72831
Ketoreductase
recombinant, expressed in E. coli, ≥2.2 U/mg
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About This Item
recombinant
expressed in E. coli
form
powder
powder with small lumps
specific activity
≥2.2 U/mg
storage temp.
2-8°C
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Application
Ketoreductases are used to study the stereospecificity of ketoreductase domains . They may be used to reduce precursors of α-chloroalcohols, which are synthetic intermediates for various pharmaceutical compounds . Product 72831 is recombinant and expressed in E. coli at ≥ 2.2 U/mg.
Biochem/physiol Actions
Ketoreductase, Product 77857, reduces 4-chloroacetoacetate with NADPH as a cosubstrate.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Unit Definition
1 U corresponds to the amount of enzyme which reduces 1 μmol 4-chloroacetoacetate per minute at pH 6.0 and 25°C (cosubstrate NADPH).
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Automation Highlights from the Literature
Journal of Laboratory Automation, 11, 1-6 (2006)
Journal of the American Chemical Society, 130(35), 11598-11599 (2008-08-13)
Tylactone synthase (TYLS) is a modular polyketide synthase that catalyzes the formation of tylactone (1), the parent aglycone precursor of the macrolide antibiotic tylosin. TYLS modules 1 and 2 are responsible for the generation of antidiketide and triketide intermediates, respectively
European journal of biochemistry, 269(22), 5738-5745 (2002-11-09)
A new NADP(H)-dependent alcohol dehydrogenase (the YCR105W gene product, ADHVII) has been identified in Saccharomyces cerevisiae. The enzyme has been purified to homogeneity and found to be a homodimer of 40 kDa subunits and a pI of 6.2-6.4. ADHVII shows
Biochemistry, 43(41), 13106-13114 (2004-10-13)
4-Oxonon-2-enal (4ONE) was demonstrated to be a product of lipid peroxidation, and previous studies found that it was highly reactive toward DNA and protein. The present study sought to determine whether carbonyl reductase (CR) catalyzes reduction of 4ONE, representing a
Wei sheng wu xue bao = Acta microbiologica Sinica, 41(4), 463-468 (2003-01-30)
ANADPH-dependent 2-Oxoaldehyde reductase was isolated and purified from a marine bacteria Bacillus sp. The purification procedure involved ammonium sulfate fractionation and Q Sepharose FF, Hydroxyapatite, Sephadex G-100 column chromatographies. The specific activity of the purified enzyme was increased by 141.1
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