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Literature summary for 1.14.13.6 extracted from

  • Ryerson, C.C.; Walsh, C.
    The stereochemistry of NADH utilization by the flavoenzyme monooxygenase orcinol hydroxylase (1979), J. Biol. Chem., 254, 4349-4351.
    View publication on PubMed
Search for more literature for 1.14.13.6

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.026
-
 orcinol
-
 Pseudomonas putida
0.17
-
 NADH
-
 Pseudomonas putida
0.17
-
 3-cresol
-
 Pseudomonas putida
0.22
-
 resorcinol
-
 Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
 01
-
Pseudomonas putida 1
-
 01
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
37
-
-
 Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-cresol + NADH + O2 20 to 70% coupled in various assays Pseudomonas putida 3-methylcatechol + NAD+ + H2O
-
 ?
3-cresol + NADH + O2 20 to 70% coupled in various assays Pseudomonas putida 1 3-methylcatechol + NAD+ + H2O
-
 ?
orcinol + NADH + O2
-
 Pseudomonas putida 2,3,5-trihydroxytoluene + NAD+ + H2O
-
 ?
orcinol + NADH + O2
-
 Pseudomonas putida 1 2,3,5-trihydroxytoluene + NAD+ + H2O
-
 ?
resorcinol + NADH + O2 the enzyme processes resorcinol to hydroxylated product 66% of the time Pseudomonas putida hydroxyquinol + NAD+ + H2O
-
 ?
resorcinol + NADH + O2 the enzyme processes resorcinol to hydroxylated product 66% of the time Pseudomonas putida 1 hydroxyquinol + NAD+ + H2O
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
 assay at Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
NADH 4R stereospecificity with respect to dihydronicotinamide oxidation with the substrates: orcinol, resorcinol and m-cresol Pseudomonas putida