Role of Aggregatibacter actinomycetemcomitans in glutathione catabolism

L. Chu, X. Xu, J. Su, L. Song, Y. Lai, Zheng Dong, D. Cappelli

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Introduction: Our previous studies demonstrated that three enzymes, γ-glutamyltransferase (GGT), cysteinylglycinase (CGase) and cystalysin, are required for the catabolism of glutathione to produce hydrogen sulfide (H 2S) in Treponema denticola. In this study, we examined glutathione catabolism in Aggregatibacter actinomycetemcomitans. Methods: The GGT and CGase of A. actinomycetemcomitans were determined by biological methods and GGT was characterized using a molecular biological approach. Results: A. actinomycetemcomitans showed GGT and CGase activity, but could not produce H 2S from glutathione. The addition of recombinant T. denticola cystalysin, an l-cysteine desulfhydrase, to whole cells of A. actinomycetemcomitans resulted in the production of H 2S from glutathione. Subsequently, we cloned A. actinomycetemcomitans GGT gene (ggt) and overexpressed the 63 kDa GGT protein. The recombinant A. actinomycetemcomitans GGT was purified and identified. The K cat/K m of the recombinant GGT from N-γ-l-glutamyl-4-nitroaniline as substrate was 31/μm/min. The activity of GGT was optimum at pH 6.9-7.1 and enhanced by thiol-containing compounds. Conclusion: The results demonstrated that A. actinomycetemcomitans had GGT and CGase activities and that the GGT was characterized. The possible role of A. actinomycetemcomitans in glutathione metabolism and H 2S production from oral bacteria was discussed.

Original languageEnglish (US)
Pages (from-to)236-242
Number of pages7
JournalOral Microbiology and Immunology
Volume24
Issue number3
DOIs
StatePublished - Jun 1 2009

Fingerprint

Aggregatibacter actinomycetemcomitans
Glutathione
Treponema denticola
Cystathionine gamma-Lyase
Hydrogen Sulfide
Sulfhydryl Compounds
Cats
Bacteria

Keywords

  • Aggregatibacter actinomycetemcomitans
  • Glutathione catabolism
  • Hydrogen sulfide production
  • Oral bacteria
  • γ-glutamyltransferase

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Dentistry(all)
  • Microbiology (medical)

Cite this

Role of Aggregatibacter actinomycetemcomitans in glutathione catabolism. / Chu, L.; Xu, X.; Su, J.; Song, L.; Lai, Y.; Dong, Zheng; Cappelli, D.

In: Oral Microbiology and Immunology, Vol. 24, No. 3, 01.06.2009, p. 236-242.

Research output: Contribution to journalArticle

Chu, L. ; Xu, X. ; Su, J. ; Song, L. ; Lai, Y. ; Dong, Zheng ; Cappelli, D. / Role of Aggregatibacter actinomycetemcomitans in glutathione catabolism. In: Oral Microbiology and Immunology. 2009 ; Vol. 24, No. 3. pp. 236-242.
@article{1941ce09423b40188a51f3f5a35400bb,
title = "Role of Aggregatibacter actinomycetemcomitans in glutathione catabolism",
abstract = "Introduction: Our previous studies demonstrated that three enzymes, γ-glutamyltransferase (GGT), cysteinylglycinase (CGase) and cystalysin, are required for the catabolism of glutathione to produce hydrogen sulfide (H 2S) in Treponema denticola. In this study, we examined glutathione catabolism in Aggregatibacter actinomycetemcomitans. Methods: The GGT and CGase of A. actinomycetemcomitans were determined by biological methods and GGT was characterized using a molecular biological approach. Results: A. actinomycetemcomitans showed GGT and CGase activity, but could not produce H 2S from glutathione. The addition of recombinant T. denticola cystalysin, an l-cysteine desulfhydrase, to whole cells of A. actinomycetemcomitans resulted in the production of H 2S from glutathione. Subsequently, we cloned A. actinomycetemcomitans GGT gene (ggt) and overexpressed the 63 kDa GGT protein. The recombinant A. actinomycetemcomitans GGT was purified and identified. The K cat/K m of the recombinant GGT from N-γ-l-glutamyl-4-nitroaniline as substrate was 31/μm/min. The activity of GGT was optimum at pH 6.9-7.1 and enhanced by thiol-containing compounds. Conclusion: The results demonstrated that A. actinomycetemcomitans had GGT and CGase activities and that the GGT was characterized. The possible role of A. actinomycetemcomitans in glutathione metabolism and H 2S production from oral bacteria was discussed.",
keywords = "Aggregatibacter actinomycetemcomitans, Glutathione catabolism, Hydrogen sulfide production, Oral bacteria, γ-glutamyltransferase",
author = "L. Chu and X. Xu and J. Su and L. Song and Y. Lai and Zheng Dong and D. Cappelli",
year = "2009",
month = "6",
day = "1",
doi = "10.1111/j.1399-302X.2008.00501.x",
language = "English (US)",
volume = "24",
pages = "236--242",
journal = "Molecular Oral Microbiology",
issn = "2041-1006",
publisher = "American Journal of Nursing Company",
number = "3",

