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Literature summary extracted from

  • Meyer, A.; Schmid, A.; Held, M.; Westphal, A.H.; Rothlisberger, M.; Kohler, H.P.E.; Van Berkel, W.J.H.; Witholt, B.
    Changing the substrate reactivity of 2-hydroxybiphenyl 3-monooxygenase from Pseudomonas azelaica HBP1 by directed evolution (2002), J. Biol. Chem., 277, 5575-5582.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.44 I244V mutant enzyme has a 30% higher specific activity with 2-sec-butylphenol, guaiacol, and 2-hydroxybiphenyl. The Km-value for guaiacol decreases with this mutant, but the Km-value for 2-hydroxybiphenyl increase Pseudomonas nitroreducens
1.14.13.44 V368A/L417F double replacement improves the efficiency of substrate hydroxylation by reducing the uncoupled oxidation of NADH. With guaiacol as substrate, the Vmax is increased and the Km-value is decreased. With 2-tert-butylphenol as substrate the turnover number is increased more than 5fold Pseudomonas nitroreducens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.44 additional information
-
 additional information Km-values for wild-type and mutant enzymes Pseudomonas nitroreducens

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.44 Pseudomonas nitroreducens
-
 HBP1
-
1.14.13.44 Pseudomonas nitroreducens HBP1
-
 HBP1
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.44 2-hydroxybiphenyl + NADH + O2
-
 Pseudomonas nitroreducens 2,3-dihydroxybiphenyl + NAD+ + H2O
-
 ?
1.14.13.44 2-hydroxybiphenyl + NADH + O2
-
 Pseudomonas nitroreducens HBP1 2,3-dihydroxybiphenyl + NAD+ + H2O
-
 ?
1.14.13.44 2-sec-butylphenol + NADH + O2
-
 Pseudomonas nitroreducens 2-sec-butylcatechol + NAD+ + H2O
-
 ?
1.14.13.44 2-sec-butylphenol + NADH + O2
-
 Pseudomonas nitroreducens HBP1 2-sec-butylcatechol + NAD+ + H2O
-
 ?
1.14.13.44 2-tert-butylphenol + NADH + O2
-
 Pseudomonas nitroreducens 1,2-dihydroxy-3-tert-butylbenzene + NAD+ + H2O
-
 ?
1.14.13.44 2-tert-butylphenol + NADH + O2
-
 Pseudomonas nitroreducens HBP1 1,2-dihydroxy-3-tert-butylbenzene + NAD+ + H2O
-
 ?
1.14.13.44 guaiacol + NADH + O2 i.e. 2-methoxyphenol Pseudomonas nitroreducens 2,3-dihydroxy-methoxybenzene + NAD+ + H2O
-
 ?
1.14.13.44 guaiacol + NADH + O2 i.e. 2-methoxyphenol Pseudomonas nitroreducens HBP1 2,3-dihydroxy-methoxybenzene + NAD+ + H2O
-
 ?
1.14.13.44 additional information Ile244 is located in the substrate binding pocket and is involved in accomodating the phenyl substituent of the phenol Pseudomonas nitroreducens ?
-
 ?
1.14.13.44 additional information Ile244 is located in the substrate binding pocket and is involved in accomodating the phenyl substituent of the phenol Pseudomonas nitroreducens HBP1 ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.13.44 additional information
-
 additional information turnover-numbers for mutant enzymes Pseudomonas nitroreducens
1.14.13.44 0.95
-
 guaiacol
-
 Pseudomonas nitroreducens
1.14.13.44 11.9
-
 2-Hydroxybiphenyl wild-type enzyme Pseudomonas nitroreducens
1.14.13.44 14.5
-
 2-sec-Butylphenol wild-type enzyme Pseudomonas nitroreducens

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.44 FAD flavoenzyme Pseudomonas nitroreducens
1.14.13.44 NADH
-
 Pseudomonas nitroreducens