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應用
可用于通过 O′Brien, W., Anal. Biochem., FB76, 423 (1976) 介绍的方法进行焦磷酸盐测定。
生化/生理作用
Fructose-1,6-bisphosphatase (FBP) is an important enzyme in glucose metabolism. It catalyzes the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate. Fructose-6-phosphate kinase converts fructose-6-phosphate into fructose 1,6-bisphophate in the rate limiting step of the glycolysis cycle.
其他說明
这两种焦磷酸依赖性果糖-6-磷酸激酶的区别在于它们对生理活化剂果糖 2,6-二磷酸 [Fru (2,6)-P2]的反应不同。据报道,来自费氏丙酸杆菌的酶 (F8381) 不受 Fru (2,6)-P2 影响。而来自马铃薯块茎的酶 (F2258) 则可被 Fru (2,6)-P2 激活(在 5.5nM Fru (2,6)-P2 条件下,半最大活化马铃薯块茎酶)。
單位定義
在 pH 7.4 和 30°C 下,一单位每分钟可将 1.0μmol 的焦磷酸盐和果糖-6-磷酸转化为果糖-1,6-二磷酸和无机磷酸盐。
外觀
含咪唑盐和稳定剂
訊號詞
Danger
危險聲明
危險分類
Eye Dam. 1 - Repr. 1B - Resp. Sens. 1 - Skin Corr. 1C
儲存類別代碼
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
水污染物質分類(WGK)
WGK 3
閃點(°F)
Not applicable
閃點(°C)
Not applicable
個人防護裝備
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
其他客户在看
Corrigendum: Online Pyrophosphate Assay for Analyzing Adenylation Domains of Nonribosomal Peptide Synthetases.
Chembiochem : a European journal of chemical biology, 23(18), e202200381-e202200381 (2022-07-28)
Chembiochem : a European journal of chemical biology, 23(18), e202200325-e202200325 (2022-07-26)
Detection of pyrophosphate is important in quantifying enzyme activity, particularly adenylation domain activity during non-ribosomal peptide synthesis. The previous development of an enzyme coupled PPi /NADH assay allowed the measurement of such activity in an online fashion using commercially available
Biochemistry, 23(18), 4101-4108 (1984-08-28)
Inorganic pyrophosphate dependent D-fructose-6-phosphate 1-phosphotransferase from Propionibacterium freudenreichii was purified to apparent homogeneity by the criterion of silver staining on sodium dodecyl sulfate (SDS) gels. In the direction of phosphorylation of fructose 6-phosphate (F6P), an intersecting initial velocity pattern is
Planta, 214(1), 106-116 (2002-01-05)
The role of pyrophosphate:fructose-6-phosphate 1-phosphotransferase (PFP) in developing leaves was studied using wild-type tobacco (Nicotiana tabacum L.) and transformants with decreased expression of PFP. (i) The leaf base, which is the youngest and most actively growing area of the leaf
Archives of biochemistry and biophysics, 414(1), 101-107 (2003-05-15)
The intrinsic fluorescence of potato tuber pyrophosphate:fructose-6-phosphate 1-phosphotransferase (PFP) was used as an indicator of conformational changes due to ligand binding. Binding of the substrates and the allosteric activator fructose-2,6-bisphosphate was quantitatively compared to their respective kinetic effects on enzymatic
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