The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity.
about
Limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis DCL14 belongs to a novel class of epoxide hydrolasesA second leukotriene B(4) receptor, BLT2. A new therapeutic target in inflammation and immunological disordersLeukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375.Binding of Pro-Gly-Pro at the active site of leukotriene A4 hydrolase/aminopeptidase and development of an epoxide hydrolase selective inhibitorEffect of the leukotriene A4 hydrolase aminopeptidase augmentor 4-methoxydiphenylmethane in a pre-clinical model of pulmonary emphysemaA critical role for LTA4H in limiting chronic pulmonary neutrophilic inflammationProtective effects of bestatin in the retina of streptozotocin-induced diabetic mice.Leukotriene A4 hydrolase: mapping of a henicosapeptide involved in mechanism-based inactivation.A glutathione peroxidase, intracellular peptidases and the TOR complexes regulate peptide transporter PEPT-1 in C. elegans.Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase.The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a "molecular ruler" mechanism.Structural origins for the loss of catalytic activities of bifunctional human LTA4H revealed through molecular dynamics simulations.A remarkable activity of human leukotriene A4 hydrolase (LTA4H) toward unnatural amino acidsEngagement of the S1, S1' and S2' subsites drives efficient catalysis of peptide bond hydrolysis by the M1-family aminopeptidase from Plasmodium falciparum.Leukotriene A4 hydrolase: protection from mechanism-based inactivation by mutation of tyrosine-378.Aminopeptidase B is structurally related to leukotriene-A4 hydrolase but is not a bifunctional enzyme with epoxide hydrolase activity.Leukotriene A4 hydrolase: a critical role of glutamic acid-296 for the binding of bestatin.The cytotoxic activity of Bacillus anthracis lethal factor is inhibited by leukotriene A4 hydrolase and metallopeptidase inhibitors.Glu121-Lys319 salt bridge between catalytic and N-terminal domains is pivotal for the activity and stability of Escherichia coli aminopeptidase N.The human leukotriene A4 hydrolase gene is expressed in two alternatively spliced mRNA forms.A tyrosine residue essential for catalytic activity in aminopeptidase A.
P2860
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P2860
The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity.
description
1994 nî lūn-bûn
@nan
1994 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
The bifunctional enzyme leukot ...... gh efficiency and specificity.
@ast
The bifunctional enzyme leukot ...... gh efficiency and specificity.
@en
The bifunctional enzyme leukot ...... gh efficiency and specificity.
@nl
type
label
The bifunctional enzyme leukot ...... gh efficiency and specificity.
@ast
The bifunctional enzyme leukot ...... gh efficiency and specificity.
@en
The bifunctional enzyme leukot ...... gh efficiency and specificity.
@nl
prefLabel
The bifunctional enzyme leukot ...... gh efficiency and specificity.
@ast
The bifunctional enzyme leukot ...... gh efficiency and specificity.
@en
The bifunctional enzyme leukot ...... gh efficiency and specificity.
@nl
P2093
P1476
The bifunctional enzyme leukot ...... igh efficiency and specificity
@en
P2093
F A Fitzpatrick
J K Gierse
P304
11269-11273
P407
P577
1994-04-01T00:00:00Z