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8JQE

Structure of CmCBDA in complex with Mn2+ and glycerol

Summary for 8JQE
Entry DOI10.2210/pdb8jqe/pdb
DescriptorYdjC family protein, GLYCEROL, MANGANESE (II) ION, ... (5 entities in total)
Functional Keywordscmcbda, n-acetylglucosamine deacetylase, mentalloenzyme, enzyme engineering, hydrolase
Biological sourceCyclobacterium marinum
Total number of polymer chains2
Total formula weight71152.37
Authors
Li, X. (deposition date: 2023-06-14, release date: 2024-01-03, Last modification date: 2024-01-24)
Primary citationHu, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.31 Å)
Structure validation

227344

數據於2024-11-13公開中

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