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Structural analysis of metalloform-selective inhibition of methionine aminopeptidase.

Xie SX, Huang WJ, Ma ZQ, Huang M, Hanzlik RP, Ye QZ
Acta Crystallogr D Biol Crystallogr 62 425-32 (2006)
Related entries: 2evc, 2evo

Cited: 15 times
EuropePMC logo PMID: 16552144

Abstract

One of the challenges in the development of methionine aminopeptidase (MetAP) inhibitors as antibacterial and anticancer agents is to define the metal ion actually used by MetAP in vivo and to discover MetAP inhibitors that can inhibit the metalloform that is relevant in vivo. Two distinct classes of novel nonpeptidic MetAP inhibitors that are not only potent but also highly selective for either the Mn(II) or Co(II) form have been identified. Three crystal structures of Escherichia coli MetAP complexed with the metalloform-selective inhibitors 5-(2,5-dichlorophenyl)furan-2-carboxylic acid (2), 5-[2-(trifluoromethyl)phenyl]furan-2-carboxylic acid (3) and N-cyclopentyl-N-(thiazol-2-yl)oxalamide (4) have been solved and analysis of these structures has revealed the structural basis for their metalloform-selective inhibition. The Mn(II)-form selective inhibitors (2) and (3) both use their carboxylate group to coordinate with the two Mn(II) ions at the dinuclear metal site and both adopt a non-coplanar conformation for the two aromatic rings. The unique coordination geometry of these inhibitors may determine their Mn(II)-form selectivity. In contrast, the Co(II)-form selective inhibitor (4) recruits an unexpected third metal ion, forming a trimetallic enzyme-metal-inhibitor complex. Thus, an important factor in the selectivity of (4) for the Co(II) form may be a consequence of a greater preference for a softer N,O-donor ligand for the softer Co(II).

Reviews - 2evm mentioned but not cited (1)

  1. Advances in Bacterial Methionine Aminopeptidase Inhibition. Helgren TR, Wangtrakuldee P, Staker BL, Hagen TJ. Curr Top Med Chem 16 397-414 (2016)

Articles - 2evm mentioned but not cited (3)

  1. Rickettsia prowazekii methionine aminopeptidase as a promising target for the development of antibacterial agents. Helgren TR, Chen C, Wangtrakuldee P, Edwards TE, Staker BL, Abendroth J, Sankaran B, Housley NA, Myler PJ, Audia JP, Horn JR, Hagen TJ. Bioorg Med Chem 25 813-824 (2017)
  2. Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymes. Ma ZQ, Xie SX, Huang QQ, Nan FJ, Hurley TD, Ye QZ. BMC Struct Biol 7 84 (2007)
  3. The identification of inhibitory compounds of Rickettsia prowazekii methionine aminopeptidase for antibacterial applications. Helgren TR, Seven ES, Chen C, Edwards TE, Staker BL, Abendroth J, Myler PJ, Horn JR, Hagen TJ. Bioorg Med Chem Lett 28 1376-1380 (2018)


Articles citing this publication (11)

  1. Inhibitors of Plasmodium falciparum methionine aminopeptidase 1b possess antimalarial activity. Chen X, Chong CR, Shi L, Yoshimoto T, Sullivan DJ, Liu JO. Proc Natl Acad Sci U S A 103 14548-14553 (2006)
  2. FE(II) is the native cofactor for Escherichia coli methionine aminopeptidase. Chai SC, Wang WL, Ye QZ. J Biol Chem 283 26879-26885 (2008)
  3. Structural basis of catalysis by monometalated methionine aminopeptidase. Ye QZ, Xie SX, Ma ZQ, Huang M, Hanzlik RP. Proc Natl Acad Sci U S A 103 9470-9475 (2006)
  4. Discovery of inhibitors of Escherichia coli methionine aminopeptidase with the Fe(II)-form selectivity and antibacterial activity. Wang WL, Chai SC, Huang M, He HZ, Hurley TD, Ye QZ. J Med Chem 51 6110-6120 (2008)
  5. Catalysis and inhibition of Mycobacterium tuberculosis methionine aminopeptidase. Lu JP, Chai SC, Ye QZ. J Med Chem 53 1329-1337 (2010)
  6. 2-Oxoglutarate analogue inhibitors of prolyl hydroxylase domain 2. Mecinović J, Loenarz C, Chowdhury R, Schofield CJ. Bioorg Med Chem Lett 19 6192-6195 (2009)
  7. Inhibition of monometalated methionine aminopeptidase: inhibitor discovery and crystallographic analysis. Huang M, Xie SX, Ma ZQ, Huang QQ, Nan FJ, Ye QZ. J Med Chem 50 5735-5742 (2007)
  8. Metal-mediated inhibition is a viable approach for inhibiting cellular methionine aminopeptidase. Chai SC, Ye QZ. Bioorg Med Chem Lett 19 6862-6864 (2009)
  9. Analyzing the binding of Co(II)-specific inhibitors to the methionyl aminopeptidases from Escherichia coli and Pyrococcus furiosus. Mitra S, Sheppard G, Wang J, Bennett B, Holz RC. J Biol Inorg Chem 14 573-585 (2009)
  10. Metal promiscuity and metal-dependent substrate preferences of Trypanosoma brucei methionine aminopeptidase 1. Marschner A, Klein CD. Biochimie 115 35-43 (2015)
  11. Pyridinylquinazolines selectively inhibit human methionine aminopeptidase-1 in cells. Zhang F, Bhat S, Gabelli SB, Chen X, Miller MS, Nacev BA, Cheng YL, Meyers DJ, Tenney K, Shim JS, Crews P, Amzel LM, Ma D, Liu JO. J Med Chem 56 3996-4016 (2013)


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