}

TY - JOUR

T1 - Role of Aggregatibacter actinomycetemcomitans in glutathione catabolism

AU - Chu, L.

AU - Xu, X.

AU - Su, J.

AU - Song, L.

AU - Lai, Y.

AU - Dong, Zheng

AU - Cappelli, D.

PY - 2009/6/1

Y1 - 2009/6/1

N2 - Introduction: Our previous studies demonstrated that three enzymes, γ-glutamyltransferase (GGT), cysteinylglycinase (CGase) and cystalysin, are required for the catabolism of glutathione to produce hydrogen sulfide (H 2S) in Treponema denticola. In this study, we examined glutathione catabolism in Aggregatibacter actinomycetemcomitans. Methods: The GGT and CGase of A. actinomycetemcomitans were determined by biological methods and GGT was characterized using a molecular biological approach. Results: A. actinomycetemcomitans showed GGT and CGase activity, but could not produce H 2S from glutathione. The addition of recombinant T. denticola cystalysin, an l-cysteine desulfhydrase, to whole cells of A. actinomycetemcomitans resulted in the production of H 2S from glutathione. Subsequently, we cloned A. actinomycetemcomitans GGT gene (ggt) and overexpressed the 63 kDa GGT protein. The recombinant A. actinomycetemcomitans GGT was purified and identified. The K cat/K m of the recombinant GGT from N-γ-l-glutamyl-4-nitroaniline as substrate was 31/μm/min. The activity of GGT was optimum at pH 6.9-7.1 and enhanced by thiol-containing compounds. Conclusion: The results demonstrated that A. actinomycetemcomitans had GGT and CGase activities and that the GGT was characterized. The possible role of A. actinomycetemcomitans in glutathione metabolism and H 2S production from oral bacteria was discussed.

AB - Introduction: Our previous studies demonstrated that three enzymes, γ-glutamyltransferase (GGT), cysteinylglycinase (CGase) and cystalysin, are required for the catabolism of glutathione to produce hydrogen sulfide (H 2S) in Treponema denticola. In this study, we examined glutathione catabolism in Aggregatibacter actinomycetemcomitans. Methods: The GGT and CGase of A. actinomycetemcomitans were determined by biological methods and GGT was characterized using a molecular biological approach. Results: A. actinomycetemcomitans showed GGT and CGase activity, but could not produce H 2S from glutathione. The addition of recombinant T. denticola cystalysin, an l-cysteine desulfhydrase, to whole cells of A. actinomycetemcomitans resulted in the production of H 2S from glutathione. Subsequently, we cloned A. actinomycetemcomitans GGT gene (ggt) and overexpressed the 63 kDa GGT protein. The recombinant A. actinomycetemcomitans GGT was purified and identified. The K cat/K m of the recombinant GGT from N-γ-l-glutamyl-4-nitroaniline as substrate was 31/μm/min. The activity of GGT was optimum at pH 6.9-7.1 and enhanced by thiol-containing compounds. Conclusion: The results demonstrated that A. actinomycetemcomitans had GGT and CGase activities and that the GGT was characterized. The possible role of A. actinomycetemcomitans in glutathione metabolism and H 2S production from oral bacteria was discussed.

KW - Aggregatibacter actinomycetemcomitans

KW - Glutathione catabolism

KW - Hydrogen sulfide production

KW - Oral bacteria

KW - γ-glutamyltransferase

UR - http://www.scopus.com/inward/record.url?scp=67449160962&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=67449160962&partnerID=8YFLogxK

U2 - 10.1111/j.1399-302X.2008.00501.x

DO - 10.1111/j.1399-302X.2008.00501.x

M3 - Article

C2 - 19416454

AN - SCOPUS:67449160962

VL - 24

SP - 236

EP - 242

JO - Molecular Oral Microbiology

JF - Molecular Oral Microbiology

SN - 2041-1006

IS - 3

ER -