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J Biol Chem, Vol. 273, Issue 28, 17726-17731, July 10, 1998
From the When the genome of the thermophilic archaeon
Pyrococcus horikoshii was sequenced, a gene homologous to
the mammalian gene for an acylamino acid-releasing enzyme (EC 3.4.19.1)
was found in which the enzyme's proposed active residues were
conserved. The P. horikoshii gene comprised an open reading
frame of 1,896 base pairs with an ATG initiation codon and a TAG
termination codon, encoding a 72,390-Da protein of 632 amino acid
residues. This gene was overexpressed in Escherichia coli
with the pET vector system, and the resulting enzyme showed the
anticipated amino-terminal sequence and high hydrolytic activity for
acylpeptides. This enzyme was concluded to be the first acylamino
acid-releasing enzyme from an organism other than a eukaryotic cell.
The existence of the enzyme in archaea suggests that the mechanisms of
protein degradation or initiation of protein synthesis or both in
archaea may be similar to those in eukaryotes. The enzyme was stable at 90 °C, with its optimum temperature over 90 °C. The specific
activity of the enzyme increased 7-14-fold with heat treatment,
suggesting the modification of the enzyme's structure for optimal
hydrolytic activity by heating. This enzyme is expected to be useful
for the removal of N
Acylamino Acid-releasing Enzyme from the Thermophilic Archaeon
Pyrococcus horikoshii
,,,¶,
,, and
National Institute of Bioscience and
Human-Technology and the National Institute of Materials and
Chemical Research,
-acylated
residues in short peptide sequence analysis at high temperatures.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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