Fructose-1,6-Bisphosphate Aldolase from Rabbit Liver. Reaction Mechanism and Physiological Function
نویسندگان
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...
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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 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 کاملStructure of fructose bisphosphate aldolase from Encephalitozoon cuniculi
Fructose bisphosphate aldolose (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. Bioinformatic analysis of the genome of the eukaryotic microsporidian parasite Ence...
متن کاملEvidence for formation of a rabbit liver aldolase--rabbit liver fructose-1,6-bisphosphatase complex.
The ability of rabbit liver aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphatate-lyase, EC 4.1.2.13) and rabbit liver fructose-1,6-bisphosphatase (Fru-P2ase; D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) to partition into the gel phase of Ultrogel AcA 34 is decreased in a mixture of the two enzymes. Titration experiments indicate that a 1:1 complex is formed. The ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1979
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1979.tb02049.x