Expression of peptidylarginine deiminase from Porphyromonas gingivalis in Escherichia coli: enzyme purification and characterization.
Expression of peptidylarginine deiminase from Porphyromonas gingivalis in Escherichia coli: enzyme purification and characterization.
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DOI：
10.1016/j.abb.2009.06.010
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发表时间：
2009-08-01
影响因子：
3.9
通讯作者：
Ash DE
中科院分区：
文献类型：
--
作者：
Rodríguez SB;Stitt BL;Ash DE
Porphyromonas gingivalis peptidylarginine deiminase (PAD) catalyzes the deimination of peptidylarginine residues of various peptides to produce peptidylcitrulline and ammonia. P. gingivalis is associated with adult-onset periodontitis and cardiovascular disease, and its proliferation depends on secretion of PAD. We have expressed two recombinant forms of the P. gingivalis PAD in Escherichia coli, a truncated form with a 43-amino acid N-terminal deletion and the full-length form of PAD as predicted from the DNA sequence. Both forms contain a poly-His tag and Xpress epitope at the N-terminus to aid in detection and purification. The activities and stabilities of these two forms have been evaluated. PAD is cold sensitive; it aggregates within 30 min at 4 °C, and optimal storage conditions are at 25 °C in the presence of a reducing agent. PAD is not a metalloenzyme and does not need a co-factor for catalysis or stability. Multiple L-arginine analogs, various arginine-containing peptides, and free L-arginine were used to evaluate substrate specificity and determine kinetic parameters.
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通讯作者：
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通讯作者：
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