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Safety Information

P9752

Sigma-Aldrich

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:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

spinach

Quality Level

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

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

P9752-BULK:
P9752-VAR:
P9752-1KU:
P9752-5KU:


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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
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
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
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
Tae Gyun Kim et al.
Molecules and cells, 27(1), 99-103 (2009-02-14)
Ribose-5-phosphate isomerase A (RpiA) plays an important role in interconverting between ribose-5-phosphate (R5P) and ribulose-5-phosphate in the pentose phosphate pathway and the Calvin cycle. We have determined the crystal structures of the open form RpiA from Vibrio vulnificus YJ106 (VvRpiA)

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