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Chemical Compound Review:

AG-K-62401 2-(2-bromoethanoylamino) ethoxyphosphonic acid

Synonyms: AC1L4MMJ, CTK4J5262, AR-1D6061, AC1Q6T3D, 52011-43-5, ...

Meng, M. et al., Sakakibara, R. et al., Harada, Y. et al., Chou, C.C. et al., Kitamura, K. et al., et al.

Meng, Chane, Sun, Hsiao, Foster, Wiedemann, Pan, Chou, Nordlie,

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Disease relevance of N-Bromoacetylethanolamine phosphate

In the present study, this conserved histidine, His311, of the enzyme from Bacillus stearothermophilus was subjected to mutational analysis, and the mutational effect on the inactivation kinetics by N-bromoacetylethanolamine phosphate was investigated [1].

High impact information on N-Bromoacetylethanolamine phosphate

Here we present the crystal structures of phosphoglucose isomerase complexed with 5-phospho-D-arabinonate and N-bromoacetylethanolamine phosphate at 2.5- and 2.3-A resolution, respectively [2].
Fructose-6-P binding sites of rat liver and bovine heart Fru-6-P,2-kinase:Fru-2,6-bisphosphatase were investigated with an affinity labeling reagent, N-bromoacetylethanolamine phosphate [3].
The inactivation reaction follows pseudo first-order kinetics to completion and with increasing concentrations of N-bromoacetylethanolamine phosphate a rate saturation effect is observed [4].
N-bromoacetylethanolamine phosphate inactivated irreversibly the activity of wild-type phosphoglucose isomerase; however, His311 --> Ala became resistant to this inhibitor, indicating that His311 is located in the active site and is responsible for the inactivation of the enzyme by this active site-directed inhibitor [1].
In addition, G6P accumulation was nearly abolished in microsomes treated with N-bromoacetylethanolamine phosphate, an irreversible inhibitor of the G6PT [5].

Biological context of N-Bromoacetylethanolamine phosphate

Hexose phosphate binding sites of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase. Interaction with N-bromoacetylethanolamine phosphate and 3-bromo-1,4-dihydroxy-2-butanone 1,4-bisphosphate [4].
The purpose of this study was to determine whether or not N-bromoacetylethanolamine phosphate (BrAcNHEtOP), a specific active site-directed inactivator of Fru-6-P,2-kinase, is useful for studies on the role of Fru-6-P,2-kinase in the regulation of glycolysis in vivo [6].
Inhibition of tumor cell growth by a specific 6-phosphofructo-2-kinase inhibitor, N-bromoacetylethanolamine phosphate, and its analogues [7].

Associations of N-Bromoacetylethanolamine phosphate with other chemical compounds

Ribulose-5-phosphate kinase from spinach was rapidly inactivated by N-bromoacetylethanolamine phosphate in a bimolecular fashion with a k2 of 2.0 M-1 S-1 at 2 degrees C and pH 8 [8].

References

Probing the location and function of the conserved histidine residue of phosphoglucose isomerase by using an active site directed inhibitor N-bromoacetylethanolamine phosphate. Meng, M., Chane, T.L., Sun, Y.J., Hsiao, C.D. Protein Sci. (1999) [Pubmed]
The crystal structure of phosphoglucose isomerase/autocrine motility factor/neuroleukin complexed with its carbohydrate phosphate inhibitors suggests its substrate/receptor recognition. Chou, C.C., Sun, Y.J., Meng, M., Hsiao, C.D. J. Biol. Chem. (2000) [Pubmed]
Catalytic site of rat liver and bovine heart fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase. Identification of fructose 6-phosphate binding site. Kitamura, K., Uyeda, K., Hartman, F.C., Kangawa, K., Matsuo, H. J. Biol. Chem. (1989) [Pubmed]
Hexose phosphate binding sites of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase. Interaction with N-bromoacetylethanolamine phosphate and 3-bromo-1,4-dihydroxy-2-butanone 1,4-bisphosphate. Sakakibara, R., Kitajima, S., Hartman, F.C., Uyeda, K. J. Biol. Chem. (1984) [Pubmed]
Discriminant responses of the catalytic unit and glucose 6-phosphate transporter components of the hepatic glucose-6-phosphatase system in Ehrlich ascites-tumor-bearing mice. Foster, J.D., Wiedemann, J.M., Pan, C.J., Chou, J.Y., Nordlie, R.C. Arch. Biochem. Biophys. (2001) [Pubmed]
Inhibition of fructose-6-phosphate,2-kinase by N-bromoacetylethanolamine phosphate in vitro and in vivo. Harada, Y., Tominaga, N., Watanabe, M., Shimokawa, R., Ishiguro, M., Sakakibara, R. J. Biochem. (1997) [Pubmed]
Inhibition of tumor cell growth by a specific 6-phosphofructo-2-kinase inhibitor, N-bromoacetylethanolamine phosphate, and its analogues. Hirata, T., Watanabe, M., Miura, S., Ijichi, K., Fukasawa, M., Sakakibara, R. Biosci. Biotechnol. Biochem. (2000) [Pubmed]
Evidence for a reactive cysteine at the nucleotide binding site of spinach ribulose-5-phosphate kinase. Omnaas, J., Porter, M.A., Hartman, F.C. Arch. Biochem. Biophys. (1985) [Pubmed]

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