I5907
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:
UNSPSC Code:
12352204
NACRES:
NA.32
EC Number:
232-784-7
MDL number:
Specific activity:
≥800 units/mg protein
Assay:
≥90%
Recombinant:
expressed in E. coli
recombinant
expressed in E. coli
assay
≥90%
form
lyophilized powder
specific activity
≥800 units/mg protein
mol wt
hexamer subunit mol wt 20 kDa
storage temp.
−20°C
Quality Level
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.
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.
Physical form
Lyophilized powder in Tris-buffered salts containing protease inhibitors
Other Notes
A homohexameric protein containing 175 amino acid residues per subunit, its activity is Mg2+ dependent. It is a relatively thermostable protein.
One unit will release 1.0 μmole of inorganic orthophosphate per minute at pH 9 at 25 °C.
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Directed evolution of glycopeptides using mRNA display
Horiya S, et al.
Methods in Enzymology, 597, 83-141 (2017)
Structure and function analysis of Escherichia coli inorganic pyrophosphatase: is a hydroxide ion the key to catalysis?
Salminen, T, et al.
Biochemistry, 34(3), 782-791 (1995)
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
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)
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
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