P9752
Phosphoriboisomerase from spinach
Type I, partially purified powder, ≥40 units/mg protein (biuret)
Synonym(s):
D-Ribose-5-phosphate ketol-isomerase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
biological source
spinach
type
Type I
form
partially purified powder
specific activity
≥40 units/mg protein (biuret)
storage temp.
−20°C
Application
Phosphoriboisomerase is used to study the ribulose monophosphate pathway. Phosphoriboisomerase from spinach is used in enzyme assays to convert ribose 5-phosphate to ribulose 5-phosphate.
Biochem/physiol Actions
Phosphoriboisomerase is responsible for the converstion of ribose 5-phosphate to ribulose 5-phosphate.
Unit Definition
One unit will convert 1.0 μmole of D-ribose 5-phosphate to D-ribulose 5-phosphate per min at pH 7.7 at 30 °C.
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
Certificates of Analysis (COA)
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Mirjam M C Wamelink et al.
Journal of molecular medicine (Berlin, Germany), 88(9), 931-939 (2010-05-26)
Ribose 5-phosphate isomerase (RPI) deficiency is an enzymopathy of the pentose phosphate pathway. It manifests with progressive leukoencephalopathy and peripheral neuropathy and belongs, with one sole diagnosed case, to the rarest human disorders. The single patient was found compound heterozygous
Thomas E Edwards et al.
BMC structural biology, 11, 39-39 (2011-10-15)
Ribose-5-phosphate isomerase is an enzyme that catalyzes the interconversion of ribose-5-phosphate and ribulose-5-phosphate. This family of enzymes naturally occurs in two distinct classes, RpiA and RpiB, which play an important role in the pentose phosphate pathway and nucleotide and co-factor
Z Wu et al.
Journal of applied microbiology, 106(1), 41-48 (2009-01-06)
This paper describes optimization of electrotransformation of Mu transposition complexes into Lactococcus lactis cells and identification of genes affecting nisin production. The highest transformation efficiency, 1.1 x 10(2) transformants microg(-1) of input transposon DNA, was achieved when cells were grown
Soo-Jin Yeom et al.
Biotechnology letters, 32(6), 829-835 (2010-02-16)
The activity of ribose-5-phosphate isomerases (RpiB) from Clostridium difficile for D-ribose isomerization was optimal at pH 7.5 and 40 degrees C, while that from Thermotoga maritima for L-talose isomerization was optimal at pH 8.0 and 70 degrees C. C. difficile
Sandrine Mariano et al.
Carbohydrate research, 344(7), 869-880 (2009-03-31)
This study reports syntheses of d-allose 6-phosphate (All6P), D-allulose (or D-psicose) 6-phosphate (Allu6P), and seven D-ribose 5-phosphate isomerase (Rpi) inhibitors. The inhibitors were designed as analogues of the 6-carbon high-energy intermediate postulated for the All6P to Allu6P isomerization reaction (Allpi
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