IUPHAR/BPS Guide to Pharmacology CITE
https://doi.org/10.2218/gtopdb/F917/2023.1

S33: Prolyl aminopeptidase in GtoPdb v.2023.1



Stephen P.H. Alexander1, Patrick Doherty2 and Christopher J. Fowler3
  1. University of Nottingham, UK
  2. King's College London, UK
  3. University Hospital of Umeå, Sweden


Abstract

Peptidase family S33 contains mainly exopeptidases that act at the N-terminus of peptides.

Contents

This is a citation summary for S33: Prolyl aminopeptidase in the Guide to Pharmacology database (GtoPdb). It exists purely as an adjunct to the database to facilitate the recognition of citations to and from the database by citation analyzers. Readers will almost certainly want to visit the relevant sections of the database which are given here under database links.

GtoPdb is an expert-driven guide to pharmacological targets and the substances that act on them. GtoPdb is a reference work which is most usefully represented as an on-line database. As in any publication this work should be appropriately cited, and the papers it cites should also be recognized. This document provides a citation for the relevant parts of the database, and also provides a reference list for the research cited by those parts. For further details see [3].

Please note that the database version for the citations given in GtoPdb are to the most recent preceding version in which the family or its subfamilies and targets were substantially changed. The links below are to the current version. If you need to consult the cited version, rather than the most recent version, please contact the GtoPdb curators.

Database links

S33: Prolyl aminopeptidase
https://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=917
    Enzymes
            lipase, gastric
            https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2626
            protein phosphatase methylesterase 1
            https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2875
            MAGL(Monoacylglycerol lipase)
            https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=1399

References

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  2. Bachovchin DA, Koblan LW, Wu W, Liu Y, Li Y, Zhao P, Woznica I, Shu Y, Lai JH and Poplawski SE et al.. (2014) A high-throughput, multiplexed assay for superfamily-wide profiling of enzyme activity. Nat Chem Biol 10: 656-63 [PMID:24997602]
  3. Buneman P, Christie G, Davies JA, Dimitrellou R, Harding SD, Pawson AJ, Sharman JL and Wu Y. (2020) Why data citation isn't working, and what to do about it Database 2020 [PMID:32367113]
  4. Chang JW, Niphakis MJ, Lum KM, Cognetta 3rd AB, Wang C, Matthews ML, Niessen S, Buczynski MW, Parsons LH and Cravatt BF. (2012) Highly selective inhibitors of monoacylglycerol lipase bearing a reactive group that is bioisosteric with endocannabinoid substrates. Chem Biol 19: 579-88 [PMID:22542104]
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  11. Niphakis MJ, Cognetta 3rd AB, Chang JW, Buczynski MW, Parsons LH, Byrne F, Burston JJ, Chapman V and Cravatt BF. (2013) Evaluation of NHS carbamates as a potent and selective class of endocannabinoid hydrolase inhibitors. ACS Chem Neurosci 4: 1322-32 [PMID:23731016]
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  13. Petersen A, Benz J, Grether U, Hornsperger B, Kocer B, Kuhn B, Richter H, Tsuchiya S, Qui Y and Chen R. (2019) Octahydropyrido[1,2-alpha]pyrazines as magl inhibitors Patent number: WO2019134985A1. Assignee: Hoffmann-La Roche. Priority date: 08/01/2018. Publication date: 11/07/2019.
  14. Wyatt RM, Fraser I, Welty N, Lord B, Wennerholm M, Sutton S, Ameriks MK, Dugovic C, Yun S and White A et al.. (2020) Pharmacologic Characterization of JNJ-42226314, [1-(4-Fluorophenyl)indol-5-yl]-[3-[4-(thiazole-2-carbonyl)piperazin-1-yl]azetidin-1-yl]methanone, a Reversible, Selective, and Potent Monoacylglycerol Lipase Inhibitor. J Pharmacol Exp Ther 372: 339-353 [PMID:31818916]
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