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Cover Picture: Hydroxamic Acids as Potent Inhibitors of Fe II and Mn II E. coli Methionine Aminopeptidase: Biological Activities and X‐ray Structures of Oxazole Hydroxamate– Ec MetAP‐Mn Complexes (ChemMedChem 6/2012)
Author(s) -
Huguet Florian,
Melet Armelle,
Alves de Sousa Rodolphe,
Lieutaud Aurélie,
Chevalier Jacqueline,
Maigre Laure,
Deschamps Patrick,
Tomas Alain,
Leulliot Nicolas,
Pages JeanMarie,
Artaud Isabelle
Publication year - 2012
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201290024
Subject(s) - oxazole , hydroxamic acid , chemistry , stereochemistry , imidazole , methionine , enzyme , derivative (finance) , amino acid , organic chemistry , biochemistry , financial economics , economics
The cover picture shows an oxazole derivative in complex with Escherichia coli methionine aminopeptidase (MetAP) in its Mn II form. The enzyme is consistently dinuclear even when crystallized with a substoichiometric ratio of Mn II /apo‐protein. The derivative shown is part of a new series of hydroxamic acids linked to five‐membered heterocycles, such as oxazole and oxadiazole or imidazole, that are potent and specific inhibitors of both the Mn II and Fe II forms of E. coli MetAP. For more details, see the Full Paper by Isabelle Artaud et al. on p. 1020 ff.