Fructose-1,6-bisphosphate and aldolase mediate glucose sensing by AMPK
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چکیده
منابع مشابه
ALDOB (aldolase B, fructose-bisphosphate)
Other names: ALDB, EC 4.1.2.13, OTTHUMP00000021803 HGNC (Hugo): ALDOB Location: 9q31.1 Local order: Telomeric to the PRG-3 (plasticity related gene 3), BAAT (bile acid Coenzyme A: amino acid N-acyltransferase), MRPL50 (mitochondrial ribosomal protein L50) and ZNF189 (zinc finger protein 189) genes. Centromeric to C9orf125 (chromosome 9 open reading frame 125), RNF20 (ring finger protein 20), PP...
متن کاملIntracellular localization of fructose 1,6-bisphosphate aldolase.
Submission of a rat liver homogenate made in 250 mM sucrose-1 mM EDTA to centrifugation between 9,500 times g for 10 min and 105,000 times g for 60 min results in the sedimentation of 60 to 70% of the total cellular fructose 1,6-bisphosphate aldolase (EC 4.1.2.13). Under these conditions only about one-quarter of the total triose phosphate dehydrogenase and phosphoglycerate kinase appears in th...
متن کاملFructose 1,6-bisphosphate aldolase activity is essential for synthesis of alginate from glucose by Pseudomonas aeruginosa.
We have isolated a mutant of Pseudomonas aeruginosa deficient in fructose 1,6-bisphosphate aldolase activity. This mutant, similar to the mutants deficient in any of the Entner-Doudoroff pathway enzymes, does not allow appreciable alginate formation from glucose and gluconate, but allows alginate synthesis from mannitol and fructose. This suggests that glucose and gluconate must be converted to...
متن کاملStructure of fructose bisphosphate aldolase from Bartonella henselae bound to fructose 1,6-bisphosphate
Fructose bisphosphate aldolase (FBPA) enzymes have been found in a broad range of eukaryotic and prokaryotic organisms. FBPA catalyses the cleavage of fructose 1,6-bisphosphate into glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. The SSGCID has reported several FBPA structures from pathogenic sources, including the bacterium Brucella melitensis and the protozoan Babesia bovis. Bioinf...
متن کاملAction of cathepsin D on fructose-1,6-bisphosphate aldolase.
Cathepsin D inactivated aldolase at pH values between 4.2 and 5.2; the chloride, sulphate or iodide, but not citrate or acetate, salts of sodium or potassium accelerated the rate of inactivation. Cathepsin D cleaved numerous peptide bonds in the C-terminus of aldolase, but the major site of cleavage in this region was Leu354-Phe355. The most prominent peptide products of hydrolysis were Phe-Ile...
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ژورنال
عنوان ژورنال: Nature
سال: 2017
ISSN: 0028-0836,1476-4687
DOI: 10.1038/nature23275