Target type: molecularfunction
Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor). [GOC:jl]
Pentosyltransferase activity refers to the enzymatic transfer of a pentose sugar moiety from a donor molecule to an acceptor molecule. This process is crucial for various biological functions, including:
1. **Nucleotide biosynthesis:** Pentosyltransferases play a vital role in the synthesis of nucleotides, the building blocks of DNA and RNA. For instance, the enzyme ribose-phosphate pyrophosphokinase (PRPP synthetase) catalyzes the transfer of a ribose-5-phosphate group from ATP to a pyrophosphate molecule, producing PRPP, an essential precursor for nucleotide biosynthesis.
2. **Polysaccharide synthesis:** Pentosyltransferases participate in the synthesis of various polysaccharides, including glycosaminoglycans and certain bacterial capsular polysaccharides. These polysaccharides are important for structural integrity, cell signaling, and immune recognition.
3. **Glycoprotein and glycolipid biosynthesis:** Pentosyltransferases are involved in the addition of pentose sugars to proteins and lipids, forming glycoproteins and glycolipids, respectively. These modifications are crucial for diverse biological processes, including cell recognition, adhesion, and signal transduction.
4. **Metabolic pathways:** Pentosyltransferases play a role in various metabolic pathways, such as the pentose phosphate pathway and the nucleotide salvage pathway. These pathways are essential for maintaining cellular redox balance, providing NADPH for reductive biosynthesis, and recycling nucleotides.
5. **Drug development:** Pentosyltransferases have emerged as potential drug targets for various diseases, including cancer, viral infections, and inflammatory disorders. Inhibiting or enhancing the activity of specific pentosyltransferases could offer therapeutic benefits in these conditions.
The mechanism of pentosyltransferase activity typically involves the formation of a transient covalent intermediate between the enzyme and the donor molecule, followed by the transfer of the pentose sugar moiety to the acceptor molecule. The specificity of pentosyltransferases is determined by the structure of the active site, which recognizes and binds specific donor and acceptor molecules. Different pentosyltransferases exhibit varying degrees of substrate specificity and catalytic efficiency, reflecting their diverse roles in biological processes.'
"
Protein | Definition | Taxonomy |
---|---|---|
Thymidine phosphorylase | A thymidine phosphorylase that is encoded in the genome of Escherichia coli K-12. [OMA:P07650, PRO:DNx] | Escherichia coli K-12 |
Compound | Definition | Classes | Roles |
---|---|---|---|
thymidine | pyrimidine 2'-deoxyribonucleoside | Escherichia coli metabolite; human metabolite; metabolite; mouse metabolite | |
2',3'-dideoxythymidine | |||
6-amino-5-bromouracil | |||
5-nitro-2'-deoxyuridine | |||
5-phenyl-1,3,4-oxadiazole-2-thiol | 5-phenyl-1,3,4-oxadiazole-2-thiol: structure in first source | ||
ma-1 | tipiracil : A member of the class of pyrimidones that is uracil substituted by chloro and (2-iminopyrrolidin-1-yl)methyl groups at positions 5 and 6 respectively. Used (as the hydrochloride salt) in combination with trifluridine, a nucleoside metabolic inhibitor, for treatment of advanced/relapsed unresectable colorectal cancer. tipiracil: inhibits thymidine phosphorylase | carboxamidine; organochlorine compound; pyrimidone; pyrrolidines | antineoplastic agent; EC 2.4.2.4 (thymidine phosphorylase) inhibitor |
5-chloro-6-(1-(2-iminopyrrolidinyl) methyl)uracil hydrochloride | tipiracil hydrochloride : A hydrochloride obtained by combining tipiracil with one equivalent of hydrochloric acid. Used in combination with trifluridine, a nucleoside metabolic inhibitor, for treatment of advanced/relapsed unresectable colorectal cancer. | hydrochloride; iminium salt | antineoplastic agent; EC 2.4.2.4 (thymidine phosphorylase) inhibitor |
sesone | 7-deazaxanthine: structure in first source | ||
5'-o-tritylinosine | 5'-O-tritylinosine: structure in first source |