XMP 5'-nucleosidase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: 5'XMP + H20 = phosphate + xanthosine. [PMID:34824243, RHEA:28530]

XMP 5'-nucleosidase is an enzyme that catalyzes the hydrolysis of XMP (xanthosine 5'-monophosphate) to xanthine and ribose 5-phosphate. This reaction is part of the purine nucleotide salvage pathway, which recycles purine bases from degraded nucleic acids. XMP 5'-nucleosidase plays a vital role in maintaining the cellular pool of purine nucleotides, which are essential building blocks for DNA and RNA synthesis. The enzyme exhibits high specificity for XMP, efficiently hydrolyzing it while displaying negligible activity towards other purine nucleotides such as AMP (adenosine 5'-monophosphate) or GMP (guanosine 5'-monophosphate). The catalytic mechanism of XMP 5'-nucleosidase involves a two-step process: 1) Binding of XMP to the active site of the enzyme. 2) Hydrolysis of the glycosidic bond between the ribose and xanthine moieties, leading to the release of xanthine and ribose 5-phosphate. The enzyme's activity is influenced by various factors including pH, temperature, and the presence of metal ions. Notably, XMP 5'-nucleosidase is also involved in the catabolism of purine nucleotides, contributing to the degradation of these molecules in certain biological pathways.'
"

Proteins (1)

Compounds (16)