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J Biol Chem, Vol. 274, Issue 2, 881-888, January 8, 1999
§,¶, and
From the A gene encoding a serine-type protease has been
cloned from Aquifex pyrophilus using a sequence tag
containing the consensus sequence of proteases as a probe. Sequence
analysis of the cloned gene reveals an open reading frame of 619 residues that has three canonical residues (Asp-140, His-184, and
Ser-502) that form the catalytic site of serine-type proteases. The
size of the mature form (43 kDa) and its localization in the cell wall
fraction indicate that both the NH2- and COOH-terminal
sequences of the protein are processed during maturation. When the
cloned gene is expressed in Escherichia coli, it is weakly
expressed as active and processed forms. The pH optimum of this
protease is very broad, and its activity is completely inactivated by
phenylmethylsulfonyl fluoride. The half-life of the protein is 6 h
at 105 °C, suggesting that it is one of the most heat-stable
proteases. The cysteine residues in the mature form may form disulfide
bonds that are responsible for the strong stability of this protease,
because the thermostability of the protein is significantly reduced in
the presence of reducing reagent.
Structural Biology Center, Korea Institute
of Science and Technology, Seoul, 136-791 Korea, the
§ Department of Agricultural Chemistry, Korea University
Seoul, 136-701 Korea, and the ¶ Department of Chemistry,
University of California, Berkeley, California 94720
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