2Y8U

A. nidulans chitin deacetylase

Summary for 2Y8U

• Entry DOI: 10.2210/pdb2y8u/pdb
• Descriptor: CHITIN DEACETYLASE, PHOSPHATE ION, COBALT (II) ION, ... (6 entities in total)
• Functional Keywords: hydrolase
• Biological source: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
• Total number of polymer chains: 2
• Total formula weight: 51669.16

Authors

Penman, G.,Gay, L.M.,van Aalten, D.M.F. (deposition date: 2011-02-10, release date: 2012-02-22, Last modification date: 2024-05-08)

Primary citation

Liu, Z.,Gay, L.M.,Tuveng, T.R.,Agger, J.W.,Westereng, B.,Mathiesen, G.,Horn, S.J.,Vaaje-Kolstad, G.,van Aalten, D.M.F.,Eijsink, V.G.H.
Structure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A4.
Sci Rep, 7:1746-1746, 2017

PubMed Abstract: Enzymatic conversion of chitin, a β-1,4 linked polymer of N-acetylglucosamine, is of major interest in areas varying from the biorefining of chitin-rich waste streams to understanding how medically relevant fungi remodel their chitin-containing cell walls. Although numerous chitinolytic enzymes have been studied in detail, relatively little is known about enzymes capable of deacetylating chitin. We describe the structural and functional characterization of a 237 residue deacetylase (AnCDA) from Aspergillus nidulans FGSC A4. AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and acetylxylan, but not on peptidoglycan. The K and k of AnCDA for the first deacetylation of penta-N-acetyl-chitopentaose are 72 µM and 1.4 s, respectively. Combining mass spectrometry and analyses of acetate release, it was shown that AnCDA catalyses mono-deacetylation of (GlcNAc) and full deacetylation of (GlcNAc) in a non-processive manner. Deacetylation of the reducing end sugar was much slower than deacetylation of the other sugars in chito-oligomers. These enzymatic characteristics are discussed in the light of the crystal structure of AnCDA, providing insight into how the chitin deacetylase may interact with its substrates. Interestingly, AnCDA activity on crystalline chitin was enhanced by a lytic polysaccharide monooxygenase that increases substrate accessibility by oxidative cleavage of the chitin chains.

PubMed: 28496100
DOI: 10.1038/s41598-017-02043-1

Experimental method

X-RAY DIFFRACTION (1.99 Å)