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
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
Produits recommandés
Source biologique
bakers yeast
Forme
lyophilized powder
Activité spécifique
50-100 units/mg protein (modified Warburg-Christian)
Activité étrangère
phosphoriboisomerase, alcohol dehydrogenase, transketolase, and transaldolase <0.1%
Température de stockage
−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.
Actions biochimiques/physiologiques
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].
Définition de l'unité
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.
Forme physique
Lyophilized and essentially sulfate-free; contains approx. 35% citrate buffer salts
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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M Teige et al.
FEBS letters, 377(3), 349-352 (1995-12-27)
A cDNA clone encoding the chloroplast enzyme pentose-5-phosphate 3-epimerase (EC 5.1.3.1) in potato (Solanum tuberosum) was isolated and sequenced. The deduced sequence of 235 amino acids is similar to protein sequences of bacterial epimerases. Northern blot analysis showed the highest
Matthew B Rogers et al.
BMC evolutionary biology, 7, 89-89 (2007-06-15)
Lateral gene transfer is increasingly invoked to explain phylogenetic results that conflict with our understanding of organismal relationships. In eukaryotes, the most common observation interpreted in this way is the appearance of a bacterial gene (one that is not clearly
Kui K Chan et al.
Biochemistry, 47(36), 9608-9617 (2008-08-15)
Enzymes that share the (beta/alpha) 8-barrel fold catalyze a diverse range of reactions. Many utilize phosphorylated substrates and share a conserved C-terminal (beta/alpha) 2-quarter barrel subdomain that provides a binding motif for the dianionic phosphate group. We recently reported functional
J Caruthers et al.
Proteins, 62(2), 338-342 (2005-11-24)
The crystal structure of Pfal009167AAA, a putative ribulose 5-phosphate 3-epimerase (PfalRPE) from Plasmodium falciparum, has been determined to 2 A resolution. RPE represents an exciting potential drug target for developing antimalarials because it is involved in the shikimate and the
Helena Sävenstrand et al.
Plant & cell physiology, 43(4), 402-410 (2002-04-30)
Suppression subtractive hybridisation was used to isolate genes differentially regulated by low levels (UV-B(BE,300) 0.13 W m(-2)) of ultraviolet-B radiation (UV-B; 290-320 nm) in Pisum sativum. Six genes were regulated, two of which were novel. The mRNA levels for these
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