R3251
D-Ribulose-5-phosphate 3-Epimerase from baker′s yeast (S. cerevisiae)
lyophilized powder, 50-100 units/mg protein (modified Warburg-Christian)
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
Pricing and availability is not currently available.
Recommended Products
biological source
bakers yeast
form
lyophilized powder
specific activity
50-100 units/mg protein (modified Warburg-Christian)
foreign activity
phosphoriboisomerase, alcohol dehydrogenase, transketolase, and transaldolase <0.1%
storage temp.
−20°C
Application
D-Ribulose-5-phosphate 3-Epimerase is an enzyme that converts the reversible conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate, which is important for the cellular response against oxidative stress [1]. D-Ribulose-5-phosphate 3-Epimerase is involved in the pentose phosphate pathway, pentose and glucuronate interconversions and carbon fixation. Product R3251 is from baker′s yeast and is provided as a lyophilized powder. It is useful in enzyme systems requiring low sulfate.
Biochem/physiol Actions
RPE is a metalloenzyme and has been shown to use the divalent Zn2+ ion predominantly for catalysis. Human D-ribulose-5-phosphate 3-epimerase (hRPE) has been shown to use Fe2+ for catalysis [1].
Unit Definition
One unit will convert 1 μmole of D-ribulose 5-phosphate to D-xylulose 5-phosphate per min at pH 7.7 at 25°C when coupled with transketolase, α-glycerophosphate dehydrogenase, and triosephosphate isomerase.
Physical form
Lyophilized and essentially sulfate-free; contains approx. 35% citrate buffer salts
Storage Class Code
11 - 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
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Jason M Sobota et al.
Proceedings of the National Academy of Sciences of the United States of America, 108(13), 5402-5407 (2011-03-16)
H(2)O(2) is commonly generated in biological habitats by environmental chemistry and by cellular immune responses. H(2)O(2) penetrates cells, disrupts metabolism, and blocks growth; it therefore is of interest to identify the major cellular molecules that H(2)O(2) damages and the strategies
Stefan Jelakovic et al.
Journal of molecular biology, 326(1), 127-135 (2003-01-28)
Cytosolic D-ribulose-5-phosphate 3-epimerase from rice was crystallized after EDTA treatment and structurally elucidated by X-ray diffraction to 1.9A resolution. A prominent Zn(2+) site at the active center was established in a soaking experiment. The structure was compared with that of
D L Falcone et al.
Journal of bacteriology, 175(16), 5066-5077 (1993-08-01)
A ribulose 1,5-bisphosphate carboxylase-oxygenase (RubisCO) deletion strain of Rhodospirillum rubrum that was incapable of photolithoautotrophic growth was constructed. Photoheterotrophic growth, however, was possible for the R. rubrum RubisCO deletion strain when oxidized carbon compounds such as malate were supplied. The
S Graupner et al.
Biomolecular engineering, 17(1), 11-16 (2000-10-24)
A series of expression vectors for gram-negative bacteria was constructed which combine broad-host-range, inducible expression from the tac promoter and diverse antibiotic resistance determinants. The tac promoter activity and the repression by lacIq can be quantitated with a separate test
S Kopriva et al.
The Journal of biological chemistry, 275(2), 1294-1299 (2000-01-08)
Plant cells contain a complete oxidative pentose phosphate pathway in the chloroplasts, but an incomplete pathway was proposed to be present in the cytosol, with cytosolic (cyt) isoforms of ribulose-5-phosphate 3-epimerase (RPEase) and other non-oxidative branch enzymes being undetectable. Here
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