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Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima.

Abstract:

TM0077 from Thermotoga maritima is a member of the carbohydrate esterase family 7 and is active on a variety of acetylated compounds, including cephalosporin C. TM0077 esterase activity is confined to short-chain acyl esters (C2-C3), and is optimal around 100°C and pH 7.5. The positional specificity of TM0077 was investigated using 4-nitrophenyl-β-D-xylopyranoside monoacetates as substrates in a β-xylosidase-coupled assay. TM0077 hydrolyzes acetate at positions 2, 3, and 4 with equal efficien...

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Publisher copy:
10.1002/prot.24041

Authors


Levisson, M More by this author
Deller, MC More by this author
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Journal:
Proteins
Volume:
80
Issue:
6
Pages:
1545-1559
Publication date:
2012-06-05
DOI:
EISSN:
1097-0134
ISSN:
0887-3585
URN:
uuid:28254dc8-135f-4db7-be26-4104f05968f9
Source identifiers:
316402
Local pid:
pubs:316402

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