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Article

Structure-Function Relationship of the β-Hairpin of Thermus thermophilus HB27 Laccase.

International journal of molecular sciences - 16 Jan 2025

Miranda-Zaragoza Beatriz, Huerta-Miranda Guillermo A, García-García Wendy I, Hernández-Álvarez Elizabeth, Solano-Peralta Alejandro, Lee Jaeyong, Strynadka Natalie, Miranda-Hernández Margarita, Rodríguez-Almazán Claudia

Abstract excerpt

Thermus thermophilus HB27 laccase (Tth-Lac) is a thermostable enzyme that contains a β-hairpin (Ala292-Gln307) covering the substrate entrance. We analyzed the role of this β-hairpin in the enzymatic activity of Tth-Lac through three β-hairpin mutants: two variants without the β-hairpin (C1Tth-Lac and C2Tth-Lac) and one with a partially modified β-hairpin (P1Tth-Lac). Enzymatic activity was assayed with different...

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Topics

Thermus thermophilus
Laccase
Copper
Structure-Activity Relationship
Models, Molecular

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Bacterial Proteins

Substrate Specificity

Crystallography, X-Ray

Mutation

Source

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Identifiers

PMID: 39859450
DOI: 10.3390/ijms26020735
PMCID: PMC11766367

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