Literature DB >> 20834142

Functional analysis of the carbohydrate-binding module of an esterase from Neisseria sicca SB involved in the degradation of cellulose acetate.

Kunihiko Moriyoshi1, Daisuke Koma, Hayato Yamanaka, Takashi Ohmoto, Kiyofumi Sakai.   

Abstract

An esterase gene from Neisseria sicca SB encoding CaeA, which catalyzes the deacetylation of cellulose acetate, was cloned. CaeA contained a putative catalytic domain of carbohydrate esterase family 1 and a carbohydrate-binding module (CBM) family 2. We constructed two derivatives, with and without the CBM of CaeA. Binding assay indicated that the CBM of CaeA had an affinity for cellulose.

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Year:  2010        PMID: 20834142     DOI: 10.1271/bbb.100213

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  2 in total

1.  Crystal structure of acetylxylan esterase from Caldanaerobacter subterraneus subsp. tengcongensis.

Authors:  Kohei Sasamoto; Tomoki Himiyama; Kunihiko Moriyoshi; Takashi Ohmoto; Koichi Uegaki; Yoshiaki Nishiya; Tsutomu Nakamura
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2021-10-19       Impact factor: 1.056

2.  Role for a Lytic Polysaccharide Monooxygenase in Cell Wall Remodeling in Streptomyces coelicolor.

Authors:  Xiaobo Zhong; Le Zhang; Gilles P van Wezel; Erik Vijgenboom; Dennis Claessen
Journal:  mBio       Date:  2022-03-31       Impact factor: 7.786

  2 in total

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