Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Engineering Klebsiella sp. 601 multicopper oxidase enhances the catalytic efficiency towards phenolic substrates.

BMC biochemistry - 31 May 2011

Li Yadong, Gong Zijun, Li Xin, Li Yang, Wang Xing-Guo

Abstract excerpt

BACKGROUND: Structural comparison between bacterial CueO and fungal laccases has suggested that a charged residue Glu (E106) in CueO replaces the corresponding residue Phe in fungal laccases at the gate of the tunnel connecting type II copper to the protein surface and an extra α-helix (L351-G378) near the type I copper site covers the substrate binding pocket and might compromise the electron transfer from...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Substitution
Share to Biocatalysis
Share to Copper

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Klebsiella

Share to Oxidoreductases

Share to Phenols

Share to Protein Engineering

Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 21624144
DOI: 10.1186/1471-2091-12-30
PMCID: PMC3123277

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Engineering Klebsiella sp. 601 multicopper oxidase enhances the catalytic efficiency towards phenolic substrates.PMID 21624144Read ↗

The functional roles of the three copper sites associated with the methionine-rich insert in the multicopper oxidase CueO from E. coli.Semantic proximity Read ↗

Modifications of laccase activities of copper efflux oxidase, CueO by synergistic mutations in the first and second coordination spheres of the type I copper center.Semantic proximity Read ↗

The catalytic properties of Thermus thermophilus SG0.5JP17-16 laccase were regulated by the conformational dynamics of pocket loop 6.Semantic proximity Read ↗

A versatile and efficient markerless gene disruption system for Acidithiobacillus thiooxidans: application for characterizing a copper tolerance related multicopper oxidase gene.Semantic proximity Read ↗

Controlling the regiospecific oxidation of aromatics via active site engineering of toluene para-monooxygenase of Ralstonia pickettii PKO1.Semantic proximity Read ↗

Regulate catalytic performance by engineering non-regular structure of extradiol dioxygenase: An entrance to bottom strategy.Semantic proximity Read ↗

Artificial dicopper oxidase: rational reprogramming of bacterial metallo-β-lactamase into a catechol oxidase.Semantic proximity Read ↗

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

Enhancement in catalytic activity of CotA-laccase from Bacillus pumilus W3 via site-directed mutagenesis.Semantic proximity Read ↗

Amino acids located in the outer-sphere of the trinuclear copper center in a multicopper oxidase, CueO as the putative electron donor in the four-electron reduction of dioxygen.Semantic proximity Read ↗

Influencing the monophenolase/diphenolase activity ratio in tyrosinase.Semantic proximity Read ↗

Compensatory binding of an asparagine residue to the coordination-unsaturated type I Cu center in bilirubin oxidase mutants.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.