72831
Ketoreductase
recombinant, expressed in E. coli, ≥2.2 U/mg
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About This Item
CAS Number:
UNSPSC Code:
12352204
EC Number:
232-823-8
MDL number:
recombinant
expressed in E. coli
form
powder, powder with small lumps
specific activity
≥2.2 U/mg
storage temp.
2-8°C
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.
Other Notes
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).
wgk
WGK 3
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class
13 - Non Combustible Solids
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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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
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Journal of Laboratory Automation, 11, 1-6 (2006)
João R M Almeida et al.
Applied microbiology and biotechnology, 78(6), 939-945 (2008-03-12)
Saccharomyces cerevisiae alcohol dehydrogenases responsible for NADH-, and NADPH-specific reduction of the furaldehydes 5-hydroxymethyl-furfural (HMF) and furfural have previously been identified. In the present study, strains overexpressing the corresponding genes (mut-ADH1 and ADH6), together with a control strain, were compared
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Structure determination of porcine aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat was carried out to explain the difference in the potency of the inhibitor for aldose and aldehyde reductases. The hydrogen bonds between the active-site
Q Ye et al.
Proteins, 44(1), 12-19 (2001-05-17)
Pig aldehyde reductase containing the active site mutation tyrosine(50) to phenylalanine has been crystallized in the presence of the cofactor NADP(H) to a resolution of 2.2 A. This structure clearly shows loss of the tyrosine hydroxyl group and no other
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