Evidence map›Paper›PMID 16830185›Full record

ArticlePlant molecular biology2006

Evolution of novel O-methyltransferases from the Vanilla planifolia caffeic acid O-methyltransferase.

Huaijun Michael Li, David Rotter, Thomas G Hartman, Fulya E Pak, Daphna Havkin-Frenkel, Faith C Belanger

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Article in Plant molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Frontiers in plant science · 2023
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Molecular Cloning and Characterization of aInternational journal of molecular sciences · 2018
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Huaijun Michael LiDepartment of Plant Biology and Pathology and The Biotechnology Center for Agriculture & the Environment, Cook College, Rutgers University, 59 Dudley Road, New Brunswick, NJ 08901, USA.
David Rotter
Thomas G Hartman
Fulya E Pak
Daphna Havkin-Frenkel
Faith C Belanger

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biosynthesis of many plant secondary compounds involves the methylation of one or more hydroxyl groups, catalyzed by O-methyltransferases (OMTs). Here, we report the characterization of two OMTs, Van OMT-2 and Van OMT-3, from the orchid Vanilla planifolia Andrews. These enzymes catalyze the methylation of a single outer hydroxyl group in substrates possessing a 1,2,3-trihydroxybenzene moiety, such as methyl gallate and myricetin. This is a substrate requirement not previously reported for any OMTs. Based on sequence analysis these enzymes are most similar to caffeic acid O-methyltransferases (COMTs), but they have negligible activity with typical COMT substrates. Seven of 12 conserved substrate-binding residues in COMTs are altered in Van OMT-2 and Van OMT-3. Phylogenetic analysis of the sequences suggests that Van OMT-2 and Van OMT-3 evolved from the V. planifolia COMT. These V. planifolia OMTs are new instances of COMT-like enzymes with novel substrate preferences.

Indexed as

Evolution, MolecularAmino Acid SequenceCloning, MolecularDNA, ComplementaryEscherichia coliMethyltransferasesMolecular Sequence DataPhylogenyPlant ProteinsSequence AlignmentSubstrate SpecificityVanillacaffeate O-methyltransferaseDNA, ComplementaryMethyltransferasesPlant Proteins

Identifiers

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.