ArticleExtremophiles : life under extreme conditions2013
Purification and biochemical characterisation of a glucose-6-phosphate dehydrogenase from the psychrophilic green alga Koliella antarctica.
Article in Extremophiles : life under extreme conditions, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- Glucose-6-Phosphate Dehydrogenases: The Hidden Players of Plant Physiology.International journal of molecular sciences · 2022Review
- Cloning, Expression, and Characterization of a Psychrophilic Glucose 6-Phosphate Dehydrogenase fromInternational journal of molecular sciences · 2019Article
- Comparative analysis of photosynthetic and respiratory parameters in the psychrophilic unicellular green algaPhysiology and molecular biology of plants : an international journal of functional plant biology · 2018Article
- Nitrogen Assimilation, Abiotic Stress and Glucose 6-Phosphate Dehydrogenase: The Full Circle of Reductants.Plants (Basel, Switzerland) · 2016Review
- Polar Microalgae: New Approaches towards Understanding Adaptations to an Extreme and Changing Environment.Biology · 2014Article
- The Antarctic Chlamydomonas raudensis: an emerging model for cold adaptation of photosynthesis.Extremophiles : life under extreme conditions · 2013Review
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4 authors at 2 institutions in 2 countries.
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Abstract
Psychrophilic organisms have evolved a number of modifications of cellular structures to survive in the cold environment; among them it is worth noting an increased efficiency of enzymes at lower temperatures. Glucose-6-phosphate dehydrogenase (G6PDH; EC 1.1.1.49) was purified and characterised from the psychrophilic green alga Koliella antarctica (Trebouxiophyceae, Chlorophyta) from the Ross Sea (Antarctica). It was possible to isolate a single G6PDH using biochemical strategies; its maximum activity was measured at 35 °C, and the enzyme showed an E (a) of 39.6 kJ mol(-1). This protein reacted with antibodies raised against higher plants plastidic isoforms. KaG6PDH showed peculiar kinetic properties, with a K (iNADPH) value lower than [Formula: see text]. Notably, catalytic activity was inactivated in vitro by DTT and chloroplastic thioredoxin f. These biochemical properties of G6PDH are discussed with respect to higher plant G6PDHs and the adaptation of K. antarctica to polar low-temperature environment.
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