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Ligand beta-Asp-Gly Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C6 H1 0 N2 O5
beta-Asp-Gly
ZTEDWFWBGPKUOD-VKHMYHEASA-N
Roles as Enzyme Ligand
Substrate in Enzyme-catalyzed Reactions (1 result)
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beta-Asp-Gly + H2O = Asp + Gly
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Enzyme Kinetic Parameters
kcat Value (Turnover Number) (2 results)
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0.93
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wild-type enzyme, pH 8.1, 30°C
KM Value (2 results)
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18
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wild-type enzyme, pH 8.1, 30°C
References & Links Literature References (4)
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beta-Aspartyl peptidase from rat liver
1970
Haley, E.E.
Methods Enzymol.
19
737-741
Determination of beta-aspartylpeptidase activity in human faeces by high-performance liquid chromatography using pre-column derivatization with phenyl isothiocyanate
1986
van der Leij, F.R.; Welling, G.W.
J. Chromatogr.
383
35-42
Mechanism of the reaction catalyzed by isoaspartyl dipeptidase from Escherichia coli
2005
Marti-Arbona, R.; Fresquet, V.; Thoden, J.B.; Davis, M.L.; Holden, H.M.; Raushel, F.M.
Biochemistry
44
7115-7124
Crystal structure and functional characterization of an isoaspartyl dipeptidase (CpsIadA) from Colwellia psychrerythraea strain 34H
2017
Park, S.H.; Lee, C.W.; Lee, S.G.; Shin, S.C.; Kim, H.J.; Park, H.; Lee, J.H.
PLoS ONE
12
e0181705
Links to other databases for beta-Asp-Gly