Abstract
The gene encoding pyrrolidone carboxyl peptidase (Pcp) has been cloned from the hyperthermophilic archaeon Thermococcus litoralis. The recombinant enzyme has been expressed in Escherichia coli, purified, and characterized. The T. litoralis Pcp demonstrates strong sequence homology to previously characterized bacterial Pcps. Some investigations have been carried out on enzyme substrate specificity and stability.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Archaeal Proteins / chemistry
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Archaeal Proteins / genetics
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Archaeal Proteins / isolation & purification
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Archaeal Proteins / metabolism
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Biotransformation
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Cloning, Molecular
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Electrophoresis, Polyacrylamide Gel
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Enzyme Stability / drug effects
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Escherichia coli
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Molecular Sequence Data
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Molecular Weight
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Pyroglutamyl-Peptidase I / chemistry
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Pyroglutamyl-Peptidase I / genetics*
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Pyroglutamyl-Peptidase I / isolation & purification
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Pyroglutamyl-Peptidase I / metabolism*
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Sequence Alignment
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Solvents / pharmacology
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Substrate Specificity
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Temperature
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Thermococcus / enzymology*
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Thermococcus / genetics
Substances
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Archaeal Proteins
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Recombinant Proteins
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Solvents
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Pyroglutamyl-Peptidase I