Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.6.1.1 extracted from

  • Rodina, E.V.; Vorobyeva, N.N.; Kurilova, S.A.; Belenikin, M.S.; Fedorova, N.V.; Nazarova, T.I.
    ATP as effector of inorganic pyrophosphatase of Escherichia coli. Identification of the binding site for ATP (2007), Biochemistry (Moscow), 72, 93-99.
    View publication on PubMed
Search for more literature for 3.6.1.1

Activating Compound

Activating Compound Comment Organism Structure
ATP ATP activates hydrolysis of MgPPi by E-PPase, molecular docking and kinetic analysis involving Lys112 and Lys115, activation mechanism, and regulatory function of ATP, modelling, overview Escherichia coli
additional information no activation by ADP and AMP Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Ca2+-diphosphate nonhydrolyzable substrate analogue Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic analysis of wild-type and mutant enzymes, Mg2+ binding kinetics, overview Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
diphosphate + H2O Escherichia coli
-
 2 phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diphosphate + H2O
-
 Escherichia coli 2 phosphate
-
 ?
diphosphate + H2O residues Arg43, Lys148, and Lys115 are involved in binding of diphosphate Escherichia coli 2 phosphate
-
 ?

Synonyms

Synonyms Comment Organism
E-PPase
-
 Escherichia coli
inorganic pyrophosphatase
-
 Escherichia coli
PPase
-
 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7.5 assay at Escherichia coli