Leukotriene A4 hydrolase: abrogation of the peptidase activity by mutation of glutamic acid-296.
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Lipoxin synthase activity of human platelet 12-lipoxygenaseLeukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substratesLeukotriene 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 inhibitorCloning and characterization of a bifunctional leukotriene A(4) hydrolase from Saccharomyces cerevisiae.Mutation of active site residues of insulin-degrading enzyme alters allosteric interactionsMolecular cloning and functional expression of a Caenorhabditis elegans aminopeptidase structurally related to mammalian leukotriene A4 hydrolases.A critical role for LTA4H in limiting chronic pulmonary neutrophilic inflammationStructure, function, and regulation of leukotriene A4 hydrolase.Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus.Structural origins for the loss of catalytic activities of bifunctional human LTA4H revealed through molecular dynamics simulations.UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism.Purification, characterization, and sequencing of an extracellular cold-active aminopeptidase produced by marine psychrophile Colwellia psychrerythraea strain 34HLeukotriene A4 hydrolase/aminopeptidase, the gatekeeper of chemotactic leukotriene B4 biosynthesis.Examination of mechanism of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) reveals unexpected role for dynamic tyrosineLeukotriene A4 hydrolase: protection from mechanism-based inactivation by mutation of tyrosine-378.Identification of glutamate residues essential for catalytic activity and zinc coordination in aminopeptidase A.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.
P2860
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P2860
Leukotriene A4 hydrolase: abrogation of the peptidase activity by mutation of glutamic acid-296.
description
article científic
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article scientifique
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articolo scientifico
@it
artigo científico
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bilimsel makale
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scientific article published on October 1992
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Leukotriene A4 hydrolase: abro ...... mutation of glutamic acid-296.
@en
Leukotriene A4 hydrolase: abro ...... mutation of glutamic acid-296.
@nl
type
label
Leukotriene A4 hydrolase: abro ...... mutation of glutamic acid-296.
@en
Leukotriene A4 hydrolase: abro ...... mutation of glutamic acid-296.
@nl
prefLabel
Leukotriene A4 hydrolase: abro ...... mutation of glutamic acid-296.
@en
Leukotriene A4 hydrolase: abro ...... mutation of glutamic acid-296.
@nl
P2093
P2860
P356
P1476
Leukotriene A4 hydrolase: abro ...... mutation of glutamic acid-296.
@en
P2093
Haeggström JZ
Wetterholm A
P2860
P304
P356
10.1073/PNAS.89.19.9141
P407
P577
1992-10-01T00:00:00Z