the coordination of the Rossmann-fold. The transmembrane region is responsible for the stability of the enzyme and is involved in the regulation of its activity.

The nucleotide-binding domain of PAPOLG is responsible for the binding of nucleotides to the enzyme. It consists of a nucleotide-binding region and a region responsible for the interaction with the catalytic domain. The nucleotide-binding region consists of a nucleotide-binding loop and a region that is involved in the interaction with the catalytic domain. The interaction between the nucleotide-binding region and the catalytic domain is responsible for the regulation of the activity of the enzyme.

PAPOLG is involved in the biosynthesis of DNA and RNA in all living organisms. It is a key enzyme in the cell division cycle and is involved in the regulation of DNA replication, transcription, and repair. It is a protein that consists of 256 amino acids and has a calculated molecular mass of 31 kDa. PAPOLG has a unique structure that consists of a catalytic domain and a nucleotide-binding domain. The catalytic domain of PAPOLG is the active site where the enzyme carries out its catalytic activity, while the nucleotide-binding domain is responsible for the binding of nucleotides to the enzyme.

PAPOLG is a potential drug target and may be a biomarker for various diseases. For instance, PAPOLG has been shown to be involved in the development and progression of various types of cancer, including breast, ovarian, and colorectal cancer. Studies have also shown that PAPOLG is involved in the regulation of cell growth and that its levels are regulated in various types of cancer.

In addition to its potential as a drug target, PAPOLG is also a potential biomarker for various diseases. For instance, PAPOLG has been shown to be involved in the diagnosis of neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease. Studies have also shown that PAPOLG is involved in the regulation of inflammation and that its levels are regulated in various types of inflammatory diseases.

Overall, PAPOLG is a complex enzyme that plays a crucial role in the biosynthesis of DNA and RNA in all living organisms. Its unique structure and its involvement in the cell division cycle make it a potential drug target and a valuable biomarker for various diseases. Further research is needed to fully understand the role of PAPOLG in

Protein Name: Poly(A) Polymerase Gamma

Functions: Responsible for the post-transcriptional adenylation of the 3'-terminal of mRNA precursors and several small RNAs including signal recognition particle (SRP) RNA, nuclear 7SK RNA, U2 small nuclear RNA, and ribosomal 5S RNA

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