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Intracellular beta-carbonic anhydrase of the unicellular green alga Coccomyxa
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Institutionen för fysiologisk botanik. Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Umeå Plant Science Centre (UPSC).
Vise andre og tillknytning
1998 (engelsk)Inngår i: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 117, nr 4, s. 1341-1349Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Carbonic anhydrase (CA) (EC 4.2.1.1) enzymes catalyze the reversible hydration of CO,, a reaction that is important in many physiological processes. We have cloned and sequenced a full length cDNA encoding an intracellular P-CA from the unicellular green alga Coccomyxa. Nucleotide sequence data show that the isolated cDNA contains an open reading frame encoding a polypeptide of 227 amino acids. The predicted polypeptide is similar to beta-type CAs from Escherichia coli and higher plants, with an identity of 26% to 30%. The Coccomyxa cDNA was overexpressed in E. coli, and the enzyme was purified and biochemically characterized. The mature protein is a homotetramer with an estimated molecular mass of 100 kD. The CO2-hydration activity of the Coccomyxa enzyme is comparable with that of the pea homolog. However, the activity of Coccomyxa CA is largely insensitive to oxidative conditions, in contrast to similar enzymes from most higher plants. Fractionation studies further showed that Coccomyxa CA is extrachloroplastic.

sted, utgiver, år, opplag, sider
1998. Vol. 117, nr 4, s. 1341-1349
Identifikatorer
URN: urn:nbn:se:umu:diva-44629ISI: 000075485800023OAI: oai:DiVA.org:umu-44629DiVA, id: diva2:434815
Tilgjengelig fra: 2011-08-16 Laget: 2011-06-09 Sist oppdatert: 2018-06-08

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