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Sugar synthesis in Leptospira. II. Presence of glyoxylate cycle enzymes.
Microbiol Immunol. 1984; 28(5):529-34.MI

Abstract

The presence and some properties of the key enzymes of the glyoxylate cycle, isocitrate lyase (threo-Ds-isocitrate glyoxylate-lyase, EC 4.1.3.1) and malate synthase (L-malate glyoxylate-lyase (CoA-acetylating) EC 4.1.3.2), were investigated in Leptospira biflexa. Isocitrate lyase activity was found for the first time in the organism. The enzyme was induced by ethanol but not by acetate. The optimum pH was 6.8. The activity was inhibited by phosphoenolpyruvate, a specific inhibitor of isocitrate lyase. The optimum pH of malate synthase of L. biflexa was about 8.5. The Km value for glyoxylate was 3.0 X 10(-3) M and the activity was inhibited by glycolate, the inhibitor. The results strongly suggested the presence of a glyoxylate cycle in Leptospira. The possibility that the glyoxylate cycle plays an essential role in the synthesis of sugars, amino acids and other cellular components as an anaplerotic pathway of the tricarboxylic acid cycle in Leptospira was discussed.

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Authors

Yanagihara Y
No affiliation info available
Kobayashi S
No affiliation info available
Mifuchi I
No affiliation info available

MeSH

CarbohydratesGlyoxylatesHydrogen-Ion ConcentrationIsocitrate LyaseLeptospiraMalate SynthaseOxo-Acid-Lyases

Pub Type(s)

Comparative Study
Journal Article

Language

eng

PubMed ID

6472133

Citation

Yanagihara, Y, et al. "Sugar Synthesis in Leptospira. II. Presence of Glyoxylate Cycle Enzymes." Microbiology and Immunology, vol. 28, no. 5, 1984, pp. 529-34.
Yanagihara Y, Kobayashi S, Mifuchi I. Sugar synthesis in Leptospira. II. Presence of glyoxylate cycle enzymes. Microbiol Immunol. 1984;28(5):529-34.
Yanagihara, Y., Kobayashi, S., & Mifuchi, I. (1984). Sugar synthesis in Leptospira. II. Presence of glyoxylate cycle enzymes. Microbiology and Immunology, 28(5), 529-34.
Yanagihara Y, Kobayashi S, Mifuchi I. Sugar Synthesis in Leptospira. II. Presence of Glyoxylate Cycle Enzymes. Microbiol Immunol. 1984;28(5):529-34. PubMed PMID: 6472133.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Sugar synthesis in Leptospira. II. Presence of glyoxylate cycle enzymes. AU - Yanagihara,Y, AU - Kobayashi,S, AU - Mifuchi,I, PY - 1984/1/1/pubmed PY - 1984/1/1/medline PY - 1984/1/1/entrez SP - 529 EP - 34 JF - Microbiology and immunology JO - Microbiol Immunol VL - 28 IS - 5 N2 - The presence and some properties of the key enzymes of the glyoxylate cycle, isocitrate lyase (threo-Ds-isocitrate glyoxylate-lyase, EC 4.1.3.1) and malate synthase (L-malate glyoxylate-lyase (CoA-acetylating) EC 4.1.3.2), were investigated in Leptospira biflexa. Isocitrate lyase activity was found for the first time in the organism. The enzyme was induced by ethanol but not by acetate. The optimum pH was 6.8. The activity was inhibited by phosphoenolpyruvate, a specific inhibitor of isocitrate lyase. The optimum pH of malate synthase of L. biflexa was about 8.5. The Km value for glyoxylate was 3.0 X 10(-3) M and the activity was inhibited by glycolate, the inhibitor. The results strongly suggested the presence of a glyoxylate cycle in Leptospira. The possibility that the glyoxylate cycle plays an essential role in the synthesis of sugars, amino acids and other cellular components as an anaplerotic pathway of the tricarboxylic acid cycle in Leptospira was discussed. SN - 0385-5600 UR - https://www.unboundmedicine.com/medline/citation/6472133/Sugar_synthesis_in_Leptospira__II__Presence_of_glyoxylate_cycle_enzymes_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0385-5600&date=1984&volume=28&issue=5&spage=529 DB - PRIME DP - Unbound Medicine ER -