1.13.11.38: 1-hydroxy-2-naphthoate 1,2-dioxygenase
This is an abbreviated version!
For detailed information about 1-hydroxy-2-naphthoate 1,2-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.38
-
1.13.11.38
-
nocardioides
-
gentisate
-
salicylate
-
phenanthrene
-
ring-cleaving
-
salicylatoxidans
-
pseudaminobacter
-
phenanthrene-degrading
-
2-carboxybenzaldehyde
-
alcaligenes
-
sphingomonas
-
unobserved
-
extradiol-type
- 1.13.11.38
- nocardioides
- gentisate
- salicylate
- phenanthrene
-
ring-cleaving
- salicylatoxidans
-
pseudaminobacter
-
phenanthrene-degrading
- 2-carboxybenzaldehyde
- alcaligenes
- sphingomonas
-
unobserved
-
extradiol-type
Reaction
Synonyms
1-H2NA dioxygenase, 1-HNDO, 1-hydroxy-2-naphthoate 1,2-dioxygenase, 1-hydroxy-2-naphthoate dioxygenase, 1-hydroxy-2-naphthoate-degrading enzyme, 1-hydroxy-2-naphthoic acid dioxygenase, 1H2NDO, Diox1, Diox2, oxygenase, 1-hydroxy-2-naphthoate di-, Sphe3 1-H2NA dioxygenase
ECTree
Advanced search results
Engineering
Engineering on EC 1.13.11.38 - 1-hydroxy-2-naphthoate 1,2-dioxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
A85H
-
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate than the wild-type enzyme and no more activity with gentisate. substitution of Ala85 with a histidine residue caused significant changes in the orientation of the loop containing this residue which is involved in the active site closing upon substrate binding. In SDO A85H this specific loop shifts away from the active site and thus opens the cavity favoring the binding of bulkier substrates. Since this loop also interacts with the N-terminal residues of the vicinal subunit, the structure and packing of the holoenzyme might be also affected.
L38Q
-
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate than the wild-type enzyme
W104Y
-
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows increased catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate and to the wild-type enzyme. W104Y SDO mutant exhibits reduced reaction rates for all substrates
A85H
-
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate than the wild-type enzyme and no more activity with gentisate. substitution of Ala85 with a histidine residue caused significant changes in the orientation of the loop containing this residue which is involved in the active site closing upon substrate binding. In SDO A85H this specific loop shifts away from the active site and thus opens the cavity favoring the binding of bulkier substrates. Since this loop also interacts with the N-terminal residues of the vicinal subunit, the structure and packing of the holoenzyme might be also affected.
-
L38Q
-
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate than the wild-type enzyme
-
W104Y
-
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows increased catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate and to the wild-type enzyme. W104Y SDO mutant exhibits reduced reaction rates for all substrates
-
additional information
-
generation of a 1-hydroxy-2-naphthoate 1,2-dioxygenase by single point mutation M46V of salicylate 1,2-dioxygenase, rational design of mutants, structure comparisons, overview
additional information
-
generation of a 1-hydroxy-2-naphthoate 1,2-dioxygenase by single point mutation M46V of salicylate 1,2-dioxygenase, rational design of mutants, structure comparisons, overview
-