Protonation States of Methionine Aminopeptidase Studied by QM/MM Car-Parrinello Molecular Dynamics Simulations

Christian D. P. Klein ()
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Christian D. P. Klein: Universität des Saarlandes, Pharmazeutische und Medizinische Chemie

A chapter in High Performance Computing in Science and Engineering ’03, 2003, pp 393-402 from Springer

Abstract: Abstract Methionine aminopeptidases (MetAPs) play a central role for in vivo protein synthesis as they remove the starter methionine from newly synthetized proteins. MetAPs are metaldependent enzymes. It is not clear which metal activates the MetAPs in vivo. For in vitro experiments, cobalt is commonly used because it activates all known MetAPs and the cobaltsubstituted enzymes are usually the most active. [1] Zinc and iron(II) have also been shown to activate some MetAPs. [2] The metalchelating residues in all known MetAPs are two glutamates, two aspartates and one histidine. The geometric arrangement of these residues is practically identical in all MetAP x-ray structures.

Keywords: Protonation State; Methionine Aminopeptidase; Kinetic Energy Cutoff; CPMD Simulation; Active Site Water Molecule (search for similar items in EconPapers)
Date: 2003
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Persistent link: https://EconPapers.repec.org/RePEc:spr:sprchp:978-3-642-55876-4_29

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DOI: 10.1007/978-3-642-55876-4_29

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