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Literature summary for 3.1.3.48 extracted from

  • Tsuruta, H.; Tamura, J.; Yamagata, H.; Aizono, Y.
    Specification of amino acid residues essential for the catalytic reaction of cold-active protein-tyrosine phosphatase of a psychrophile, Shewanella sp. (2004), Biosci. Biotechnol. Biochem., 68, 440-443.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D112N GST fusion protein, no enzymic activity Shewanella sp.
D115N GST fusion protein, no enzymic activity Shewanella sp.
D76N GST fusion protein, no enzymic activity Shewanella sp.
H148N GST fusion protein, no enzymic activity Shewanella sp.
H44N GST fusion protein, acitivity slightly lower than wild-type Shewanella sp.
H78N GST fusion protein, 8fold reduction of activity compared to wild-type Shewanella sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.53
-
4-nitrophenyl phosphate mutant H44N, GST fusion protein Shewanella sp.
0.58
-
4-nitrophenyl phosphate wild-type, GST fusion protein Shewanella sp.

Organism

Organism UniProt Comment Textmining
Shewanella sp.
-
-
-

Reaction

Reaction Comment Organism Reaction ID
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate H148 acts as a general acid catalyst, D115 assists the protonation of the leaving group of a substrate, and D76 and D112 are involved in binding of magnesium ions Shewanella sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
Shewanella sp. 4-nitrophenol + phosphate
-
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