91252
2-Deoxyribose 5-phosphate Aldolase, E. coli K12, recombinant K12 from E. coli
≥2 U/mg
Synonym(s):
DERA, Deoxyriboaldolase
recombinant
expressed in E. coli
Quality Level
form
crystals
powder
specific activity
≥2 U/mg
shipped in
wet ice
storage temp.
−20°C
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
Storage Class Code
13 - Non Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Yong-Mo Kim et al.
Journal of microbiology and biotechnology, 20(6), 995-1000 (2010-07-14)
A novel deoC gene was identified from Paenibacillus sp. EA001 isolated from soil. The gene had an open reading frame (ORF) of 663 base pairs encoding 220 amino acids with a molecular mass of 24.5 kDa. The amino acid sequence
A Heine et al.
Science (New York, N.Y.), 294(5541), 369-374 (2001-10-13)
In classical enzymology, intermediates and transition states in a catalytic mechanism are usually inferred from a series of biochemical experiments. Here, we derive an enzyme mechanism from true atomic-resolution x-ray structures of reaction intermediates. Two ultra-high resolution structures of wild-type
Xiaolin Pei et al.
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
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
X Zeng et al.
Journal of bacteriology, 181(6), 1719-1727 (1999-03-12)
The deoR gene located just upstream the dra-nupC-pdp operon of Bacillus subtilis encodes the DeoR repressor protein that negatively regulates the expression of the operon at the level of transcription. The control region upstream of the operon was mapped by
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