(Q24314473)

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Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design

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Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design (English)

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Leukotriene A4 hydrolase

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GOA release 2020-03-11

peptide catabolic process

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GOA release 2020-03-11

3

object named as

Bernard-Pierre Roques

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Marie-Claude Fournié-Zaluski

4

object named as

Marie-Claude Fournié-Zaluski

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Marjolein M G M Thunnissen

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object named as

Marjolein M G M Thunnissen

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author name string

Fredrik Tholander

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Ayumo Muroya

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Jesper Z Haeggström

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language of work or name

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publication date

22 September 2008

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Chemistry and Biology

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15

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9

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920-9

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Analysis of zinc binding sites in protein crystal structures

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Making optimal use of empirical energy functions: force-field parameterization in crystal space

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Assay for rapid analysis of the tri-peptidase activity of LTA4 hydrolase

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Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase

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Accurate determination of rate constants of very slow, tight-binding competitive inhibitors by numerical solution of differential equations, independently of precise knowledge of the enzyme concentration

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XtalView/Xfit--A versatile program for manipulating atomic coordinates and electron density

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Quantitative analysis of the time courses of enzyme-catalyzed reactions

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MOPAC: a semiempirical molecular orbital program

1 reference

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Leukotriene A4 hydrolase, a bifunctional enzyme. Distinction of leukotriene A4 hydrolase and aminopeptidase activities by site-directed mutagenesis at Glu-297

1 reference

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Kinetics of slow and tight-binding inhibitors

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Fast empirical pKa prediction by Ewald summation.

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On the size of the active site in proteases. I. Papain

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Structural basis of the action of thermolysin and related zinc peptidases

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Study of asparagine 353 in aminopeptidase A: characterization of a novel motif (GXMEN) implicated in exopeptidase specificity of monozinc aminopeptidases.

1 reference

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Arazoformyl dipeptide substrates for thermolysin. Confirmation of a reverse protonation catalytic mechanism

1 reference

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Characterization of Glu350 as a critical residue involved in the N-terminal amine binding site of aminopeptidase N (EC 3.4.11.2): insights into its mechanism of action

1 reference

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Recent Advances in Zinc Enzymology

1 reference

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Phosphinic derivatives as new dual enkephalin-degrading enzyme inhibitors: synthesis, biological properties, and antinociceptive activities

1 reference

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Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation

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Substrate recognition strategy for botulinum neurotoxin serotype A.

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Leukotriene A4 hydrolase: a critical role of glutamic acid-296 for the binding of bestatin

1 reference

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Binding to thermolysin of phenolate-containing inhibitors necessitates a revised mechanism of catalysis

1 reference

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Mutational analysis of the active site of human insulin-regulated aminopeptidase

1 reference

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A smooth particle mesh Ewald method

1 reference

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Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375.

1 reference

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Leukotriene A4 hydrolase: determination of the three zinc-binding ligands by site-directed mutagenesis and zinc analysis

1 reference

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Leukotriene A4 hydrolase: abrogation of the peptidase activity by mutation of glutamic acid-296

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Aminophosphinic inhibitors as transition state analogues of enkephalin-degrading enzymes: a class of central analgesics

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The role of histidine 231 in thermolysin-like enzymes. A site-directed mutagenesis study

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Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms

1 reference

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Leukotriene A4 hydrolase, insights into the molecular evolution by homology modeling and mutational analysis of enzyme from Saccharomyces cerevisiae

1 reference

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Leukotriene A4 hydrolase/aminopeptidase, the gatekeeper of chemotactic leukotriene B4 biosynthesis

1 reference

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MEROPS: the peptidase database.

1 reference

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Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants

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Refinement of macromolecular structures by the maximum-likelihood method

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Evidence for a catalytic role of tyrosine 383 in the peptidase reaction of leukotriene A4 hydrolase

1 reference

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