High impact information on FBP1

• Fructose 2-phosphorothioate 6-phosphate was 10-100-fold less potent than authentic fructose 2,6-bisphosphate in stimulating 6-phosphofructo-1-kinase and pyrophosphate:fructose 6-phosphate phosphotransferase, but about 10 times more potent in inhibiting fructose 1,6-bisphosphatase [1].
• The ESR spectrum of spin-labeled chicken liver fructose-1,6-bisphosphatase showed that the sites of labeling were highly immunobilized when the enzyme was chemically modified by spin label iodoacetate, suggesting that the sulfhydryl groups of the protein are in a small, confined environment [2].
• The local environment of the essential sulfhydryl groups in chicken liver fructose-1,6-bisphosphatase has been investigated by ESR techniques using a series of iodoacetamide spin labels, varying in chain length between the iodoacetate and nitroxide free radical group [2].
• Evidence for heat-stable liver cytosol substance(s) capable of causing oxidative activation of fructose 1,6-bisphosphatase [3].
• Affinity labeling of the allosteric site of fructose 1,6-bisphosphatase with an AMP analog [4].

Associations of FBP1 with chemical compounds

• The extreme sensitivity of chicken muscle fructose 1,6-bisphosphatase to inhibition by 5'-AMP has been utilized to develop a new method for the assay of cAMP phosphodiesterase activity [5].
• Low dietary protein decreased activities of hepatic isocitrate dehydrogenase (EC 1.1.1.42), fructose-1,6-bisphosphatase (EC 3.1.3.11) and glucose-6-phosphatase (EC 3.1.3.9; GP) and increased activities of fatty acid synthase (FAS), citrate cleavage enzyme (EC 4.1.3.8; CCE) and malate dehydrogenase (decarboxylating) (EC 1.1.1.39) [6].
• Modification of catalytic properties of chicken liver fructose 1,6-bisphosphatase by allicin [7].
• Microenvironment around the essential cysteine residues in chicken liver fructose-1,6-bisphosphatase as analyzed by ESR spin labelling [8].
• Selective modification of the AMP allosteric site of fructose 1,6-bisphosphatase with pyridoxal-P and NaBH4 renders the enzyme more resistant to tryptic inactivation, but the modified enzyme is no longer responsive to the protective effect of AMP [9].

Analytical, diagnostic and therapeutic context of FBP1

• Immobilization of chicken liver fructose 1,6-bisphosphatase on CNBr-activated Sepharose [10].

References