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Article

Spatially remote motifs cooperatively affect substrate preference of a ruminal GH26-type endo-β-1,4-mannanase.

The Journal of biological chemistry - 10 Apr 2020

Mandelli Fernanda, de Morais Mariana Abrahão Bueno, de Lima Evandro Antonio, Oliveira Leane, Persinoti Gabriela Felix, Murakami Mário Tyago

Abstract excerpt

β-Mannanases from the glycoside hydrolase 26 (GH26) family are retaining hydrolases that are active on complex heteromannans and whose genes are abundant in rumen metagenomes and metatranscriptomes. These enzymes can exhibit distinct modes of substrate recognition and are often fused to carbohydrate-binding modules (CBMs), resulting in a molecular puzzle of mechanisms governing substrate preference and mode of...

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Identifiers

PMID: 32139511
DOI: 10.1074/jbc.RA120.012583
PMCID: PMC7152760

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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