Literature DB >> 12369979

Leucine aminopeptidase as a target for inhibitor design.

J Grembecka1, P Kafarski.   

Abstract

In this review we focus on the most effective and the most promising inhibitors of leucine aminopeptidase. Their binding modes to the enzyme, the attempt to explain the origin of the inhibitory activity, as well as the structure-activity relationship for some of these compounds are discussed. Besides, the structural and electronic requirements of the enzyme active site and the binding pockets, together with the specificity towards the ligands, based on the structural and kinetic data, are presented.

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Year:  2001        PMID： 12369979     DOI： 10.2174/1389557013406990

Source DB:  PubMed          Journal:  Mini Rev Med Chem        ISSN： 1389-5575            Impact factor:   3.862


  9 in total

1.  Pyrrolidine and oxazolidine ring transformations in proline and serine derivatives of α-hydroxyphosphonates induced by deoxyfluorinating reagents.

Authors:  Patrycja Kaczmarek; Magdalena Rapp; Henryk Koroniak
Journal:  RSC Adv       Date:  2018-07-06       Impact factor: 4.036

2.  Chemical target validation studies of aminopeptidase in malaria parasites using alpha-aminoalkylphosphonate and phosphonopeptide inhibitors.

Authors:  Eithne Cunningham; Marcin Drag; Pawel Kafarski; Angus Bell
Journal:  Antimicrob Agents Chemother       Date:  2008-05-05       Impact factor: 5.191

3.  Biochemical and conformational characterization of a leucine aminopeptidase from Geobacillus thermodenitrificans NG80-2.

Authors:  Fanghua Wang; Shaohua Guo; Yuanyuan Liu; Dongming Lan; Bo Yang; Yonghua Wang
Journal:  World J Microbiol Biotechnol       Date:  2012-08-28       Impact factor: 3.312

4.  Phosphonic Acid Analogues of Phenylglycine as Inhibitors of Aminopeptidases: Comparison of Porcine Aminopeptidase N, Bovine Leucine Aminopeptidase, Tomato Acidic Leucine Aminopeptidase and Aminopeptidase from Barley Seeds.

Authors:  Weronika Wanat; Michał Talma; Małgorzata Pawełczak; Paweł Kafarski
Journal:  Pharmaceuticals (Basel)       Date:  2019-09-17

Review 5.  Metallo-aminopeptidase inhibitors.

Authors:  Artur Mucha; Marcin Drag; John P Dalton; Paweł Kafarski
Journal:  Biochimie       Date:  2010-05-10       Impact factor: 4.079

6.  Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases.

Authors:  Stamatia Vassiliou; Ewelina Węglarz-Tomczak; Łukasz Berlicki; Małgorzata Pawełczak; Bogusław Nocek; Rory Mulligan; Andrzej Joachimiak; Artur Mucha
Journal:  J Med Chem       Date:  2014-09-22       Impact factor: 7.446

7.  Friedel-Crafts-type reaction of pyrene with diethyl 1-(isothiocyanato)alkylphosphonates. Efficient synthesis of highly fluorescent diethyl 1-(pyrene-1-carboxamido)alkylphosphonates and 1-(pyrene-1-carboxamido)methylphosphonic acid.

Authors:  Anna Wrona-Piotrowicz; Janusz Zakrzewski; Anna Gajda; Tadeusz Gajda; Anna Makal; Arnaud Brosseau; Rémi Métivier
Journal:  Beilstein J Org Chem       Date:  2015-12-04       Impact factor: 2.883

8.  In Silico Screening for Novel Leucine Aminopeptidase Inhibitors with 3,4-Dihydroisoquinoline Scaffold.

Authors:  Joanna Ziemska; Jolanta Solecka; Małgorzata Jarończyk
Journal:  Molecules       Date:  2020-04-10       Impact factor: 4.411

9.  Phosphinotripeptidic Inhibitors of Leucylaminopeptidases.

Authors:  Michał Jewgiński; Kinga Haremza; Jesús M de Los Santos; Zouhair Es Sbai; Bartosz Oszywa; Małgorzata Pawełczak; Francisco Palacios; Rafał Latajka
Journal:  Int J Mol Sci       Date:  2021-05-11       Impact factor: 5.923
  9 in total

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