form
lyophilized powder
specific activity
≥2 units/mg protein (Lowry)
composition
Protein, 20-40% Lowry
storage temp.
−20°C
Biochem/physiol Actions
Fructose-6-phosphate kinase converts fructose-6-phosphate into fructose 1,6-bisphophate in the rate limiting step of the glycolysis cycle.
Physical form
Lyophilized powder containing sodium phosphate buffer and stabilizers with traces of inorganic pyrophosphate and dithiothreitol
Other Notes
One unit will convert 1.0 μmole of pyrophosphate and fructose 6-phosphate to fructose 1,6-diphosphate and inorganic phosphate per min at pH 8.0 at 30 °C in the presence of 1μM fructose 2,6-diphosphate and 17 mM glucose 6-phosphate.
These two pyrophosphate-dependent fructose-6-phosphate kinases differ in their response to the physiological activator fructose 2,6-diphosphate [Fru (2,6)-P2]. The enzyme from Propionibacterium freudenreichii (F8381) reportedly is not affected by Fru (2,6)-P2. The enzyme from potato tubers (F2258) is stimulated by Fru (2,6)-P2 (half-maximal activation at 5.5 nM Fru (2,6)-P2 for potato tuber enzyme).
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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J Suzuki et al.
Genetics and molecular research : GMR, 2(4), 376-382 (2004-03-11)
Pyrophosphate-dependent phosphofructokinase (PPi-PFK) has been detected in several types of plant cells, but the gene has not been reported in sugar cane. Using Citrus paradisi PPi-PFK gene (AF095520 and AF095521) sequences to search the sugar cane EST database, we have
M E Theodorou et al.
Planta, 213(1), 147-157 (2001-08-29)
A major problem in defining the physiological role of pyrophosphate:fructose 6-phosphate 1-phosphotransferase (PFP, EC 2.7.1.90) is the 1,000-fold discrepancy between the apparent affinity of PFP for its activator, fructose 2,6-bisphosphate (Fru-2,6-P2), determined under optimum conditions in vitro and the estimated
Guillaume Meurice et al.
In silico biology, 4(4), 517-528 (2004-10-28)
We performed a detailed bioinformatic study of the catalytic step of fructose-6-phosphate phosphorylation in glycolysis based on the raw genomic draft of Propionibacterium freudenreichii subsp. shermanii (P. shermanii) ATCC9614 [Meurice et al., 2004]. Our results provide the first in silico
Fabrício Ramon Lopes et al.
Molecular genetics and genomics : MGG, 279(4), 385-401 (2008-01-31)
Transposable elements are major components of plant genomes and they influence their evolution, acting as recombination hot spots, acquiring specific cell functions or becoming part of protein-coding regions. The latter is the subject of the present analysis. This study is
Maher Chaouachi et al.
Journal of agricultural and food chemistry, 55(20), 8003-8010 (2007-09-11)
In the first part of the paper, we report the description of a new strategy for the development of a plant reference gene system that can be used for genetically modified organism (GMO) analysis. On the basis of in silico
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