Acta Crystallographica Section D
Acta Crystallographica
Section D
STRUCTURAL BIOLOGY
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Acta Cryst.
(2014).
D
70
,
242-252
https://doi.org/10.1107/S1399004713026461
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Understanding the highly efficient catalysis of prokaryotic peptide deformylases by shedding light on the determinants specifying the low activity of the human counterpart
S. Fieulaine
,
M. Desmadril
,
T. Meinnel
and
C. Giglione
This work reports the structural basis of the highly efficient catalysis of most PDF enzymes by analyzing the impact of the two main substitutions of animal mitochondrial PDFs which cause unusually weak rate.
Keywords:
peptide deformylase
;
human
;
mitochondria
;
Arabidopsis thaliana
;
N-terminal methionine excision
.
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