↓ Skip to main content

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

Overview of attention for article published in Plant Physiology & Biochemistry, February 2018
Altmetric Badge

About this Attention Score

  • Average Attention Score compared to outputs of the same age
  • Above-average Attention Score compared to outputs of the same age and source (62nd percentile)

Mentioned by

twitter
2 tweeters

Citations

dimensions_citation
9 Dimensions

Readers on

mendeley
37 Mendeley
You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output. Click here to find out more.
Title
Structural and kinetic studies of a novel nerol dehydrogenase from Persicaria minor , a nerol-specific enzyme for citral biosynthesis
Published in
Plant Physiology & Biochemistry, February 2018
DOI 10.1016/j.plaphy.2017.12.033
Pubmed ID
Authors

Cheng Seng Tan, Maizom Hassan, Zeti Azura Mohamed Hussein, Ismanizan Ismail, Kok Lian Ho, Chyan Leong Ng, Zamri 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 active site mutants demonstrated that the substrate specificity of rPmNeDH can be altered by changing any selected active site residues (Asp280, Leu294 and Ala303). Interestingly, the L294F, A303F and A303G mutants were able to revamp the substrate preference towards geraniol. Furthermore, mutant that exhibited a broader substrate range was also obtained. This study demonstrates that P. minor may have evolved to contain enzyme that optimally recognise cis-configured nerol as substrate. rPmNeDH structure provides new insights into the substrate specificity and active site plasticity in MDR superfamily.

Twitter Demographics

The data shown below were collected from the profiles of 2 tweeters who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 37 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 37 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 8 22%
Student > Master 7 19%
Student > Bachelor 5 14%
Lecturer > Senior Lecturer 3 8%
Student > Doctoral Student 2 5%
Other 5 14%
Unknown 7 19%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 15 41%
Agricultural and Biological Sciences 8 22%
Chemistry 2 5%
Nursing and Health Professions 1 3%
Economics, Econometrics and Finance 1 3%
Other 1 3%
Unknown 9 24%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 12 February 2018.
All research outputs
#7,842,738
of 12,498,628 outputs
Outputs from Plant Physiology & Biochemistry
#401
of 1,204 outputs
Outputs of similar age
#195,113
of 344,703 outputs
Outputs of similar age from Plant Physiology & Biochemistry
#15
of 48 outputs
Altmetric has tracked 12,498,628 research outputs across all sources so far. This one is in the 23rd percentile – i.e., 23% of other outputs scored the same or lower than it.
So far Altmetric has tracked 1,204 research outputs from this source. They receive a mean Attention Score of 1.4. This one has gotten more attention than average, scoring higher than 58% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 344,703 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 33rd percentile – i.e., 33% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 48 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 62% of its contemporaries.