Structural and kinetic studies of a novel nerol dehydrogenase from Persicaria minor, a nerol-specific enzyme for citral biosynthesis

Plant Physiology and Biochemistry : PPB
Cheng Seng TanZamri Zainal

Abstract

Geraniol degradation pathway has long been elucidated in microorganisms through bioconversion studies, yet weakly characterised in plants; enzyme with specific nerol-oxidising activity has not been reported. A novel cDNA encodes nerol dehydrogenase (PmNeDH) was isolated from Persicaria minor. The recombinant PmNeDH (rPmNeDH) is a homodimeric enzyme that belongs to MDR (medium-chain dehydrogenases/reductases) superfamily that catalyses the first oxidative step of geraniol degradation pathway in citral biosynthesis. Kinetic analysis revealed that rPmNeDH has a high specificity for allylic primary alcohols with backbone ≤10 carbons. rPmNeDH has ∼3 fold higher affinity towards nerol (cis-3,7-dimethyl-2,6-octadien-1-ol) than its trans-isomer, geraniol. To our knowledge, this is the first alcohol dehydrogenase with higher preference towards nerol, suggesting that nerol can be effective substrate for citral biosynthesis in P. minor. The rPmNeDH crystal structure (1.54 Å) showed high similarity with enzyme structures from MDR superfamily. Structure guided mutation was conducted to describe the relationships between substrate specificity and residue substitutions in the active site. Kinetics analyses of wild-type rPmNeDH and several act...Continue Reading

Citations

Jan 10, 2019·Journal of Experimental Botany·Bernd Markus Lange, Narayanan Srividya
Jan 8, 2021·Frontiers in Bioengineering and Biotechnology·Ahmad Bazli RamziNigel S Scrutton
Feb 16, 2021·Plant Physiology and Biochemistry : PPB·Mahasakthy-Vijeyasri SatyaveanthanMaizom Hassan
Mar 11, 2020·Journal of Agricultural and Food Chemistry·Davide SlaghenaufiMaurizio Ugliano
Aug 31, 2021·Critical Reviews in Food Science and Nutrition·Zhenghui JiangChenyan Lv

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