ArticleAmino acids2014
A remarkable activity of human leukotriene A4 hydrolase (LTA4H) toward unnatural amino acids.
Article in Amino acids, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 24 citations in OpenAlex.
- Modulation of the 5-Lipoxygenase Pathway by Chalcogen-Containing Inhibitors of Leukotriene AInternational journal of molecular sciences · 2023Article
- Substrate-dependent modulation of the leukotriene AScientific reports · 2022Article
- Mapping the substrate specificity of the Plasmodium M1 and M17 aminopeptidases.The Biochemical journal · 2021Article
- Design of Optical-Imaging Probes by Screening of Diverse Substrate Libraries Directly in Disease-Tissue Extracts.Angewandte Chemie (International ed. in English) · 2020Article
- X-ray crystal structure and specificity of the Toxoplasma gondii ME49 TgAPN2.The Biochemical journal · 2020Article
- Feasibility and physiological relevance of designing highly potent aminopeptidase-sparing leukotriene A4 hydrolase inhibitors.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
Abstract
Leukotriene A4 hydrolase (LTA4H--EC 3.3.2.6) is a bifunctional zinc metalloenzyme, which processes LTA4 through an epoxide hydrolase activity and is also able to trim one amino acid at a time from N-terminal peptidic substrates via its aminopeptidase activity. In this report, we have utilized a library of 130 individual proteinogenic and unnatural amino acid fluorogenic substrates to determine the aminopeptidase specificity of this enzyme. We have found that the best proteinogenic amino acid recognized by LTA4H is arginine. However, we have also observed several unnatural amino acids, which were significantly better in terms of cleavage rate (k cat/K m values). Among them, the benzyl ester of aspartic acid exhibited a k cat/K m value that was more than two orders of magnitude higher (1.75 × 10(5) M(-1) s(-1)) as compared to L-Arg (1.5 × 10(3) M(-1) s(-1)). This information can be used for design of potent inhibitors of this enzyme, but may also suggest yet undiscovered functions or specificities of LTA4H.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.