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Literature summary extracted from

  • Dayal, P.V.; Singh, H.; Busenlehner, L.S.; Ellis, H.R.
    Exposing the alkanesulfonate monooxygenase protein-protein interaction sites (2015), Biochemistry, 54, 7531-7538 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.14.14.5 D251A/D252A/E253A mutation of conserved charged amino acids, 4fold decrease in kcat/Km value Escherichia coli
1.14.14.5 DELTA251-261 deletion of alpha-helix containing conserved charged amino acids, complete loss of activity Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.14.5 0.043
-
octanesulfonate wild-type, pH 7.5, 25°C Escherichia coli
1.14.14.5 0.157
-
octanesulfonate mutant D251A/D252A/E253A, pH 7.5, 25°C Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.5 Escherichia coli P80645
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.5 octanesulfonate + FMNH2 + O2
-
Escherichia coli octanal + FMN + sulfite + H2O
-
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Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.14.5 0.85
-
octanesulfonate mutant D251A/D252A/E253A, pH 7.5, 25°C Escherichia coli
1.14.14.5 0.88
-
octanesulfonate wild-type, pH 7.5, 25°C Escherichia coli

General Information

EC Number General Information Comment Organism
1.14.14.5 physiological function optimal transfer of reduced flavin from NADPH-dependent FMN reductase SsuE to SsuD requires defined protein-protein interactions, but diffusion can occur under specified conditions. A SsuD variant containing substitutions of charged residues shows a 4fold decrease in coupled assays that include SsuE to provide reduced FMN, but there is no activity observed with an SsuD variant containing a deletion of the alpha-helix containing conserved charged amino acids Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.14.14.5 0.005
-
octanesulfonate mutant D251A/D252A/E253A, pH 7.5, 25°C Escherichia coli
1.14.14.5 0.02
-
octanesulfonate wild-type, pH 7.5, 25°C Escherichia coli