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Literature summary for 3.1.8.2 extracted from

  • Hartleib, J.; Ruterjans, H.
    Insights into the reaction mechanism of the diisopropyl fluorophosphatase from Loligo vulgaris by means of kinetic studies, chemical modification and site-directed mutagenesis (2001), Biochim. Biophys. Acta, 1546, 312-324.
    View publication on PubMed
Search for more literature for 3.1.8.2

Cloned(Commentary)

Cloned (Comment) Organism
-
 Loligo vulgaris

Protein Variants

Protein Variants Comment Organism
H181N 20% loss of activity in comparison to wild-type enzyme Loligo vulgaris
H219N no effect on catalytic activity Loligo vulgaris
H224N 115% activity in comparison to wild-type enzyme Loligo vulgaris
H248N no effect on catalytic activity Loligo vulgaris
H274N slight loss of activity in comparison to wild-type enzyme using pH Stat measurements, no alteration is observed with fluoride assay Loligo vulgaris
H287N 96% loss of activity in comparison to wild-type enzyme Loligo vulgaris
additional information chemical modification of Tyr, Cys, Arg, Lys, Glu and Asp, this residues are not critical for catalysis Loligo vulgaris

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information effects of pH, temperature and ionic strength on KM are studied Loligo vulgaris

Organism

Organism UniProt Comment Textmining
Loligo vulgaris
-
-
-

Reaction

Reaction Comment Organism Reaction ID
diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride catalytic mechanism, H287 is required for catalytic activity Loligo vulgaris
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 pH dependence of the specific activity of the mutant H287N Loligo vulgaris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diisopropyl fluorophosphate + H2O
-
 Loligo vulgaris diisopropyl phosphate + fluoride
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
208
-
 diisopropyl fluorophosphate pH 8, 35°C, effects of pH, temperature and ionic strength on kcat are studied Loligo vulgaris

pH Range

pH Minimum pH Maximum Comment Organism
6 9 the effect of pH 6.0-9.0 on kinetic constants kcat and KM is studied, KM shows no perceivable dependence on pH within this pH range, kcat increases with pH to a limiting value at pH 8.0 Loligo vulgaris