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I5907

Sigma-Aldrich

Pyrophosphatase, Inorganic from Escherichia coli

recombinant, expressed in E. coli, lyophilized powder, ≥90%, ≥800 units/mg protein

Synonym(s):

Inorganic Pyrophosphatase, Pyrophosphate phosphohydrolase

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About This Item

CAS Number:
9024-82-2
Enzyme Commission number:
3.6.1.1 (BRENDA, IUBMB)
EC Number:
232-784-7
MDL number:
MFCD00131379
UNSPSC Code:
12352200
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

200

assay

≥90%

form

lyophilized powder

specific activity

≥800 units/mg protein

mol wt

hexamer subunit mol wt 20 kDa

storage temp.

−20°C

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General description

Pyrophosphatase from E coli (E-PPase) has a broader pH optimum and contains four divalent cations per subunit. It comprises 175 amino acids with additional aspartate residue in the active site cavity. Structurally E-PPase is a homohexamer with six identical 20 kDa subunits. Magnesium is a cofactor for E-PPase.

Application

Inorganic pyrophosphatase (PPase) is a ubiquitous enzyme catalyzing the reaction PPi + H2O → 2Pi.
It plays an important role in protein, RNA, and DNA synthesis.
Pyrophosphatase, Inorganic from Escherichia coli has been used as a component of transcription buffer.
Pyrophosphatase, inorganic from Escherichia coli has been used in assay for conjugation of ubiquitin and ubiquitin-like proteins. It has been used for one-pot three-enzyme system for synthesis of Lewis x and sialyl Lewis x antigens.

Biochem/physiol Actions

Pyrophosphatase from E coli (E-PPase) is an essential enzyme in yeast and bacteria The active site residues are crucial for binding to magnesium.

Other Notes

A homohexameric protein containing 175 amino acid residues per subunit, its activity is Mg2+ dependent. It is a relatively thermostable protein.

Unit Definition

One unit will release 1.0 μmole of inorganic orthophosphate per minute at pH 9 at 25 °C.

Physical form

Lyophilized powder in Tris-buffered salts containing protease inhibitors

pictograms

Exclamation mark
GHS07

signalword

Warning

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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The structure of E. coli soluble inorganic pyrophosphatase at 2.7
Kankare J, et al.
Protein engineering, design & selection : PEDS, 7(7), 823-830 (1994)
Microbial inorganic pyrophosphatases.
R Lahti
Microbiological reviews, 47(2), 169-178 (1983-06-01)
Hai Yu et al.
Current protocols in chemical biology, 4, 233-247 (2012-09-01)
L-Fucose has been found abundantly in human milk oligosaccharides, bacterial lipopolysaccharides, glycolipids, and many
Ngoc Truongvan et al.
Nature communications, 13(1), 4789-4789 (2022-08-16)
The covalent modification of target proteins with ubiquitin or ubiquitin-like modifiers is initiated by E1 activating enzymes, which typically transfer a single modifier onto cognate conjugating enzymes. UBA6 is an unusual E1 since it activates two highly distinct modifiers, ubiquitin
Christopher E Berndsen et al.
Analytical biochemistry, 418(1), 102-110 (2011-07-21)
Ubiquitination is a widely studied regulatory modification involved in protein degradation, DNA damage repair, and the immune response. Ubiquitin is conjugated to a substrate lysine in an enzymatic cascade involving an E1 ubiquitin-activating enzyme, an E2 ubiquitin-conjugating enzyme, and an
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