The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme.

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Citation

D'souza VM, Holz RC

The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme.

Biochemistry. 1999 Aug 24;38(34):11079-85.

PubMed ID
10460163 [ View in PubMed
]
Abstract

The identity of the physiologically relevant metal ions for the methionyl aminopeptidase (MetAP) from Escherichia coli was investigated and is suggested to be Fe(II). The metal content of whole cells in the absence and presence of expression of the type I MetAP from E. coli was determined by inductively coupled plasma (ICP) emission analysis. The observed change in whole cell concentrations of cobalt, cadmium, copper, nickel, strontium, titanium, and vanadium upon expression of MetAP was negligible. On the other hand, significant increases in the cellular metal ion concentrations of chromium, zinc, manganese, and iron were observed with the increase in iron concentration being 4.4 and 6.2 times greater than that of manganese and zinc, respectively. Activity assays of freshly lysed BL21(DE3) cells containing the pMetAAP plasmid revealed detectable levels (>2 units/mg) of MetAP activity. Control experiments with BL21(DE3) without the MetAP plasmid showed no detectable enzymatic activity. Since MetAP is active upon expression, these data strongly suggest that cobalt is not the in vivo metal ion for the MetAP from E. coli. The MetAP from E. coli as purified was found to be catalytically inactive (

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Methionine aminopeptidaseP0AE18Details