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72831

Sigma-Aldrich

Ketoreductase

recombinant, expressed in E. coli, ≥2.2 U/mg

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204

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).

Pictograms

Health hazard

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
Kerstin Thurow and Hilmar Weinmann
Journal of Laboratory Automation, 11, 1-6 (2006)
Roselyne Castonguay et al.
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
Carol Larroy et al.
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
Jonathan A Doorn et al.
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
X Li et al.
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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