FE(II) Is the Native Cofactor for Escherichia coli Methionine Aminopeptidase

Chai, Sergio C.; Wang, Wen Long; Ye, Qi Zhuang

doi:10.1074/jbc.m804345200

Cited by 50 publications

(81 citation statements)

References 65 publications

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“…While the study of metalloenzymes in vitro has a long history, there are now several examples where the cofactor required for in vivo function was initially misassigned (Jain et al, 2005, Chai et al, 2008). This reflects the fact that metalloenzymes are often assayed under conditions that may not mimic the levels of metal ion availability in the cell.…”

Section: Microbial Adaptation and Acclimation To Metal Ion Limitmentioning

confidence: 99%

Elemental Economy

Merchant

Helmann

2012

Advances in Microbial Physiology

182

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Section: Microbial Adaptation and Acclimation To Metal Ion Limitmentioning

confidence: 99%

Elemental Economy

Merchant

Helmann

2012

Advances in Microbial Physiology

182

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“…Also, there are some proteins whose natural metal ion was assigned as Co II in pioneering studies, and taken as such in Kobayashi and Shimizu's review, but was later on proven to be a different one. For example, Fe II , but not Co II , is the native metal ion in methionine aminopeptidase (Chai et al, 2008;Sule et al, 2012) and Mn II , but not Co II , is the native ion in prolidase (Besio et al, 2013). In other proteins, the native requirement for Co II is not clear because similar variants and isoforms seem to employ different ions; for example, some xylose isomerases require one of either Co II or Mg II for maximal stability and activity (Epting et al, 2005), whereas at least one isoform of glucose isomerase requires the presence of both ions in the medium to achieve maximum activity (Wang et al, 2011).…”

Section: Resultsmentioning

confidence: 99%

Investigation of non-corrin cobalt(II)-containing sites in protein structures of the Protein Data Bank

Abriata

2013

Acta Crystallogr Sect B

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Protein X-ray structures with non-corrin cobalt(II)-containing sites, either natural or substituting another native ion, were downloaded from the Protein Data Bank and explored to (i) describe which amino acids are involved in their first ligand shells and (ii) analyze cobalt(II)-donor bond lengths in comparison with previously reported target distances, CSD data and EXAFS data. The set of amino acids involved in Co II binding is similar to that observed for catalytic Zn II sites, i.e. with a large fraction of carboxylate O atoms from aspartate and glutamate and aromatic N atoms from histidine. The computed Co II -donor bond lengths were found to depend strongly on structure resolution, an artifact previously detected for other metal-donor distances. Small corrections are suggested for the target bond lengths to the aromatic N atoms of histidines and the O atoms of water and hydroxide. The available target distance for cysteine (Scys) is confirmed; those for backbone O and other donors remain uncertain and should be handled with caution in refinement and modeling protocols. Finally, a relationship between both Co II -O bond lengths in bidentate carboxylates is quantified.

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“…For example, conversion of ( 17 ) to hydroxamic acid derivative ( 21 ) results in dramatic activity increases when screened against these cofactors ( Ec MetAP IC 50 for ( 17 ) = >200, 94 and 2.9 μM; Co(II), Fe (II), Mn(II) cofactors, respectively; Ec MetAP IC 50 for ( 21 ) = 3.5, 1, 1.3 μM; Co(II), Fe (II), Mn(II) cofactors, respectively) [41]. Additionally, ( 21 ) was crystallized with Ec MetAP1 bearing Mn(II) cofactors (PDB: 4A6W); the crystal structure demonstrates bridging interactions to both active site metals as opposed to chelation demonstrated for the crystal structure of ( 17 ) (Fig.…”

Section: Classes Of Metap Inhibitorsmentioning

confidence: 99%

“…Finally, other 5-aryl-2-heterocyclic carboxylic acids (i.e. oxazole, 1,2,4-oxadiazole, 1,3,4-oxadiazole, and imidazole) were screened against Ec MetAP1 and were found to exhibit comparable or worse inhibitory activity [41]. …”

Section: Classes Of Metap Inhibitorsmentioning

confidence: 99%

Advances in Bacterial Methionine Aminopeptidase Inhibition

Helgren¹,

Wangtrakuldee²,

Staker³

et al. 2015

CTMC

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Methionine aminopeptidases (MetAPs) are metalloenzymes that cleave the N-terminal methionine from newly synthesized peptides and proteins. These MetAP enzymes are present in bacteria, and knockout experiments have shown that MetAP activity is essential for cell life, suggesting that MetAPs are good antibacterial drug targets. MetAP enzymes are also present in the human host and selectivity is essential. There have been significant structural biology efforts and over 65 protein crystal structures of bacterial MetAPs are deposited into the PDB. This review highlights the available crystallographic data for bacterial MetAPs. Structural comparison of bacterial MetAPs with human MetAPs highlights differences that can lead to selectivity. In addition, this review includes the chemical diversity of molecules that bind and inhibit the bacterial MetAP enzymes. Analysis of the structural biology and chemical space of known bacterial MetAP inhibitors leads to a greater understanding of this antibacterial target and the likely development of potential antibacterial agents.

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FE(II) Is the Native Cofactor for Escherichia coli Methionine Aminopeptidase

Cited by 50 publications

References 65 publications

Elemental Economy

Elemental Economy

Investigation of non-corrin cobalt(II)-containing sites in protein structures of the Protein Data Bank

Advances in Bacterial Methionine Aminopeptidase Inhibition

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