Disease relevance of FBP2

• A PFK-2/FBPase-2 sequence in the genome of one prokaryote, the proteobacterium Desulfovibrio desulfuricans, could be the result of horizontal gene transfer from a eukaryote distantly related to all other organisms, possibly a protist [1].

High impact information on FBP2

• PFK-2/FBPase-2: maker and breaker of the essential biofactor fructose-2,6-bisphosphate [2].
• The protein products of these genes, designated floral binding protein 1 (FBP1) and 2 (FBP2), are putative transcription factors with the MADS box DNA binding domain [3].
• A homolog of FBP2/KSRP binds to localized mRNAs in Xenopus oocytes [4].
• Four different isolates encoded a Xenopus homolog of the human transcription factor, FUSE-binding protein 2 (FBP2) [4].
• The bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2) has been identified as an activating binding partner of beta-cell GK, increasing the V(max) value of the enzyme, while the S(0.5) value for glucose remains unchanged [5].

Biological context of FBP2

• The human gene (FBP2), localized at chromosome 1p36.1-2, spans about 30 kb, while the mouse gene (Fbp2) at chromosome 13B3-C1 is more compact (about 21 kb) [6].
• A truly bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (6PFK2/FBP2), with two active sites synthesizes F26P(2) from fructose-6-phosphate (F6P) and ATP or degrades F26P(2) to F6P and P(i) [7].
• Amino acid sequence comparison showed a high degree of similarity between the SaMADS D and AGL9, DEFH200, TM5, FBP2 and DEFH 72 gene products [8].
• The effect of cyclic AMP (cAMP)-dependent phosphorylation and ADP-ribosylation on the activities of the rat liver bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2), was investigated in order to determine the role of the N-terminus in covalent modification of the enzyme [9].
• 6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2) catalyzes the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis [10].

Anatomical context of FBP2

• Taken together, these results provide evidence for a new PFK-2/FBPase-2 gene coding for a human testis isozyme [11].

Associations of FBP2 with chemical compounds

• Furthermore, pyruvate accumulation and lactate production in RINm5F-GK-PFK-2/FBPase-2 cells were significantly lower at both 10 and 30 mmol/liter glucose than in RINm5F-GK and RINm5F cells [12].
• 6-Phosphofructo-2-kinase/fructose 2,6-bisphosphatase (PFK-2/FBPase-2) is a bifunctional enzyme responsible for the synthesis and breakdown of Fru-2,6-P2, a key metabolite in the regulation of glycolysis [11].
• The FBPase-2 domain of the enzyme subunit bears sequence, mechanistic and structural similarity to the histidine phosphatase family of enzymes [1].

Other interactions of FBP2

• Previous studies assigned the gene for human liver PFK-2/FBPase-2 (HGMW-approved symbol PFKFB1) to the X chromosome; however, precise localization remained ambiguous, with the gene variously placed between Xcen-q13, Xq27-q28, and Xp11.22-p11.21 [10].
• The heterogeneity of human brain PFK-2/FBPase-2 isoforms is generated by alternative splicing [13].
• Four of these overlapping YACs were mapped using rare-cutter restriction enzymes to provide in-depth characterization of an 820-kb region encompassing the PFK-2/ FBPase-2 and ALAS2 genes [10].

References