1.13.11.48: 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase
This is an abbreviated version!
For detailed information about 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase, go to the full flat file.
Reaction
Synonyms
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase, 1H-3-hydroxy-4-oxoquinaldine oxygenase, 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase, HOD, HodC, More
ECTree
1.13.11.48 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenaseAdvanced search results
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results (Engineering
Engineering on EC 1.13.11.48 - 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H251A
C69S
C69S/H251A
-
site-directed mutagenesis, the mutant is catalytically inactive owing to the Ala substitution of the essential residue His251
E224A/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
F219Y
does not affect the kinetic parameters of the enzyme
F219Y/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
H102Q
Km for the heteroaromatic substrate is increased only 2.8fold, and kcat is reduced 2.3fold
H102Q/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
S101A
about 21fold increase in the Km for the organic substrate
S101A/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
S220N
does not drastically influence the kinetic parameters of the enzyme for the organic substrate, but it causes a 3.5fold decrease in Km for O2 and a 6.2fold decrease in kcat for O2
S220N/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
Y196A/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
Y196K/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
Y196R/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
C69S
H102Q
-
Km for the heteroaromatic substrate is increased only 2.8fold, and kcat is reduced 2.3fold
-
S101A
-
about 21fold increase in the Km for the organic substrate
-
C69S
-
site-directed mutagenesis, the mutant has catalytic properties that are identical to those of wild-type HOD
-
C69S/H251A
-
site-directed mutagenesis, the mutant is catalytically inactive owing to the Ala substitution of the essential residue His251
-
C69S
C69S/H251A
-
site-directed mutagenesis, the mutant is catalytically inactive owing to the Ala substitution of the essential residue His251
-
H102Q
-
Km for the heteroaromatic substrate is increased only 2.8fold, and kcat is reduced 2.3fold
-
S101A
-
about 21fold increase in the Km for the organic substrate
-
C69S
catalytical properties unchanged, mutant enzyme with hexahistidine tag at N-terminus and amino acid exchange influencing disulfide binding between C37 and C184
C69S
site-directed mutagenesis, the mutant has catalytic properties that are identical to those of wild-type HOD
C69S
-
site-directed mutagenesis, the mutant has catalytic properties that are identical to those of wild-type HOD
C69S
site-directed mutagenesis, thermodynamic analysis of denaturant-induced unfolding of the mutant compared to the wild-type enzyme, overview
C69S
-
catalytical properties unchanged, mutant enzyme with hexahistidine tag at N-terminus and amino acid exchange influencing disulfide binding between C37 and C184
-
C69S
-
site-directed mutagenesis, the mutant has catalytic properties that are identical to those of wild-type HOD
-
C69S
-
site-directed mutagenesis, the mutant has catalytic properties that are identical to those of wild-type HOD
-
C69S
-
site-directed mutagenesis, thermodynamic analysis of denaturant-induced unfolding of the mutant compared to the wild-type enzyme, overview
-
