3.3.2.6: leukotriene-A4 hydrolase
This is an abbreviated version!
For detailed information about leukotriene-A4 hydrolase, go to the full flat file.
Word Map on EC 3.3.2.6
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3.3.2.6
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5-lipoxygenase
-
arachidonic
-
epoxide
-
medicine
-
leukocyte
-
asthma
-
bestatin
-
chemoattractant
-
eicosanoids
-
metalloenzyme
-
flap
-
ionophore
-
alox5ap
-
tuberculous
-
transcellular
-
5-lipoxygenase-activating
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aminopeptidases
-
captopril
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lipoxins
-
pro-gly-pro
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montelukast
-
proline-glycine-proline
-
5-hete
-
zileuton
-
diagnostics
-
pharmacology
-
drug development
- 3.3.2.6
-
5-lipoxygenase
-
arachidonic
- epoxide
- medicine
- leukocyte
- asthma
- bestatin
-
chemoattractant
-
eicosanoids
-
metalloenzyme
- flap
-
ionophore
-
alox5ap
-
tuberculous
-
transcellular
-
5-lipoxygenase-activating
- aminopeptidases
- captopril
-
lipoxins
- pro-gly-pro
- montelukast
- proline-glycine-proline
-
5-hete
- zileuton
- diagnostics
- pharmacology
- drug development
Reaction
Synonyms
EH, epoxide hydrolase, hydrolase, leukotriene A4, leukotriene A(4) hydrolase, leukotriene A4 hydrolase, leukotriene A4 hydrolase/aminopeptidase, leukotriene hydrolase A4, leukotriene-A4 hydrolase, leukotriene-A4-hydrolase, LT A4 hydrolase, LTA-4 hydrolase, LTA4 hydrolase, LTA4-h, LTA4H, More
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Metals Ions
Metals Ions on EC 3.3.2.6 - leukotriene-A4 hydrolase
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Br-
-
stimulates peptidase and epoxide hydrolase activity (i.e. conversion of leukotriene A4 into leukotriene B4), SCN- most effective, followed by Cl- and Br-
Cl-
-
stimulates peptidase activity, not epoxide hydrolase activity (i.e. conversion of leukotriene A4 into leukotriene B4), SCN- most effective, followed by Cl- and Br-
Co2+
thiocyanate
-
stimulates peptidase and epoxide hydrolase activity (i.e. conversion of leukotriene A4 into leukotriene B4), SCN- most effective, followed by Cl- and Br-
Zinc
Zn2+
-
apoenzyme can be restored by addition of Co2+, peptidase activity exceeds that of enzyme reactivated with zinc
Co2+
-
apoenzyme is inactive and can be reactivated by addition of stoichiometric amounts of zinc and cobalt
-
catalytic zinc site with the signature HEXXH-(X)18-E, three zinc binding ligands: His295, His299 and Glu318
Zinc
-
catalytic zinc site with the signature HEXXH-(X)18-E, three zinc binding ligands: His295, His299 and Glu318
Zinc
the sequence that codes for the zinc-ion-binding motif is identical in the short-from and long-form enzyme mRNAs
Zinc
-
zinc protein
Zinc
-
apoenzyme is inactive and can be reactivated by addition of stoichiometric amounts of zinc and cobalt
Zinc
-
catalytic zinc site with the signature HEXXH-(X)18-E, three zinc binding ligands: His295, His299 and Glu318
Zinc
-
catalytic zinc site with the signature HEXXH-(X)18-E, three zinc binding ligands: His295, His299 and Glu318
Zinc
-
three putative zinc-binding ligands: His340, His344 and Glu363, zinc atom is catalytic and also involved in the maintenance of the structural integrity of the enzyme
Zn2+
the zinc ion is essential for both catalytic activities of LTA4H, it is coordinated by three amino acid residues (His295, His299, Glu318) located in the catalytic domain
Zn2+
zinc metalloenzyme, enzyme LTA4H folds into three domains and creates a deep cleft harboring the catalytic Zn2+ site, forming the active site with an L-shaped hydrophobic pocket deep into the protein
Zn2+
zinc metalloenzyme, enzyme LTA4H folds into three domains and creates a deep cleft harboring the catalytic Zn2+ site, forming the active site with an L-shaped hydrophobic pocket deep into the protein