Crystallographic snapshots of active site metal shift in E. coli fructose 1,6-bisphosphate aldolase

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Crystallographic snapshots of active site metal shift in E. coli fructose 1,6-bisphosphate aldolase

Fructose 1,6-bisphosphate aldolase (FBA) is important for both glycolysis and gluconeogenesis in life. Class II (zinc dependent) FBA is an attractive target for the development of antibiotics against protozoa, bacteria, and fungi, and is also widely used to produce various high-value stereoisomers in the chemical and pharmaceutical industry. In this study, the crystal structures of class II Esc...

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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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Intracellular 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...

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Expression, purification, crystallization and preliminary X-ray crystallographic analysis of fructose-1,6-bisphosphate aldolase from Escherichia coli.

Fructose-1,6-bisphosphate aldolase is one of the most important enzymes in the glycolytic pathway and catalyzes the reversible cleavage of fructose-1,6-bisphosphate to dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. The full-length fbaB gene encoding fructose-1,6-bisphosphate aldolase class I (FBPA I) was cloned from Escherichia coli strain BL21. FBPA I was overexpressed in E. coli a...

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Crystallization and preliminary crystallographic data for fructose-1,6-bisphosphate aldolase from Drosophila melanogaster.

Fructose-1,6-bisphosphate aldolase from Drosophila melanogaster has been crystallized from polyethylene glycol 6000 by vapor diffusion technique against buffered polyethylene glycol solutions at 2-4 degrees C. The insect enzyme crystallizes in the orthorhombic system, heretofore unknown for aldolases. The crystals have the space group P212121 (a = 86.3 A, b = 115.7 A, and c = 151.4 A) and conta...

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ژورنال

عنوان ژورنال: BMB Reports

سال: 2016

ISSN: 1976-6696

DOI: 10.5483/bmbrep.2016.49.12.132