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
Numero CAS:
Numero MDL:
Codice UNSPSC:
12352204
Prodotti consigliati
Origine biologica
bakers yeast
Stato
lyophilized powder
Attività specifica
50-100 units/mg protein (modified Warburg-Christian)
Attività estranea
phosphoriboisomerase, alcohol dehydrogenase, transketolase, and transaldolase <0.1%
Temperatura di conservazione
−20°C
Applicazioni
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.
Azioni biochim/fisiol
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].
Definizione di unità
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.
Stato fisico
Lyophilized and essentially sulfate-free; contains approx. 35% citrate buffer salts
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, type N95 (US)
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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
Ramya Parasuram et al.
Journal of bioinformatics and computational biology, 8 Suppl 1, 1-15 (2010-12-15)
A new approach to the functional classification of protein 3D structures is described with application to some examples from structural genomics. This approach is based on functional site prediction with THEMATICS and POOL. THEMATICS employs calculated electrostatic potentials of the
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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