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Characterization of substrate specificity and novel autoprocessing mechanism of dipeptidase A from Prevotella intermedia


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Title: Characterization of substrate specificity and novel autoprocessing mechanism of dipeptidase A from Prevotella intermedia
Authors: Sarwar, Mohammad Tanvir / Ohara-Nemoto, Yuko / Kobayakawa, Takeshi / Naito, Mariko / Nemoto, Takayuki K.
Issue Date: 8-Jan-2020
Publisher: Walter de Gruyter
Citation: Biological Chemistry, Article in Press
Abstract: Prevotella intermedia, a gram-negative anaerobic rod, is frequently observed in subgingival polymicrobial biofilm from adults with chronic periodontitis. Peptidases in periodontopathic bacteria are considered to function as etiological reagents. Pre. intermedia OMA14 cells abundantly express an unidentified cysteine peptidase specific for Arg-4-methycoumaryl-7- amide (MCA). BAU17746 (locus tag, PIOMA14_I_1238) and BAU18827 (locus tag, PIOMA14_II_0322) emerged as candidates of this peptidase from the substrate specificity and sequence similarity with C69-family Streptococcus gordonii Arg-aminopeptidase. The recombinant form of the former solely exhibited hydrolyzing activity toward Arg-MCA, and BAU17746 possesses a 26.6% amino acid identity with the C69-family Lactobacillus helveticus dipeptidase A. It was found that BAU17746 as well as L. helveticus dipeptidase A was a P1-position Arg-specific dipeptidase A, although the L. helveticus entity, a representative of the C69 family, had been reported to be specific for Leu and Phe. The fulllength form of BAU17746 was intramolecularly processed to a mature form carrying the N-terminus of Cys15. In conclusion, the marked Arg-MCA-hydrolyzing activity in Pre. intermedia was mediated by BAU17746 belonging to the C69-family dipeptidase A, in which the mature form carries an essential cysteine at the N-terminus.
Keywords: dipeptidase A / cysteine peptidase / autoprocessing / Prevotella intermedia / substrate specificity / periodontal disease
URI: http://hdl.handle.net/10069/39626
ISSN: 14316730
DOI: 10.1515/hsz-2019-0387
Rights: © 2020 by Walter de Gruyter Berlin/Boston. / The final publication is available at www.degruyter.com
Type: Journal Article
Text Version: author
Appears in Collections:Articles in academic journal

Citable URI : http://hdl.handle.net/10069/39626

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