Biological and Pharmaceutical Bulletin
Online ISSN : 1347-5215
Print ISSN : 0918-6158
ISSN-L : 0918-6158
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Cloning and Functional Analysis of a Novel Aldo-Keto Reductase from Aloe arborescens
Hiroyuki MoritaYuusuke MizuuchiTsuyoshi AbeToshiyuki KohnoHiroshi NoguchiIkuro Abe
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2007 Volume 30 Issue 12 Pages 2262-2267

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Abstract

A novel aldo-keto reductase (AKR) was cloned and sequenced from roots of Aloe arborescens by a combination of RT-PCR using degenerate primers based on the conserved sequences of plant polyketide reductases (PKRs) and cDNA library screening by oligonucleotide hybridization. A. arborescens AKR share similarities with known plant AKRs (40—66% amino acid sequence identity), maintaining most of the active-site residues conserved in the AKR superfamily enzymes. Interestingly, despite the sequence similarity with PKRs, recombinant enzyme expressed in Escherichia coli did not exhibit any detectable PKR activities. Instead, A. arborescens AKR catalyzed NADPH-dependent reduction of various carbonyl compounds including benzaldehyde and DL-glyceraldehyde. Finally, a homology model on the basis of the crystal structure of Hordeum vulgare AKR predicted the active-site architecture of the enzyme.

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© 2007 The Pharmaceutical Society of Japan
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