Anomalous Citrate Synthase from Thermus aquaticus
- 1 June 1978
- journal article
- research article
- Published by Microbiology Society in Journal of General Microbiology
- Vol. 106 (2) , 383-386
- https://doi.org/10.1099/00221287-106-2-383
Abstract
Previous studies of citrate synthase [citrate oxaloacetate-lyase (CoA-acetylating), EC 4.1.3.7] from a range of organisms showed that there is a correlation between the molecular and regulatory properties of the enzyme and the taxonomic grouping of the organism. Citrate synthases from gram-negative bacteria are large (MW .apprx. 250,000) whereas those from gram-positive bacteria and eukaryotic organisms are small (MW .apprx. 100,000). Regulation through allosteric inhibition by NADH occurs only with the gram-negative bacterial enzymes and appears to be connected with their more complex quaternary structure. Studies on the citrate synthase from the extreme thermophile T. aquaticus show that citrate synthase of T. aquaticus is an exception to the general correlation between molecular size of the enzyme and Gram stain of the bacterium.Keywords
This publication has 1 reference indexed in Scilit:
- Life at High TemperaturesScience, 1967