Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima
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...
Hlavní autoři: | Levisson, M, Han, G, Deller, M, Xu, Q, Biely, P, Hendriks, S, Ten Eyck, L, Flensburg, C, Roversi, P, Miller, MD, McMullan, D, von Delft, F, Kreusch, A, Deacon, A, van der Oost, J, Lesley, SA, Elsliger, M, Kengen, S, Wilson, I |
---|---|
Médium: | Journal article |
Jazyk: | English |
Vydáno: |
2012
|
Podobné jednotky
-
Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima.
Autor: Levisson, M, a další
Vydáno: (2012) -
Characterization of exceptionally thermostable single-stranded DNA-binding proteins from <it>Thermotoga maritima </it>and <it>Thermotoga neapolitana</it>
Autor: Mickiewicz Małgorzata, a další
Vydáno: (2010-10-01) -
Crystal structure of O-acetylserine sulfhydrylase (TM0665) from Thermotoga maritima at 1.8 A resolution.
Autor: Heine, A, a další
Vydáno: (2004) -
Crystal structure of an HEPN domain protein (TM0613) from Thermotoga maritima at 1.75 A resolution.
Autor: Erlandsen, H, a další
Vydáno: (2004) -
Crystal structure of gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.0 A resolution.
Autor: Page, R, a další
Vydáno: (2004)