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Literature summary for 3.1.1.2 extracted from

  • Bajaj, P.; Aggarwal, G.; Tripathy, R.K.; Pande, A.H.
    Interplay between amino acid residues at positions 192 and 115 in modulating hydrolytic activities of human paraoxonase 1 (2014), Biochimie, 105, 202-210.
    View publication on PubMed
Search for more literature for 3.1.1.2

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
H115W mutation results in decrease in the affinity and the rate of catalysis of the enzyme Homo sapiens
H115W/R192K partially restores the phenyl acetate-hydrolyzing activity of mutant H115W Homo sapiens
H115W/R192Q complete loss of phenyl acetate-hydrolyzing activity Homo sapiens
additional information the presence of a (His)6-tag at the N-terminus and at both the N- and C-termini decreases the enzymatic activity of the recombinant protein. The activity is unaffected by the presence of a (His)6-tag at its C-terminus Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1
-
 phenyl acetate wild-type, pH 8.0, 25°C Homo sapiens
4.1
-
 phenyl acetate mutant H115W/R192K, pH 8.0, 25°C Homo sapiens
10.8
-
 phenyl acetate mutant H115W, pH 8.0, 25°C Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 x * 40000, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P27169
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phenyl acetate + H2O
-
 Homo sapiens phenol + acetate
-
 ?

Subunits

Subunits Comment Organism
? x * 40000, SDS-PAGE Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
525.8
-
 phenyl acetate mutant H115W, pH 8.0, 25°C Homo sapiens
759
-
 phenyl acetate mutant H115W/R192K, pH 8.0, 25°C Homo sapiens
843.6
-
 phenyl acetate wild-type, pH 8.0, 25°C Homo sapiens

General Information

General Information Comment Organism
physiological function the presence of a particular amino acid residue at position 192 differentially alters the effect of the H115W substitution, and the H115 residue is not always needed for the lactonase and arylesterase activities of the enzyme. The amino acid residues at position 192 and 115 act in conjunction in modulating the hydrolytic activities of the enzyme Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
48.6
-
 phenyl acetate mutant H115W, pH 8.0, 25°C Homo sapiens
185.6
-
 phenyl acetate mutant H115W/R192K, pH 8.0, 25°C Homo sapiens
401.7
-
 phenyl acetate wild-type, pH 8.0, 25°C Homo sapiens