Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates (Q24336410)

peptide catabolic process

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

Peter C Rudberg

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Fredrik Tholander

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Martina Andberg

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Marjolein M G M Thunnissen

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Jesper Z Haeggström

Journal of Biological Chemistry

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language of work or name

English

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publication date

25 June 2004

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published in

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volume

279

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issue

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page(s)

27376-82

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Isomers of leukotriene B4 possess different biological potencies

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Analogs of leukotriene B4: effects of modification of the hydroxyl groups on leukocyte aggregation and binding to leukocyte leukotriene B4 receptors

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Chemical modification of leukotriene A4 hydrolase. Indications for essential tyrosyl and arginyl residues at the active site

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Leukotriene B4 receptor BLT1 mediates early effector T cell recruitment

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Leukotriene A4 hydrolase, mutation of tyrosine 378 allows conversion of leukotriene A4 into an isomer of leukotriene B4

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7 January 2021

Mutation of tyrosine 383 in leukotriene A4 hydrolase allows conversion of leukotriene A4 into 5S,6S-dihydroxy-7,9-trans-11,14-cis-eicosatetraenoic acid. Implications for the epoxide hydrolase mechanism

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

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7 January 2021

Identifiers

DOI

10.1074/JBC.M401031200

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

15078870

1 reference

Consolidated OpenCitations Corpus – April 2017