P9752
Phosphoriboisomerase from spinach
Type I, partially purified powder, ≥40 units/mg protein (biuret)
Synonym(e):
D-Ribose-5-phosphate ketol-isomerase
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About This Item
CAS-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54
Empfohlene Produkte
Biologische Quelle
spinach
Typ
Type I
Form
partially purified powder
Spezifische Aktivität
≥40 units/mg protein (biuret)
Lagertemp.
−20°C
Anwendung
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. Wirkung
Phosphoriboisomerase is responsible for the converstion of ribose 5-phosphate to ribulose 5-phosphate.
Einheitendefinition
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.
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
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Anna Tylki-Szymańska et al.
Postepy biochemii, 57(2), 168-171 (2011-09-15)
Two previously unreported inborn errors of metabolism occur in the reversible part of the pentose phosphate pathway. Deficiency of ribose-5-phosphate isomerase has been described in one patient who suffered from a progressive leukoencephalopathy and developmental delay. Transaldolase deficiency has been
E J Dodson et al.
Acta crystallographica. Section D, Biological crystallography, 65(Pt 9), 881-891 (2009-08-20)
The density-modification procedures incorporated in ACORN, available in the CCP4 package, have proved to be very successful in solving and refining high-resolution crystal structures from very poor starting sets. These can be calculated from a correctly positioned initial fragment containing
Junho Jung et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 65(Pt 11), 1141-1144 (2009-11-20)
Rare sugars are used for many industrial and medical purposes and are produced by the interconversion between aldoses and ketoses catalyzed by sugar and sugar-phosphate isomerases. Recently, Clostridium thermocellum d-ribose-5-phosphate isomerase (CTRPI), an aldose-ketose isomerase, was cloned in order to
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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