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U8501

Uridine-5′-diphosphoglucose pyrophosphorylase from baker′s yeast

Type X, lyophilized powder, ≥40 units/mg protein

Synonym(s):

UTP:α-D-glucose-1-phosphate uridylyltransferase

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25 UNITS

$190.00

100 UNITS

$604.00

500 UNITS

$1,790.00

1000 UNITS

$2,880.00

$190.00


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About This Item

CAS Number:
EC Number:
UNSPSC Code:
12352204
EC Number:
232-811-2
NACRES:
NA.54
MDL number:

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Product Name

Uridine-5′-diphosphoglucose pyrophosphorylase from baker′s yeast, Type X, lyophilized powder, ≥40 units/mg protein

biological source

bakers yeast

type

Type X

form

lyophilized powder

specific activity

≥40 units/mg protein

composition

Protein, 30-60% modified Warburg-Christian

foreign activity

UDP-glucose dehydrogenase and galactose-1-phosphate uridyltransferase ≤0.1%
inorganic pyrophosphatase ≤0.5%

storage temp.

−20°C

Quality Level

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1 of 4

This Item
P7634P5381G4256
specific activity

≥40 units/mg protein

specific activity

≥500 units/mg protein

specific activity

≥400 units/mg protein (biuret)

specific activity

20-60 units/mg protein (modified Warburg-Christian)

biological source

bakers yeast

biological source

bakers yeast

biological source

bakers yeast

biological source

-

form

lyophilized powder

form

ammonium sulfate suspension

form

ammonium sulfate suspension

form

lyophilized powder

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

300

foreign activity

UDP-glucose dehydrogenase and galactose-1-phosphate uridyltransferase ≤0.1%, inorganic pyrophosphatase ≤0.5%

foreign activity

Glyceraldehyde-3-phosphate dehydrogenase ≤0.1%

foreign activity

-

foreign activity

6-phosphogluconate dehydrogenase ≤0.5%, UDP glucose pyrophosphorylase and galactokinase ≤0.2%

Application

Uridine-5′-diphosphoglucose pyrophosphorylase from baker′s yeast has been used:
  • in the synthesis of uridine-5′-diphosphoglucose (UDP-Glc)-13C9[1]
  • to quantify Suc synthase (SUS) enzyme activity in rice[2]
  • to study the role of hexokinase and glycogen synthase controls the flux in frog oocytes[3]

Biochem/physiol Actions

Uridine-5′-diphosphoglucose pyrophosphorylase (UDP-glc-PPase) participates in catalyzing the synthesis of UDP-glucose. This enzyme requires divalent cations such as Mg2+, Ca2+, Mn2+, Ni2+ for its activity.[4]

General description

Uridine-5′-diphosphoglucose pyrophosphorylase (UDP-glc-PPase) is ubiquitous in plants, yeast, bacteria, and mammals. This enzyme is an octamer of eight identical sub-units.[4]

Other Notes

One unit will form 1.0 μmole of glucose 1-phosphate from uridine-5′-diphosphoglucose and inorganic pyrophosphate per min at pH 7.6 at 25 °C.

Physical form

Lyophilized, sulfate-free powder containing citrate buffer salt

Storage Class

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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Orelvis Portal et al.
Plant cell reports, 30(5), 913-928 (2011-02-01)
Mycosphaerella fijiensis, a hemibiotrophic fungus, is the causal agent of black leaf streak disease, the most serious foliar disease of bananas and plantains. To analyze the compatible interaction of M. fijiensis with Musa spp., a suppression subtractive hybridization (SSH) cDNA
Expression of trehalose-6-phosphate phosphatase in maize ears improves yield in well-watered and drought conditions
Michael L N, et al.
Nature Biotechnology, 862?869-862?869 (2015)
Ziying Huang et al.
Molecular biology reports, 38(7), 4291-4302 (2010-11-30)
OsUgp2, a rice UDP-glucose pyrophosphorylase gene, has previously been shown to preferentially express in maturing pollens and plays an important role in pollen starch accumulation. Here, a 1943 bp promoter fragment (P1943) of OsUgp2 was characterized by 5' deletion and
Activities of enzymes for sucrose-starch conversion in developing endosperm of rice and their association with grain filling in extra-heavy panicle types
Kato T, et al.
Plant Protection Science, 10(4), 442-450 (2007)
Lucila I Martínez et al.
Biochimie, 93(2), 260-268 (2010-10-05)
Amoebiasis is an intestinal infection caused by the human pathogen Entamoeba histolytica and representing the third leading cause of death by parasites in the world. Host-parasite interactions mainly involve anchored glycoconjugates localized in the surface of the parasitic cell. In

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