In:
FEBS Letters, Wiley, Vol. 590, No. 8 ( 2016-04), p. 1242-1252
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1002/1873-3468.12135
Language:
English
Publisher:
Wiley
Publication Date:
2016
detail.hit.zdb_id:
1460391-3
SSG:
12
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