^Leslie NR, McLennan AG, Safrany ST (July 2002). "Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases". BMC Biochemistry. 3: 20. doi:10.1186/1471-2091-3-20. PMC117780. PMID 12121577.
^Safrany ST, Ingram SW, Cartwright JL, Falck JR, McLennan AG, Barnes LD, Shears SB (July 1999). "The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein". The Journal of Biological Chemistry. 274 (31): 21735–40. doi:10.1074/jbc.274.31.21735. PMID 10419486.
External linksedit
Diadenosine+hexaphosphate+hydrolase+(AMP-forming) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
diadenosine, hexaphosphate, hydrolase, forming, haps1, nudt11, gene, haps2, nudt10, gene, enzyme, with, systematic, name, adenosyl, hexaphosphate, nucleotidohydrolase, forming, this, enzyme, catalyses, following, chemical, reactionidentifiersec, 60databasesint. Diadenosine hexaphosphate hydrolase AMP forming EC 3 6 1 60 hAps1 NUDT11 gene hAps2 NUDT10 gene is an enzyme with systematic name P1 P6 bis 5 adenosyl hexaphosphate nucleotidohydrolase AMP forming 1 2 This enzyme catalyses the following chemical reactionDiadenosine hexaphosphate hydrolase AMP forming IdentifiersEC no 3 6 1 60DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins 1 P1 P6 bis 5 adenosyl hexaphosphate H2O displaystyle rightleftharpoons adenosine 5 pentaphosphate AMP 2 P1 P5 bis 5 adenosyl pentaphosphate H2O displaystyle rightleftharpoons adenosine 5 tetraphosphate AMPA divalent cation is essential for activity References edit Leslie NR McLennan AG Safrany ST July 2002 Cloning and characterisation of hAps1 and hAps2 human diadenosine polyphosphate metabolising Nudix hydrolases BMC Biochemistry 3 20 doi 10 1186 1471 2091 3 20 PMC 117780 PMID 12121577 Safrany ST Ingram SW Cartwright JL Falck JR McLennan AG Barnes LD Shears SB July 1999 The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase Overlapping substrate specificities in a MutT type protein The Journal of Biological Chemistry 274 31 21735 40 doi 10 1074 jbc 274 31 21735 PMID 10419486 External links editDiadenosine hexaphosphate hydrolase AMP forming at the U S National Library of Medicine Medical Subject Headings MeSH Portal nbsp Biology Retrieved from https en wikipedia org w index php title Diadenosine hexaphosphate hydrolase AMP forming amp oldid 1188090319, wikipedia, wiki, book, books, library,
