Differential binding of NAD+ to acyl glyceraldehyde-3-phosphate dehydrogenase and its role in the acyl group transfer reaction.

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dc.contributor.authorMalhotra, O Pen_US
dc.date.accessioned1991-08-01en_US
dc.date.accessioned2009-05-27T09:11:29Z
dc.date.available1991-08-01en_US
dc.date.available2009-05-27T09:11:29Z
dc.date.issued1991-08-01en_US
dc.description.abstractEnzyme protein fluorescence of di-furylacryloyl-glyceraldehyde-3-phosphate dehydrogenase (di-FA-GPDH:lambda max.excitation 290 nm, lambda max.emission 338 nm) is quenched about 28% on saturation with NAD+. Results of fluorometric titration of di-FA-GPDH with NAD+ suggest the presence of two tight and two loose coenzyme binding sites (Kdiss. 0.1 and 6.0 microM, respectively). Initial rates of the NAD(+)-dependent reaction of di-FA-GPDH with arsenate and phosphate and of mono-FA-GPDH with phosphate have been determined at varying coenzyme concentrations. The data suggest that binding of NAD+ at the tight sites does not activate the acyl group for its reaction with the acceptor (phosphate or arsenate). The group transfer reaction is dependent only on NAD+ binding to the loose sites, which carry the acyl group. The large difference in the NAD+ binding affinity to the two types of sites and their different effects on the group transfer reaction impart a sigmoidal shape to the rate versus [NAD+] plots. The sigmoidicity is abolished if the reactive SH groups at the unacylated sites are blocked by carboxymethylation.en_US
dc.description.affiliationDepartment of Chemistry, Banaras Hindu University, Varanasi.en_US
dc.identifier.citationMalhotra OP. Differential binding of NAD+ to acyl glyceraldehyde-3-phosphate dehydrogenase and its role in the acyl group transfer reaction. Indian Journal of Biochemistry & Biophysics. 1991 Aug; 28(4): 257-62en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/26743
dc.language.isoengen_US
dc.source.urihttps://https://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijbb/ijbb0.aspen_US
dc.subject.meshAcylationen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshGlyceraldehyde-3-Phosphate Dehydrogenases --chemistryen_US
dc.subject.meshKineticsen_US
dc.subject.meshNAD --metabolismen_US
dc.titleDifferential binding of NAD+ to acyl glyceraldehyde-3-phosphate dehydrogenase and its role in the acyl group transfer reaction.en_US
dc.typeJournal Articleen_US
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