When.com Web Search

Search results

  1. Results From The WOW.Com Content Network
  2. Purine nucleoside phosphorylase - Wikipedia

    en.wikipedia.org/wiki/Purine_nucleoside_phosphor...

    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 ...

  3. para-Nitrophenylphosphate - Wikipedia

    en.wikipedia.org/wiki/Para-Nitrophenylphosphate

    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).

  4. Purine metabolism - Wikipedia

    en.wikipedia.org/wiki/Purine_metabolism

    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 ...

  5. Nucleotide pyrophosphatase/phosphodiesterase - Wikipedia

    en.wikipedia.org/wiki/Nucleotide_pyrophosphatase/...

    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 ...

  6. Ribose-phosphate diphosphokinase - Wikipedia

    en.wikipedia.org/wiki/Ribose-phosphate...

    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.

  7. Polynucleotide phosphorylase - Wikipedia

    en.wikipedia.org/wiki/Polynucleotide_phosphorylase

    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.

  8. Hypoxanthine-guanine phosphoribosyltransferase - Wikipedia

    en.wikipedia.org/wiki/Hypoxanthine-guanine...

    Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) is an enzyme encoded in humans by the HPRT1 gene. [1] [2] HGPRT is a transferase that catalyzes conversion of hypoxanthine to inosine monophosphate and guanine to guanosine monophosphate. This reaction transfers the 5-phosphoribosyl group from 5-phosphoribosyl 1-pyrophosphate (PRPP) to the ...

  9. Phosphoribosyl pyrophosphate - Wikipedia

    en.wikipedia.org/wiki/Phosphoribosyl_pyrophosphate

    In de novo generation of purines, the enzyme amidophosphoribosyltransferase acts upon PRPP to create phosphoribosylamine. [2] The histidine biosynthesis pathway involves the reaction between PRPP and ATP, which activates the latter to ring cleavage. Carbon atoms from ribose in PRPP form the linear chain and part of the imidazole ring in histidine.