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Isolation of cDNA for an NADP-malic enzyme from Aloe arborescens.

作者信息

Honda H, Shimada H, Akagi H

机构信息

Life Science Institute, Mitsui Chemicals, Inc., Mobara, Japan.

出版信息

DNA Res. 1997 Dec 31;4(6):397-400. doi: 10.1093/dnares/4.6.397.

Abstract

NADP-malic enzyme catalyzes the reaction of decarboxylation from malate. In CAM plants, functions of this enzyme diverged to include both photosynthetic and non-photosynthetic roles. A full length cDNA for an NADP-malic enzyme was isolated from an 'obligate' CAM plant aloe (Aloe arborescens). The cDNA contains an ORF encoding 592 amino acid residues, whose sequence is highly homologous to the known plant NADP-malic enzymes. This gene is constitutively expressed in all organs in a low level. The amount of the transcript exhibited no diurnal variation, suggesting that this gene is not involved in photosynthetic functions.

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