Investigation of allosteric regulation of porcine fructose-1,6-bisphosphatase

dc.contributor.advisor Herbert J. Fromm
dc.contributor.advisor Richard B. Honzatko Lu, Jian
dc.contributor.department Biochemistry, Biophysics and Molecular Biology 2018-08-22T21:58:13.000 2020-06-30T07:37:22Z 2020-06-30T07:37:22Z Mon Jan 01 00:00:00 UTC 2007 2007-01-01
dc.description.abstract <p>Porcine Fructose-1,6-bisphosphatase is a homotetramer with four identical subunits. It plays a central role in gluconeogenesis and is tightly regulated by metabolites fructose 2,6-bisphosphate (F26P2) and AMP. Loop 52-72, loop 182-194 and residues 7-11 of the N-terminal segment play important role in the mechanism of catalysis and allosteric inhibition by AMP by retaining a structural hydrophobic region. Disruption of the hydrophobic region will evidently affect the catalysis and regulation of FBPase. Mutation of Thr53 reduced the catalysis activity of FBPase, mutation of Thr194 eliminated inhibition of AMP due to its low affinity to the enzyme, while double mutation Thr53/194 had accumulative effect. Mutation Ala10 exhibited biphasic AMP inhibition, an AMP high affinity site which had comparable IC50 with wild-type FBPase and an AMP low affinity site which required 3000-fold AMP to reach 50% relative inhibition.</p>
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dc.identifier.articleid 15531
dc.identifier.contextkey 6984393
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath rtd/14532
dc.language.iso en
dc.source.bitstream archive/|||Fri Jan 14 20:21:58 UTC 2022
dc.subject.disciplines Biochemistry
dc.subject.keywords Biochemistry
dc.subject.keywords biophysics
dc.subject.keywords and molecular biology;Biochemistry;
dc.title Investigation of allosteric regulation of porcine fructose-1,6-bisphosphatase
dc.type article
dc.type.genre thesis
dspace.entity.type Publication
relation.isOrgUnitOfPublication faf0a6cb-16ca-421c-8f48-9fbbd7bc3747 thesis Master of Science
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