1.14.14.47: nitric-oxide synthase (flavodoxin)
This is an abbreviated version!
For detailed information about nitric-oxide synthase (flavodoxin), go to the full flat file.
Word Map on EC 1.14.14.47
-
1.14.14.47
-
familia
-
latino
-
pacientes
-
farmworker
-
grupos
-
condom
-
analysis
- 1.14.14.47
-
familia
-
latino
-
pacientes
-
farmworker
-
grupos
-
condom
- analysis
Reaction
2 L-arginine + 2 reduced flavodoxin + 2 O2 = 2 Nomega-hydroxy-L-arginine + 2 oxidized flavodoxin + 2 H2O
Synonyms
bNOS, GK1676, nitric oxide synthetase, NO synthase, NOS, SANOS, YumC
ECTree
1.14.14.47 nitric-oxide synthase (flavodoxin)Advanced search results
results (
results (Engineering
Engineering on EC 1.14.14.47 - nitric-oxide synthase (flavodoxin)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
P332G
mutation at the center of the dimer interface, mutant displays significantly more monomer content than wild-type
P332G/A333S
mutation at the center of the dimer interface, both mutations are necessary to mimic interactions at the dimer interface displayed by the mouse enzyme
W66F
W66H
W66L
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
W66Y
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
P332G
-
mutation at the center of the dimer interface, mutant displays significantly more monomer content than wild-type
-
P332G/A333S
-
mutation at the center of the dimer interface, both mutations are necessary to mimic interactions at the dimer interface displayed by the mouse enzyme
-
W66F
-
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
-
W66H
-
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
-
W66L
-
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
-
W66Y
-
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
-
L356R
mutation Lys-356 (Bacillus subtilis NOS) to Arg-365 (gsNOS) substitution alters the conformation of a conserved Asp carboxylate, resulting in movement of an Ile residue toward the heme
additional information
W66F
-
mutation changes midpoint potential from -361 mV for wild-type to -427 mV. Mutant displays 2.5fold lower activity when reaction is supported by flavoproteins or NADPH instead of tetrahydrofolate
W66F
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
W66H
-
mutation changes midpoint potential from -361 mV for wild-type to -302 mV. Activity is similar to wild-type
W66H
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates
additional information
a chimera between enzyme and flavodoxin YkuN is 8fold more active tan wild-type. Adding excess amounts of YkuN does not significantly alter activity
additional information
the proximal hydrogen bond modulation at residue W66 can selectively decrease or increase the electron donating properties of the proximal thiolate. The modulation controls the sigma-competition between distal and proximal ligands and controls the stability of various NOS intermediates. A fine tuning of the electron donation by the proximal ligand is required to allow at the same time oxygen activation and to prevent uncoupling reactions
additional information
-
the proximal hydrogen bond modulation at residue W66 can selectively decrease or increase the electron donating properties of the proximal thiolate. The modulation controls the sigma-competition between distal and proximal ligands and controls the stability of various NOS intermediates. A fine tuning of the electron donation by the proximal ligand is required to allow at the same time oxygen activation and to prevent uncoupling reactions
-
additional information
-
a chimera between enzyme and flavodoxin YkuN is 8fold more active tan wild-type. Adding excess amounts of YkuN does not significantly alter activity
-
