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Literature summary for 3.1.3.16 extracted from

  • McWhirter, C.; Lund, E.A.; Tanifum, E.A.; Feng, G.; Sheikh, Q.I.; Hengge, A.C.; Williams, N.H.
    Mechanistic study of protein phosphatase-1 (PP1), a catalytically promiscuous enzyme (2008), J. Am. Chem. Soc., 130, 13673-13682.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain DH5alpha Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ 1 mM, Mn2+ is the most effective cofactor Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl methylphosphonate + H2O
-
Homo sapiens 4-nitrophenol + methylphosphonate
-
?
4-nitrophenyl phosphate + H2O
-
Homo sapiens 4-nitrophenol + phosphate
-
?
additional information little activity is observed with 4-nitrophenyl sulfate and 4-nitrophenyl thiophosphate Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
PP-1
-
Homo sapiens
PP1gamma catalytic subunit of PP1 Homo sapiens
protein phosphatase 1
-
Homo sapiens