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Structural and biochemical characterization of a carbohydrate acetylesterase from Sinorhizobium meliloti 1021
Author(s) -
Kim Kyungmin,
Ryu Bum Han,
Kim Sung Soo,
An Deu Rae,
Ngo Tri Duc,
Pandian Ramesh,
Kim Kyeong Kyu,
Kim T. Doohun
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.11.033
Subject(s) - sinorhizobium meliloti , carbohydrate , biochemistry , esterase , chemistry , polysaccharide , sinorhizobium , biology , enzyme , gene , bacteria , rhizobiaceae , genetics , symbiosis , mutant
In many microorganisms, carbohydrate acetylesterases remove the acetyl groups from various types of carbohydrates. Sm23 from Sinorhizobium meliloti is a putative member of carbohydrate esterase family 3 (CE3) in the CAZy classification system. Here, we determined the crystal structure of Sm23 at 1.75 Å resolution and investigated functional properties using biochemical methods. Furthermore, immobilized Sm23 exhibited improved stability compared with soluble Sm23, which can be used for the design of plant cell wall degrading‐systems.