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Structural and Biochemical Characterization of an Octameric Carbohydrate Acetylesterase from Sinorhizobium meliloti
Author(s) -
Oh Changsuk,
Ryu Bum Han,
An Deu Rae,
Nguyen Duy Duc,
Yoo Wanki,
Kim Truc,
Ngo Tri Duc,
Kim Hee Sook,
Kim Kyeong Kyu,
Kim T. Doohun
Publication year - 2016
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 - 10.1002/1873-3468.12135
Subject(s) - sinorhizobium meliloti , carbohydrate binding module , biochemistry , carbohydrate , chemistry , mutant , biology , crystallography , glycoside hydrolase , enzyme , gene
Carbohydrate acetylesterases, which have a highly specific role among plant‐interacting bacterial species, remove the acetyl groups from plant carbohydrates. Here, we determined the crystal structure of Est24, an octameric carbohydrate acetylesterase from Sinorhizobium meliloti , at 1.45 Å resolution and investigated its biochemical properties. The structure of Est24 consisted of five parallel β strands flanked by α helices, which formed an octameric assembly with two distinct interfaces. The deacetylation activity of Est24 and its mutants around the substrate‐binding pocket was investigated using several substrates, including glucose pentaacetate and acetyl alginate. Elucidation of the structure‐function relationships of Est24 could provide valuable opportunities for biotechnological explorations.