P9752
Phosphoriboisomerase from spinach
Type I, partially purified powder, ≥40 units/mg protein (biuret)
Sinónimos:
D-Ribose-5-phosphate ketol-isomerase
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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥40 units/mg protein (biuret)
Biological source:
spinach
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Permítanos ayudarleNombre del producto
Phosphoriboisomerase from spinach, Type I, partially purified powder, ≥40 units/mg protein (biuret)
biological source
spinach
type
Type I
form
partially purified powder
specific activity
≥40 units/mg protein (biuret)
storage temp.
−20°C
Quality Level
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.
Other Notes
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.
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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
Richard W Strange et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 65(Pt 12), 1214-1217 (2010-01-08)
Ribose-5-phosphate isomerase is a ubiquitous intracellular enzyme of bacterial, plant and animal origin that is involved in the pentose phosphate cycle, an essential component of cellular carbohydrate metabolism. Specifically, the enzyme catalyses the reversible conversion of ribose 5-phosphate to ribulose
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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