ArticleThe Journal of biological chemistry2008
A 52-kDa leucyl aminopeptidase from treponema denticola is a cysteinylglycinase that mediates the second step of glutathione metabolism.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 55 citations in OpenAlex.
- Aminopeptidase M17 in bacteria: insights into structure, function, and potential as a drug target.Journal of bacteriology · 2026Review
- Identification of a staphylococcal dipeptidase involved in the production of human body odor.The Journal of biological chemistry · 2024Article
- Characterization of leucine aminopeptidase (LAP) activity in sweet pepper fruits during ripening and its inhibition by nitration and reducing events.Plant cell reports · 2024Article
- Locus Coeruleus Dysfunction and Trigeminal Mesencephalic Nucleus Degeneration: A Cue for Periodontal Infection Mediated Damage in Alzheimer's Disease?International journal of environmental research and public health · 2023Review
- An unexpected role for leucyl aminopeptidase in UV tolerance revealed by a genome-wide fitness assessment in a model cyanobacterium.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Host and bacterial factors linking periodontitis and rheumatoid arthritis.Frontiers in immunology · 2022Review
- Using microbial metalo-aminopeptidases as targets in human infectious diseases.Microbial cell (Graz, Austria) · 2021Review
- New roles for glutathione: Modulators of bacterial virulence and pathogenesis.Redox biology · 2021Article
- Fruit ripening-associated leucylaminopeptidase with cysteinylglycine dipeptidase activity from durian suggests its involvement in glutathione recycling.BMC plant biology · 2021Article
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- A leucine aminopeptidase is involved in kinetoplast DNA segregation in Trypanosoma brucei.PLoS pathogens · 2017Article
- MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae.Open biology · 2015Article
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- The Staphylococcus aureus leucine aminopeptidase is localized to the bacterial cytosol and demonstrates a broad substrate range that extends beyond leucine.Biological chemistry · 2013Article
- Identification of an intracellular M17 family leucine aminopeptidase that is required for virulence in Staphylococcus aureus.Microbes and infection · 2012Article
- Virulence factors of the oral spirochete Treponema denticola.Journal of dental research · 2011Review
- Comparative proteomic analyses of Streptococcus suis serotype 2 cell wall-associated proteins.Current microbiology · 2011Article
- Dug1p Is a Cys-Gly peptidase of the gamma-glutamyl cycle of Saccharomyces cerevisiae and represents a novel family of Cys-Gly peptidases.The Journal of biological chemistry · 2009Article
- The antioxidant master glutathione and periodontal health.Dental research journalReview
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The metabolism of glutathione by the periodontal pathogen Treponema denticola produces hydrogen sulfide, which may play a role in the host tissue destruction seen in periodontitis. H2S production in this organism has been proposed to occur via a three enzyme pathway, gamma-glutamyltransferase, cysteinylglycinase (CGase), and cystalysin. In this study, we describe the purification and characterization of T. denticola CGase. Standard approaches were used to purify a 52-kDa CGase activity from T. denticola, and high pressure liquid chromatography electrospray ionization tandem mass spectrometry analysis of this molecule showed that it matches the amino acid sequence of a predicted 52-kDa protein in the T. denticola genome data base. A recombinant version of this protein was overexpressed in and purified from Escherichia coli and shown to catalyze the hydrolysis of cysteinylglycine (Cys-Gly) with the same kinetics as the native protein. Surprisingly, because sequence homology indicates that this protein is a member of a family of metalloproteases called M17 leucine aminopeptidases, the preferred substrate for the T. denticola protein is Cys-Gly (k cat/Km of 8.2 microm(-1) min(-1)) not l-Leu-p-NA (k cat/Km of 1.1 microm(-1) min(-1)). The activity of CGase for Cys-Gly is optimum at pH 7.3 and is enhanced by Mn2+, Co2+, or Mg2+ but not by Zn2+ or Ca2+. Importantly, in combination with the two other previously purified T. denticola enzymes, gamma-glutamyltransferase and cystalysin, CGase mediates the in vitro degradation of glutathione into the expected end products, including H2S. These results prove that T. denticola contains the entire three-step pathway to produce H2S from glutathione, which may be important for pathogenesis.
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Registered trials
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