Evidence map›Paper›PMID 29971843›Full record

ArticleProtein science : a publication of the Protein Society2018

Methylation of the N-terminal histidine protects a lytic polysaccharide monooxygenase from auto-oxidative inactivation.

Dejan M Petrović, Bastien Bissaro, Piotr Chylenski, Morten Skaugen, Morten Sørlie, Marianne S Jensen, Finn L Aachmann, Gaston Courtade, Anikó Várnai, Vincent G H Eijsink

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
5.8field-weighted citation impact, top 3% of its field
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

49 citing papers in PubMed, 123 citations in OpenAlex.

  1. Review
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  15. Histidine oxidation in lytic polysaccharide monooxygenase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023
    Article
  16. Article
  17. Review
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  20. Orchestrating copper binding: structure and variations on the cupredoxin fold.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Review
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

10 authors at 2 institutions in 1 country.

Dejan M PetrovićFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Ås, Norway.
Bastien BissaroFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Ås, Norway.
Piotr ChylenskiFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Ås, Norway.
Morten SkaugenFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Ås, Norway.
Morten SørlieFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Ås, Norway.
Marianne S JensenFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Ås, Norway.
Finn L AachmannDepartment of Biotechnology and Food Science, NOBIPOL, Norwegian University of Science and Technology (NTNU), Trondheim, Norway.
Gaston CourtadeDepartment of Biotechnology and Food Science, NOBIPOL, Norwegian University of Science and Technology (NTNU), Trondheim, Norway.
Anikó VárnaiFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Ås, Norway.
Vincent G H EijsinkFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Ås, Norway.ORCID 0000-0002-9220-8743
Norwegian University of Life Sciences · NONorwegian University of Science and Technology · NO

Funding

Norges Forskningsråd 226244Norges Forskningsråd 243663
6 · The paper itself

Abstract

The catalytically crucial N-terminal histidine (His1) of fungal lytic polysaccharide monooxygenases (LPMOs) is post-translationally modified to carry a methylation. The functional role of this methylation remains unknown. We have carried out an in-depth functional comparison of two variants of a family AA9 LPMO from Thermoascus aurantiacus (TaLPMO9A), one with, and one without the methylation on His1. Various activity assays showed that the two enzyme variants are identical in terms of substrate preferences, cleavage specificities and the ability to activate molecular oxygen. During the course of this work, new functional features of TaLPMO9A were discovered, in particular the ability to cleave xyloglucan, and these features were identical for both variants. Using a variety of techniques, we further found that methylation has minimal effects on the pK

Indexed as

Aspergillus oryzaeBiocatalysisHistidineMethylationMixed Function OxygenasesOxidation-ReductionPichiaPolysaccharidesProtein Processing, Post-TranslationalThermoascusHistidineMixed Function OxygenasesPolysaccharideshistidinehydrogen peroxidelytic polysaccharide monooxygenasemethylationThermoascus aurantiacus

Identifiers

PMID29971843
PMCPMC6194291
OpenAlexW2811086611

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.