Identification of zinc-binding ligands in the Class II fructose- 1,6-bisphosphate aldolase of Escherichia coli
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چکیده
منابع مشابه
The dhnA gene of Escherichia coli encodes a class I fructose bisphosphate aldolase.
The gene encoding the Escherichia coli Class I fructose-1, 6-bisphosphate aldolase (FBP aldolase) has been cloned and the protein overproduced in high amounts. This gene sequence has previously been identified as encoding an E. coli dehydrin in the GenBanktrade mark database [gene dhnA; entry code U73760; Close and Choi (1996) Submission to GenBanktrade mark]. However, the purified protein over...
متن کاملALDOB (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 کاملStructure of Class II Tagatose - 1 , 6 - bisphosphate Aldolase 22019
ion of a proton from DHAP C1 would be feasible. Glu of FBPA corresponds to Glu in TBPA, which is also positioned on a glycine-rich loop. Due to the lack of reliable electron density, this residue has not been included in the TBPA model and it is presumed to be flexible and disordered. The sequence conservation of this loop in TBPA and FBPA is high (Fig. 2), which implies that Glu could adopt a ...
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...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1993
ISSN: 0014-5793
DOI: 10.1016/0014-5793(93)81317-s