生化/生理作用
Deoxyriboaldolase catalyzes the condensation of acetaldehyde and glyceraldehyde 3-phosphate to 2-deoxyribose 5-phosphate.
单位定义
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
其他说明
The enzyme catalyzes the reversible cleavage of 2-deoxyribose-5-phosphate to acetaldehyde and D-glyceraldehyde-3-phosphate
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
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
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
Applied and environmental microbiology, 69(7), 3791-3797 (2003-07-04)
The gene encoding a deoxyriboaldolase (DERA) was cloned from the chromosomal DNA of Klebsiella pneumoniae B-4-4. This gene contains an open reading frame consisting of 780 nucleotides encoding 259 amino acid residues. The predicted amino acid sequence exhibited 94.6% homology
Applied biochemistry and biotechnology, 162(5), 1423-1434 (2010-03-17)
2-Deoxyribose-5-phosphate aldolase (DERA) catalyzes a sequential aldol reaction useful in synthetic chemistry. In this work, the effect of a feeding strategy on the production of a thermophilic DERA was investigated in fed-batch cultures of recombinant Escherichia coli BL21 (pET303-DERA008). The
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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