91252
2-Deoxyribose 5-phosphate Aldolase, E. coli K12, recombinant K12 from E. coli
≥2 U/mg
别名:
DERA, Deoxyriboaldolase
recombinant
expressed in E. coli
form
crystals, powder
specific activity
≥2 U/mg
shipped in
wet ice
storage temp.
−20°C
Quality Level
Biochem/physiol Actions
Deoxyriboaldolase catalyzes the condensation of acetaldehyde and glyceraldehyde 3-phosphate to 2-deoxyribose 5-phosphate.
Other Notes
1 U corresponds to the amount of enzyme which converts 1 μmol 2-Deoxy-D-ribose-5-phosphate per minute at pH 7.5 and 25°C
The enzyme catalyzes the reversible cleavage of 2-deoxyribose-5-phosphate to acetaldehyde and D-glyceraldehyde-3-phosphate
存储类别
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
Robert A Alberty
Biochemistry, 43(30), 9840-9845 (2004-07-28)
Recent thermodynamic measurements have made it possible to calculate the apparent equilibrium constants of the ribonucleoside diphosphate reductase reaction and the ribonucleoside triphosphate reductase reaction with various reducing agents. Third law heat capacity measurements on crystals of d-ribose and other
Francisco S Domingues et al.
Protein engineering, design & selection : PEDS, 17(6), 537-543 (2004-08-21)
Experimentally determined protein structures have been classified in different public databases according to their structural and evolutionary relationships. Frequently, alternative structural models, determined using X-ray crystallography or NMR spectroscopy, are available for a protein. These models can present significant structural
Neratur K Lokanath et al.
Acta crystallographica. Section D, Biological crystallography, 60(Pt 10), 1816-1823 (2004-09-25)
2-Deoxyribose-5-phosphate aldolase catalyzes a reversible aldol condensation of two aldehydes via formation of a covalent Schiff-base intermediate at the active lysine residue. The crystal structure of 2-deoxyribose-5-phosphate aldolase from Thermus thermophilus HB8 has been determined with and without the substrate
Naeem Rashid et al.
Journal of bacteriology, 186(13), 4185-4191 (2004-06-19)
Numerous bacteria and mammalian cells harbor two enzymes, phosphopentomutase (PPM) and 2-deoxyribose 5-phosphate aldolase (DERA), involved in the interconversion between nucleosides and central carbon metabolism. In this study, we have examined the presence of this metabolic link in the hyperthermophilic
F Sgarrella et al.
Biochimica et biophysica acta, 1118(2), 130-133 (1992-01-09)
Deoxyribose 5-phosphate aldolase was purified 41 times from Bacillus cereus induced by growth on deoxyribonucleosides. The purification procedure includes ammonium sulphate fractionation, gel filtration on Sephadex G-100, ion-exchange chromatography on DEAE-Sephacel and preparative electrophoresis on 10% polyacrylamide gel. The enzyme
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