Home LiteratureArticle Details
PMID: 14042938 Published · ppublish English Journal Article

MICROBIOLOGICAL DISSIMILATION OF TRICARBALLYLATE AND TRANS-ACONITATE.

Journal of bacteriology ·Vol. 85 ·1963-03-00 ·Pages 604-13

ALTEKAR WW, RAO MR

Abstract

Altekar, W. W. (National Chemical Laboratory, Poona, India) and M. R. Raghavendra Rao. Microbiological dissimilation of tricarballylate and trans-aconitate. J. Bacteriol. 85:604-613. 1963.-Two fluorescent pseudomonads capable of metabolizing tricarballylate and trans-aconitate were isolated by the soil-enrichment culture technique. These and some other species of bacteria were tested for their ability to utilize for growth the salts of many di- and tricarboxylic acids. Alloisocitrate and mesaconate were not utilized by any of the ten strains tested; only two strains grew on tricarballylate and itaconate. trans-Aconitate was utilized by many strains which had not been previously exposed to this compound. The resting cells of two strains could adapt to oxidize two acids (tricarballylate and trans-aconitate), and this induction was chloramphenicol-sensitive. The tricarballylate-grown cells were simultaneously induced to oxidize trans-aconitate and other tricarboxylates, whereas the trans-aconitate-grown cells were not induced to oxidize tricarballylate, and their subsequent induction was inhibited by chloramphenicol. This trans-aconitate or tricarballylate. But tricarballylate dehydrogenase was present only in tricarballylate-grown cells. The cell-free extracts of the two organisms contained the enzymes of the Krebs cycle and isocitritase. These enzymes are most probably operative during growth on and oxidation of these two acids as sole carbon sources.

Keywords
BACTERIA METABOLISM PSEUDOMONAS SOIL MICROBIOLOGY
MeSH Terms
Aconitic Acid Bacteria India Metabolism Oxidation-Reduction Oxidoreductases Pseudomonas Soil Microbiology Tricarboxylic Acids
Chemicals
Tricarboxylic Acids Aconitic Acid Oxidoreductases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
ALTEKAR W W
RAO M R
References (8)
8 references, click to expand
  1. [The biosynthesis of beta-galactosidase (lactase) in Escherichia coli; the specificity of induction].
    Biochim Biophys Acta. 1951 Nov;7(4):585-99 PMID: 14904456
  2. Effects of carbon sources and base analogues of nucleic acid on the formation of bacterial amylase.
    Nature. 1957 Aug 31;180(4583):438-9 PMID: 13464853
  3. Simultaneous Adaptation: A New Technique for the Study of Metabolic Pathways.
    J Bacteriol. 1947 Sep;54(3):339-48 PMID: 16561366
  4. Aconitate isomerase.
    Biochem Biophys Res Commun. 1961 Feb 24;4:101-5 PMID: 13739531
  5. Factors affecting the activity of aconitase.
    J Biol Chem. 1951 Jan;188(1):379-88 PMID: 14814148
  6. Tricarballylate dehydrogenase.
    Biochem Biophys Res Commun. 1962 Feb 20;7:62-6 PMID: 14490333
  7. Enzymatic synthesis of citric acid. II. Crystalline condensing enzyme.
    J Biol Chem. 1951 Dec;193(2):691-702 PMID: 14907759
  8. Spectrophotometric measurements of the enzymatic formation of fumaric and cis-aconitic acids.
    Biochim Biophys Acta. 1950 Jan;4(1-3):211-4 PMID: 15403927
Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1963-03-00
Pages
604-13
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC278189
Subset
OM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]