ArticleExtremophiles : life under extreme conditions2016
Pcal_1699, an extremely thermostable malate dehydrogenase from hyperthermophilic archaeon Pyrobaculum calidifontis.
Article in Extremophiles : life under extreme conditions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 25 citations in OpenAlex.
- Highly Active Thermophilic L-Asparaginase fromInternational journal of molecular sciences · 2021Article
- Antifreeze Proteins: A Tale of Evolution From Origin to Energy Applications.Frontiers in bioengineering and biotechnology · 2021Review
- A highly stable manganese catalase from Geobacillus thermopakistaniensis: molecular cloning and characterization.Extremophiles : life under extreme conditions · 2019Article
- Extremely stable indole-3-glycerol-phosphate synthase from hyperthermophilic archaeon Pyrococcus furiosus.Extremophiles : life under extreme conditions · 2019Article
- Pcal_0632, a phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Pyrobaculum calidifontis.Extremophiles : life under extreme conditions · 2018Article
- Pcal_1311, an alcohol dehydrogenase homologue from Pyrobaculum calidifontis, displays NADH-dependent high aldehyde reductase activity.Extremophiles : life under extreme conditions · 2017Article
- Pcal_1127, a highly stable and efficient ribose-5-phosphate pyrophosphokinase from Pyrobaculum calidifontis.Extremophiles : life under extreme conditions · 2016Article
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Authors and funding
6 authors at 2 institutions in 3 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Two malate dehydrogenase homologs, Pcal_0564 and Pcal_1699, have been found in the genome of Pyrobaculum calidifontis. The gene encoding Pcal_1699 consisted of 927 nucleotides corresponding to a polypeptide of 309 amino acids. To examine the properties of Pcal_1699, the structural gene was cloned, expressed in Escherichia coli and the purified gene product was characterized. Pcal_1699 was NADH specific enzyme exhibiting a high malate dehydrogenase activity (886 U/mg) at optimal pH (10) and temperature (90 °C). Unfolding studies suggested that urea could not induce complete unfolding and inactivation of Pcal_1699 even at a final concentration of 8 M; however, in the presence of 4 M guanidine hydrochloride enzyme structure was unfolded with complete loss of enzyme activity. Thermostability experiments revealed that Pcal_1699 is the most thermostable malate dehydrogenase, reported to date, retaining more than 90 % residual activity even after heating for 6 h in boiling water.
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