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Literature summary for 1.14.16.5 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)

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

Protein Variants

Protein Variants Comment Organism
C231A the mutant enzyme activity is not significantly different from wild type Homo sapiens
C397A the mutant enzyme activity is not significantly different from wild type Homo sapiens
D153A the mutant enzyme activity is not significantly different from wild type Homo sapiens
D384A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
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
E152A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
E203A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
E212A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
H189A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
H220A the mutant enzyme activity is not significantly different from wild type Homo sapiens
Q146A the mutant enzyme activity is not significantly different from wild type Homo sapiens
Q166A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
Q191A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
Q197A the mutant has activity of less than 5% of that of the wild type Homo sapiens
R396A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
Y174A the mutant has significantly reduced, but clearly detectable, enzyme activity Homo sapiens
Y230A the mutant enzyme activity is not significantly different from wild type Homo sapiens
Y338A the mutant has activity of less than 5% of that of the wild type Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Phenanthroline competitive inhibitor Homo sapiens

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
alkylglycerol mono-oxygenase
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
tetrahydrobiopterin dependent on Homo sapiens

IC50 Value

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