Comments: |
The enzyme, characterized from the archaeons Thermococcus kodakarensis and Pyrococcus horikoshii, deacetylates the non-reducing residue of N,N′-diacetylchitobiose, the end product of the archaeal chitinase, to produce β-D-glucosaminyl-(1→4)-N-acetyl-D-glucosamine. This is in contrast to EC 3.5.1.105, chitin disaccharide deacetylase, which deacetylates N,N′-diacetylchitobiose at the reducing residue to produce N-acetyl-β-D-glucosaminyl-(1→4)-D-glucosamine. |
References: |
1. |
Tanaka, T., Fukui, T., Fujiwara, S., Atomi, H. and Imanaka, T. Concerted action of diacetylchitobiose deacetylase and exo-β-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Biol. Chem. 279 (2004) 30021–30027. [DOI] [PMID: 15136574] |
2. |
Mine, S., Ikegami, T., Kawasaki, K., Nakamura, T. and Uegaki, K. Expression, refolding, and purification of active diacetylchitobiose deacetylase from Pyrococcus horikoshii. Protein Expr. Purif. 84 (2012) 265–269. [DOI] [PMID: 22713621] |
3. |
Nakamura, T., Yonezawa, Y., Tsuchiya, Y., Niiyama, M., Ida, K., Oshima, M., Morita, J. and Uegaki, K. Substrate recognition of N,N′-diacetylchitobiose deacetylase from Pyrococcus horikoshii. J. Struct. Biol. 195:S1047-8477( (2016). [DOI] [PMID: 27456364] |
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