Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 7-Day Trial for You or Your Team.

Learn More →

Catabolism of aspartate and asparagine byBacteroides intermedius andBacteroides gingivalis

Catabolism of aspartate and asparagine byBacteroides intermedius andBacteroides gingivalis Aspartate as asparagine catabolism was studied in representative strains ofBacteroides intermedius strain T588 andB. gingivalis strain W83. Cell suspensions of both species deamidated asparagine. The enzyme asparaginase was constitutive and was unaffected by the addition of ammonium ions to the culture medium. The enzyme aspartase was not detected, but since malate dehydrogenase was known to occur and succinate was present as a major end product of metabolism, aspartate catabolism was postulated to occur via oxaloacetate, malate, and fumarate to succinate. All enzymes of this pathway were present in cell-free extracts, and some of the major properties of these enzymes were examined. The electron carriers cytochrome b and menaquinone-9 were present inB. gingivalis, whereasB. intermedius possessed cytochrome c and menaquinone-11. The membrane-bound enzyme fumarate reductase utilized NADH as an electron donor, but the reaction was inhibited by short wave ultraviolet radiation and 2-n-heptyl-4-hydroxyquinoline-N-oxide. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current Microbiology Springer Journals

Catabolism of aspartate and asparagine byBacteroides intermedius andBacteroides gingivalis

Shah, Haroun; Williams, Ralph
Current Microbiology , Volume 15 (6) – Apr 13, 2005
Download PDF
6 pages

Loading next page...
 
/lp/springer-journals/catabolism-of-aspartate-and-asparagine-bybacteroides-intermedius-t0y2mIFg0X

References (52)

Publisher
Springer Journals
Copyright
Copyright © 1987 by Springer-Verlag New York Inc.
Subject
Life Sciences; Microbiology; Biotechnology
ISSN
0343-8651
eISSN
1432-0991
DOI
10.1007/BF01577587
Publisher site
See Article on Publisher Site

Abstract

Aspartate as asparagine catabolism was studied in representative strains ofBacteroides intermedius strain T588 andB. gingivalis strain W83. Cell suspensions of both species deamidated asparagine. The enzyme asparaginase was constitutive and was unaffected by the addition of ammonium ions to the culture medium. The enzyme aspartase was not detected, but since malate dehydrogenase was known to occur and succinate was present as a major end product of metabolism, aspartate catabolism was postulated to occur via oxaloacetate, malate, and fumarate to succinate. All enzymes of this pathway were present in cell-free extracts, and some of the major properties of these enzymes were examined. The electron carriers cytochrome b and menaquinone-9 were present inB. gingivalis, whereasB. intermedius possessed cytochrome c and menaquinone-11. The membrane-bound enzyme fumarate reductase utilized NADH as an electron donor, but the reaction was inhibited by short wave ultraviolet radiation and 2-n-heptyl-4-hydroxyquinoline-N-oxide.

Journal

Current Microbiology – Springer Journals

Published: Apr 13, 2005

There are no references for this article.