Disease relevance of fbp

• We have cloned the fructose bisphosphatase (FBP1) structural gene from Saccharomyces cerevisiae by screening a genomic library for complementation of an Escherichia coli fbp deletion mutation [1].
• Fructose-1,6-bisphosphatase from Corynebacterium glutamicum: expression and deletion of the fbp gene and biochemical characterization of the enzyme [2].
• No PCR amplification of the fbp gene was observed for other species of the Lactobacillus casei complex (L. casei and L. zeae) or strains of Lactobacillus acidophilus, Streptococcus thermophilus, and Escherichia coli [3].
• Chromatium vinosum thioredoxin was slightly larger than other bacterial thioredoxins (13 versus 12 kilodaltons) but was similar in its specificity (ability to activate chloroplast NADP-malate dehydrogenase more effectively than chloroplast fructose-1,6-bisphosphatase) and immunological properties [4].
• The Mycobacterium tuberculosis Rv1099c gene encodes a GlpX-like class II fructose 1,6-bisphosphatase [5].

High impact information on fbp

• Fructose-1,6-bisphosphatase (FBPase) governs a key step in gluconeogenesis, the conversion of fructose 1,6-bisphosphate into fructose 6-phosphate [6].
• Kinetics of activation of oxidized recombinant sorghum leaf NADP-dependent malate dehydrogenase and oxidized spinach chloroplastic fructose-1,6-bisphosphatase by wild-type Trx f, wild-type Trx m, and Trx f mutants were compared [7].
• Reduction of the cytosolic fructose-1,6-bisphosphatase in transgenic potato plants limits photosynthetic sucrose biosynthesis with no impact on plant growth and tuber yield [8].
• Based on the presence of conserved sequence motifs and the substrate specificity of the P. furiosus fructose-1,6-bisphosphatase, we propose that this enzyme belongs to a new family, class IV fructose-1,6-bisphosphatase [9].
• The P. furiosus fructose-1,6-bisphosphatase was strongly inhibited by Li(+) (50% inhibitory concentration, 1 mM) [9].

Chemical compound and disease context of fbp

• Fructose bisphosphatase of Escherichia coli: cloning of the structural gene (fbp) and preparation of a chromosomal deletion [10].
• The gluconeogenesis pathway (fbp, pckA, and ppsA) which leads to glycogen accumulation is constitutively active in E. coli BL21 regardless of glucose feeding strategy [11].
• Escherichia coli fructose-1,6-bisphosphatase was inhibited by AMP (Ki = 16 microM) and phosphoenolpyruvate caused release of AMP inhibition [12].
• Spinach fructose 1,6-bisphosphatase (FBPase, EC 3.1.3.11), a redox-modulated chloroplast enzyme and part of the Calvin cycle, and three different Cys mutants were expressed in E. coli [13].

Biological context of fbp

• In vivo mutagenesis of the clone was used to show that fbp is the structural gene [10].
• The fbp locus at 96 min on the Escherichia coli chromosome governs fructose bisphosphatase (fructose-1,6-P2 1-phosphatase) [10].
• Phylogenetic analysis of the fbp putative amino acid sequences of L. rhamnosus strains by the neighbor-joining method showed clear distinct positions of this species [3].
• The phylogenetic tree, derived from fbp nucleotide sequences, showed four clear divisions between strains of L. rhamnosus [3].
• The glpFKX operon encodes glycerol diffusion facilitator, glycerol kinase, and as shown here, a fructose 1,6-bisphosphatase that is distinct from the previously described fbp-encoded enzyme [14].

Associations of fbp with chemical compounds

• Deletion of the chromosomal fbp gene led to the absence of any detectable fructose-1,6-bisphosphatase activity in crude extracts of C. glutamicum WTDelta fbp and to an inability of this strain to grow on the carbon sources acetate, citrate, glutamate, and lactate [2].
• With glycerol as a carbon source, fbp and TCA cycle enzymes were up-regulated, while ackA was significantly down-regulated [15].
• The sequences of 1,971 nucleotides of the fbp gene were determined on both DNA strands for 21 L. rhamnosus strains, representing reference, probiotic, and clinical strains [3].
• With gluconate as a carbon source, edd, eda, fbp and TCA cycle enzymes were up-regulated [15].
• Fructose-1,6-bisphosphatase activity was dependent on the divalent cations Mg(2+) or Mn(2+) and was inhibited by the monovalent cation Li(+) with an inhibition constant of 140 micro M [2].

Analytical, diagnostic and therapeutic context of fbp

• To understand the mechanism of signal propagation involved in the cooperative AMP inhibition of the homotetrameric enzyme pig-kidney fructose-1,6-bisphosphatase, Arg49 and Lys50 residues located at the C1-C2 interface of this enzyme were replaced using site-directed mutagenesis [16].

References