8JQF

Structure of CmCBDA in complex with Ni2+ and Glycerol

8JQF の概要

• エントリーDOI: 10.2210/pdb8jqf/pdb
• 分子名称: YdjC family protein, GLYCEROL, NICKEL (II) ION, ... (5 entities in total)
• 機能のキーワード: cmcbda, n-acetylglucosamine deacetylase, mentalloenzyme, enzyme engineering, hydrolase
• 由来する生物種: Cyclobacterium marinum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71162.07

構造登録者

Li, X. (登録日: 2023-06-14, 公開日: 2024-01-03, 最終更新日: 2024-01-24)

主引用文献

Hu, S.,Xu, L.,Xie, C.,Hong, J.
Structural Insights into the Catalytic Activity of Cyclobacterium marinum N -Acetylglucosamine Deacetylase.
J.Agric.Food Chem., 72:783-793, 2024

PubMed Abstract: -Acetylglucosamine deacetylase from (CmCBDA) is a highly effective and selective biocatalyst for the production of d-glucosamine (GlcN) from -acetylglucosamine (GlcNAc). However, the underlying catalytic mechanism remains elusive. Here, we show that CmCBDA is a metalloenzyme with a preference for Ni over Mn. Crystal structures of CmCBDA in complex with Ni and Mn revealed slight remodeling of the CmCBDA active site by the metal ions. We also demonstrate that CmCBDA exists as a mixture of homodimers and monomers in solution, and dimerization is indispensable for catalytic activity. A mutagenesis analysis also indicated that the active site residues Asp22, His72, and His143 as well as the residues involved in dimerization, Pro52, Trp53, and Tyr55, are essential for catalytic activity. Furthermore, a mutation on the protein surface, Lys219Glu, resulted in a 2.3-fold improvement in the deacetylation activity toward GlcNAc. Mechanistic insights obtained here may facilitate the development of CmCBDA variants with higher activities.

PubMed: 38141024
DOI: 10.1021/acs.jafc.3c06146

実験手法

X-RAY DIFFRACTION (1.85 Å)