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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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$392.79

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:
12352204
NACRES:
NA.32

$392.79

List Price$421.00Save 7%

In StockDetails

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.[1] Structurally E-PPase is a homohexamer with six identical 20 kDa subunits. Magnesium is a cofactor for E-PPase.[2]

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.[3]
Pyrophosphatase, inorganic from Escherichia coli has been used in assay for conjugation of ubiquitin and ubiquitin-like proteins.[4] It has been used for one-pot three-enzyme system for synthesis of Lewis x and sialyl Lewis x antigens.[5]

Biochem/physiol Actions

Pyrophosphatase from E coli (E-PPase) is an essential enzyme in yeast and bacteria[6] The active site residues are crucial for binding to magnesium.[6]

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)

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Certificates of Analysis (COA)

Lot/Batch Number
0000365108
0000365108
0000173793
0000088413
079M4172V

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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
The structure of E. coli soluble inorganic pyrophosphatase at 2.7
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Protein engineering, design & selection : PEDS, 7(7), 823-830 (1994)
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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
Elodie Laine et al.
Proceedings of the National Academy of Sciences of the United States of America, 107(25), 11277-11282 (2010-06-11)
Allostery plays a key role in the regulation of the activity and function of many biomolecules. And although many ligands act through allostery, no systematic use is made of it in drug design strategies. Here we describe a procedure for
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