Evidence map›Paper›PMID 39470852›Full record

ArticleBiodegradation2024

Mutations of methionine 444 interacting with T1Cu-coordinating amino acids affect the structure and function of multicopper oxidase CopA.

Wenwei Tang, Peiqi Zhang, Xiaoyu Jin, Xiaorong Li, Shichao Chen, Xinping Zeng

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

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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Wenwei TangSchool of Chemical Science and Engineering, Tongji University, Shanghai, 200092, China.
Peiqi ZhangSchool of Chemical Science and Engineering, Tongji University, Shanghai, 200092, China.
Xiaoyu JinSchool of Chemical Science and Engineering, Tongji University, Shanghai, 200092, China.
Xiaorong LiSchool of Chemical Science and Engineering, Tongji University, Shanghai, 200092, China.
Shichao ChenSchool of Life Sciences and Technology, Tongji University, Shanghai, 200092, China.
Xinping ZengSchool of Life Sciences and Technology, Tongji University, Shanghai, 200092, China. zengxp@tongji.edu.cn.

Funding

China Scholarship Council 201706265024National Natural Science Foundation of China 22176146Science and Technology Commission of Shanghai Municipality 19ZR1459400
6 · The paper itself

Abstract

Manganese is an essential trace element for humans, animals, and plants, but excessive amounts of manganese can cause serious harm to organisms. The biological manganese oxidation process mainly oxidizes Mn(II) through the secretion of unique manganese oxidase by manganese-oxidizing bacteria. The T1 Cu site of multicopper oxidase is the main site for substrate oxidation, and its role is to transfer electrons to TNC, where dioxygen reduction occurs. In this study, methionine (Met) No. 444 interacting with the T1Cu-coordinating amino acid in the multicopper oxidase CopA from Brevibacillus panacihumi MK-8 was mutated to phenylalanine (Phe) and leucine (Leu) by the enzyme. Based on the analysis of enzymatic properties and the structural model, the mutant protein M444F with 4.58 times the catalytic efficiency of the original protein CopA and the mutant protein M444L with 1.67 times the catalytic efficiency of the original protein CopA were obtained. The study showed that the manganese removal rate of the manganese-oxidizing engineered bacterium Rosetta-pET-copA

Indexed as

Bacterial ProteinsBrevibacillusManganeseMethionineBiodegradation, EnvironmentalCopperModels, MolecularMutationOxidation-ReductionOxidoreductasesBacterial ProteinsCopA protein, BacteriaCopperManganeseMethionineOxidoreductasesManganese oxidizing bacteriaManganese removalMulticopper oxidaseSite-directed mutagenesis

Identifiers

PMID39470852

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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.