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
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
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
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