The Effect of CBM1 and Linker on the Oxidase, Peroxidase and Monooxygenase Activities of AA9 LPMOs: Insight into Their Correlation with the Nature of Reductants and Crystallinity of Celluloses.

Xu Zhao, Fei Xie, Kaixiang Chen, Liangkun Long, Shaojun Ding

Abstract read

In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing 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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

5 authors.

Xu ZhaoThe Co-Innovation Center of Efficient Processing and Utilization of Forest Resources, Jiangsu Key Lab for the Chemistry & Utilization of Agricultural and Forest Biomass, College of Chemical Engineering, Nanjing Forestry University, Nanjing 210037, China.ORCID 0009-0000-6190-5346

Fei XieThe Co-Innovation Center of Efficient Processing and Utilization of Forest Resources, Jiangsu Key Lab for the Chemistry & Utilization of Agricultural and Forest Biomass, College of Chemical Engineering, Nanjing Forestry University, Nanjing 210037, China.

Kaixiang ChenThe Co-Innovation Center of Efficient Processing and Utilization of Forest Resources, Jiangsu Key Lab for the Chemistry & Utilization of Agricultural and Forest Biomass, College of Chemical Engineering, Nanjing Forestry University, Nanjing 210037, China.

Liangkun LongThe Co-Innovation Center of Efficient Processing and Utilization of Forest Resources, Jiangsu Key Lab for the Chemistry & Utilization of Agricultural and Forest Biomass, College of Chemical Engineering, Nanjing Forestry University, Nanjing 210037, China.

Shaojun DingThe Co-Innovation Center of Efficient Processing and Utilization of Forest Resources, Jiangsu Key Lab for the Chemistry & Utilization of Agricultural and Forest Biomass, College of Chemical Engineering, Nanjing Forestry University, Nanjing 210037, China.ORCID 0000-0002-8359-9252

Funding

National Natural Science Foundation of China 22178179

6 · The paper itself

Abstract

This study explores the effect of carbohydrate-binding module 1 (CBM1) and the linker on the function of auxiliary activity 9 (AA9) lytic polysaccharide monooxygenases (LPMOs), with a particular focus on monooxygenase activity, using different crystallinity celluloses and electron donors. The tested C1/C4-oxidizing AA9 LPMOs exhibited higher oxidase and peroxidase activities compared to those of the C4-oxidizing AA9 LPMOs. While the presence of CBM1 promoted cellulose-binding affinity, it reduced the oxidase activity of modular AA9 LPMOs. The effect of CBM1 on peroxidase activity was variable and enzyme-specific. Its influence on monooxygenase activity was linked to the type of reductants and the crystallinity of celluloses. Overall, CBM1 improved the monooxygenase activity on high-, medium-, and low-crystallinity celluloses when ascorbic acid (AscA) was used as the electron donor. CBM1 also facilitated monooxygenase activity on high-crystallinity cellulose, but significantly inhibited monooxygenase activity on low-crystallinity cellulose when cellobiose dehydrogenase (CDH) was the electron donor. Linker truncation of

Indexed as

CelluloseMixed Function OxygenasesCarbohydrate DehydrogenasesOxidation-ReductionOxidoreductasesPeroxidaseReducing AgentsCarbohydrate DehydrogenasesCelluloseMixed Function OxygenasesOxidoreductasesPeroxidaseReducing Agentscarbohydrate-binding module 1electron donorH2O2linkerlytic polysaccharide monooxygenases

Identifiers

PMID39684327

DOI10.3390/ijms252312616

PMCPMC11641334

What Socratic holds

Textmetadata

LicenceCC BY

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 Socratic graph.