1.14.14.80: long-chain fatty acid omega-monooxygenase
This is an abbreviated version!
For detailed information about long-chain fatty acid omega-monooxygenase, go to the full flat file.
Word Map on EC 1.14.14.80
-
1.14.14.80
-
peroxisome
-
arachidonic
-
20-hete
-
lauric
-
20-hydroxyeicosatetraenoic
-
clofibrate
-
omega-hydroxylase
-
cyp2c11
-
omega-hydroxylation
-
proliferators
-
cyp3a1
-
pparalpha
-
epoxyeicosatrienoic
-
ethoxyresorufin
-
cyp2j3
-
ja-ile
-
sporopollenin
-
interlobar
-
cyp94b3
-
clofibrate-inducible
-
omega-1
-
ciprofibrate
-
medicine
- 1.14.14.80
- peroxisome
-
arachidonic
- 20-hete
-
lauric
-
20-hydroxyeicosatetraenoic
- clofibrate
-
omega-hydroxylase
- cyp2c11
-
omega-hydroxylation
- proliferators
- cyp3a1
- pparalpha
-
epoxyeicosatrienoic
-
ethoxyresorufin
- cyp2j3
-
ja-ile
-
sporopollenin
-
interlobar
- cyp94b3
-
clofibrate-inducible
- omega-1
- ciprofibrate
- medicine
Reaction
Synonyms
At1g69500, At2g27690, CYP4A, CYP4A1, CYP4A11, CYP4A14, CYP4A2, CYP4A3, CYP4A8, CYP4V2, CYP52-E3, CYP52-M1, CYP52-N1, CYP52E3, CYP52M1, CYP52N1, CYP704B1, CYP86A, CYP86A1, CYP86A33, CYP94C1, cytochrome P450 4A11, cytochrome P450 704B1, cytochrome P450 86A1, EC 1.14.13.205, Fatty acid omega-hydroxylase, Lauric acid omega-hydroxylase, omega-hydroxylase, P450 4A11
ECTree
1.14.14.80 long-chain fatty acid omega-monooxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.14.14.80 - long-chain fatty acid omega-monooxygenase
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
K276T
S353G
W126R
additional information
K276T
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
S353G
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
W126R
site-directed mutagenesis, the mutant W126R variant cannot be expressed in Escherichia coli.
additional information
construction of two complementary chimera between isoforms CYP4A2-CYP4A3 fused at residue 119 (CYP4A2) and 122 (CYP4A3). The chimera in which the first 119 amino acids are from CYP4A2 indicates that the first 120 amino acids control the substrate specificity. The chimera in which the first 122 amino acids are from CYP4A3 is inactive due to a defect in electron transfer to the heme group
additional information
construction of two complementary chimera between isoforms CYP4A2-CYP4A3 fused at residue 119 (CYP4A2) and 122 (CYP4A3). The chimera in which the first 119 amino acids are from CYP4A2 indicates that the first 120 amino acids control the substrate specificity. The chimera in which the first 122 amino acids are from CYP4A3 is inactive due to a defect in electron transfer to the heme group
additional information
construction of two complementary chimera between isoforms CYP4A2-CYP4A3 fused at residue 119 (CYP4A2) and 122 (CYP4A3). The chimera in which the first 119 amino acids are from CYP4A2 indicates that the first 120 amino acids control the substrate specificity. The chimera in which the first 122 amino acids are from CYP4A3 is inactive due to a defect in electron transfer to the heme group
additional information
construction of two complementary chimera between isoforms CYP4A2-CYP4A3 fused at residue 119 (CYP4A2) and 122 (CYP4A3). The chimera in which the first 119 amino acids are from CYP4A2 indicates that the first 120 amino acids control the substrate specificity. The chimera in which the first 122 amino acids are from CYP4A3 is inactive due to a defect in electron transfer to the heme group
