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n/a Ensembl n/a n/a UniProt n a n/a RefSeq (mRNA) n/a n/a RefSeq (protein) n/a n/a Location (UCSC) n/a n/a PubMed search n/a n/a Wikidata View/Edit Human Purine nucleoside phosphorylase, PNP, PNPase or inosine phosphorylase (EC 2.4.2.1) is an enzyme that in humans is encoded by the NP gene. It catalyzes the chemical reaction purine nucleoside + phosphate ⇌ {\displaystyle \rightleftharpoons ...
para-Nitrophenylphosphate (pNPP) is a non-proteinaceous chromogenic substrate for alkaline and acid phosphatases used in ELISA and conventional spectrophotometric assays. [1] Phosphatases catalyze the hydrolysis of pNPP liberating inorganic phosphate and the conjugate base of para -nitrophenol (pNP).
This ability to catalyze a reaction with a secondary substrate is known as enzyme promiscuity, [1] and may have played a role in NPP's evolutionary history. [15] NPP's promiscuity enables the enzyme to share substrates with alkaline phosphatase (AP), another member of the alkaline phosphate superfamily. Alkaline phosphatase primarily hydrolyzes ...
Each PP1 enzyme contains both a catalytic subunit and at least one regulatory subunit. [3] [4] The catalytic subunit consists of a 30-kD single-domain protein that can form complexes with other regulatory subunits. The catalytic subunit is highly conserved among all eukaryotes, thus suggesting a common catalytic mechanism. The catalytic subunit ...
The formation of 5'-phosphoribosylamine from glutamine and PRPP catalysed by PRPP amino transferase is the regulation point for purine synthesis. The enzyme is an allosteric enzyme, so it can be converted from IMP, GMP and AMP in high concentration binds the enzyme to exerts inhibition while PRPP is in large amount binds to the enzyme which ...
Polynucleotide Phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity. [2] That is, it dismantles the RNA chain starting at the 3' end and working toward the 5' end. [1] It also synthesizes long, highly heteropolymeric tails in vivo.
PNP is a key enzyme in the purine catabolic [6] pathway, and is required for purine degradation. Specifically, it catalyzes the conversion of inosine to hypoxanthine and guanosine to guanine (both guanine and hypoxanthine will be made into xanthine which will then become uric acid).
The enzyme is involved in the synthesis of nucleotides (purines and pyrimidines), cofactors NAD and NADP, and amino acids histidine and tryptophan, [1] [2] [3] linking these biosynthetic processes to the pentose phosphate pathway, from which the substrate ribose 5-phosphate is derived.