R3251
D-核酮糖-5-磷酸-3-表异构酶 来源于面包酵母（酿酒酵母）
lyophilized powder, 50-100 units/mg protein (modified Warburg-Christian)
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关于此项目
Specific activity:
50-100 units/mg protein (modified Warburg-Christian)
Biological source:
bakers yeast
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 . 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 .
Physical form
基本上无硫酸盐的冻干粉：约含35% 的柠檬酸缓冲盐
Other Notes
在 pH 7.7 和 25°C 下，与转酮醇酶、α-甘油磷酸脱氢酶和磷酸丙糖异构酶偶联时，一单位每分钟可将 1μmol 的 D-核酮糖-5-磷酸转化为 D-木酮糖-5-磷酸。
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
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
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
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
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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