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Article

Multi-method analysis revealed the mechanism of substrate selectivity in NHase: A gatekeeper residue at the activity center.

International journal of biological macromolecules - 1 Nov 2024

Meng Yiwei, Peplowski Lukasz, Wu Tong, Cheng Zhongyi, Han Laichuang, Qiao Jun, Cheng Zhongyi, Zhou Zhemin

Abstract excerpt

Recognizing the critical need to elucidate the molecular determinants of this selectivity offers a pathway to engineer enzymes with broader and more versatile catalytic capabilities. Through integrated methods including phylogenetic analysis, molecular docking, and structural analysis, we identified a pivotal amino acid residue, αTrp116, linking the substrate binding pocket and the active site of a NHase from...

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Identifiers

PMID: 39251006
DOI: 10.1016/j.ijbiomac.2024.135426

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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