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Literature summary extracted from

  • Watschinger, K.; Fuchs, J.E.; Yarov-Yarovoy, V.; Keller, M.A.; Golderer, G.; Hermetter, A.; Werner-Felmayer, G.; Hulo, N.; Werner, E.R.
    Catalytic residues and a predicted structure of tetrahydrobiopterin-dependent alkylglycerol mono-oxygenase (2012), Biochem. J., 443, 279-286.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.16.5 expressed in CHO-K1 cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.14.16.5 C231A the mutant enzyme activity is not significantly different from wild type Homo sapiens
1.14.16.5 C397A the mutant enzyme activity is not significantly different from wild type Homo sapiens
1.14.16.5 D153A the mutant enzyme activity is not significantly different from wild type Homo sapiens
1.14.16.5 D384A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
1.14.16.5 E137A the mutation leads to an 18fold increase in the Michaelis-Menten constant for tetrahydrobiopterin. The mutant has an approximately 5fold lower affinity for iron Homo sapiens
1.14.16.5 E152A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
1.14.16.5 E203A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
1.14.16.5 E212A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
1.14.16.5 H189A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
1.14.16.5 H220A the mutant enzyme activity is not significantly different from wild type Homo sapiens
1.14.16.5 Q146A the mutant enzyme activity is not significantly different from wild type Homo sapiens
1.14.16.5 Q166A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
1.14.16.5 Q191A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
1.14.16.5 Q197A the mutant has activity of less than 5% of that of the wild type Homo sapiens
1.14.16.5 R396A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
1.14.16.5 Y174A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
1.14.16.5 Y230A the mutant enzyme activity is not significantly different from wild type Homo sapiens
1.14.16.5 Y338A the mutant has activity of less than 5% of that of the wild type Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.16.5 Phenanthroline competitive inhibitor Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.16.5 0.00183
-
 tetrahydrobiopterin mutant enzyme E137A, at pH 8.5 and 37°C Homo sapiens
1.14.16.5 0.0335
-
 tetrahydrobiopterin wild type enzyme, at pH 8.5 and 37°C Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.16.5 60000
-
 x * 60000, SDS-PAGE Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.14.16.5 Homo sapiens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.16.5 1-O-pyrenedecyl-sn-glycerol + tetrahydrobiopterin + O2
-
 Homo sapiens ? + dihydrobiopterin + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.16.5 ? x * 60000, SDS-PAGE Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.14.16.5 alkylglycerol mono-oxygenase
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.16.5 tetrahydrobiopterin dependent on Homo sapiens

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.14.16.5 0.00069
-
 wild type enzyme, at pH 8.5 and 37°C Homo sapiens Phenanthroline
1.14.16.5 0.00341
-
 mutant enzyme E137A, at pH 8.5 and 37°C Homo sapiens Phenanthroline