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2.6
-
pH not specified in the publication, temperature not specified in the publication
4.5
-
mutant A163C/S244C, at pH 7.5 and 32°C
5.5
-
mutant N261A, at pH 7.5 and 32°C
5.9
-
wild type enzyme, at pH 7.5 and 32°C
5.9
-
wild-type, pH 7.5, 32°C
6
-
mutant A163C, at pH 7.5 and 32°C
6.2
-
mutant S244C, at pH 7.5 and 32°C
6.8
-
mutant S205A, at pH 7.5 and 32°C
6.8
-
mutant S205A, pH 7.5, 32°C
6.9
-
mutant S167A, at pH 7.5 and 32°C
7.1
-
mutant P198A, at pH 7.5 and 32°C
7.1
-
mutant P198A, pH 7.5, 32°C
8
-
mutant F263Y, at pH 7.5 and 32°C
8
-
mutant F263Y, pH 7.5, 32°C
9.7
-
mutant V265T, at pH 7.5 and 32°C
16.2
-
mutant V265A, at pH 7.5 and 32°C
17.3
-
mutant S165A, at pH 7.5 and 32°C
17.3
-
mutant S165A, pH 7.5, 32°C
19.6
-
mutant F242Y, at pH 7.5 and 32°C
19.6
-
mutant F242Y, pH 7.5, 32°C
24.6
-
mutant V265L, at pH 7.5 and 32°C
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Functional expression of the ectoine hydroxylase gene (thpD) from Streptomyces chrysomallus in Halomonas elongata
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Crystal structure of the ectoine hydroxylase, a snapshot of the active site
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Molecular dynamics simulations and structure-guided mutagenesis provide insight into the architecture of the catalytic core of the ectoine hydroxylase
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Molecular dynamics simulations and structure-guided mutagenesis provide insight into the architecture of the catalytic core of the ectoine hydroxylase
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Ectoine hydroxylase displays selective trans-3-hydroxylation activity towards L-proline
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Exploiting substrate promiscuity of ectoine hydroxylase for regio- and stereoselective modification of homoectoine
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Czech, L.; Wilcken, S.; Czech, O.; Linne, U.; Brauner, J.; Smits, S.H.J.; Galinski, E.A.; Bremer, E.
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2745