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Ligand D-Ala-D-Ser 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 2 N2 O4
D-Ala-D-Ser
IPWKGIFRRBGCJO-QWWZWVQMSA-N
Roles as Enzyme Ligand
In Vivo Product in Enzyme-catalyzed Reactions (1 result)
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D-alanine + D-serine + ATP = D-alanyl-D-serine + ADP + phosphate
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Substrate in Enzyme-catalyzed Reactions (1 result)
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D-Ala-D-Ser + H2O = D-Ala + D-Ser
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Product in Enzyme-catalyzed Reactions (3 results)
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D-alanine + D-serine + ATP = D-alanyl-D-serine + ADP + phosphate
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ATP + D-alanine + D-serine = ADP + D-alanyl-D-serine + D-alanyl-D-alanine + D-seryl-D-serine
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ATP + D-serine = ADP + phosphate + D-alanyl-D-serine
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Inhibitor in Enzyme-catalyzed Reactions (1 result)
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Enzyme Kinetic Parameters
kcat Value (Turnover Number) (2 results)
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0.35
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wild-type, pH 7.5, 37°C
KM Value (2 results)
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15.5
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wild-type, pH 7.5, 37°C
References & Links Literature References (3)
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Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for vancomycin resistance in Enterococcus faecium BM4147
1995
Wu, Z.; Wright, G.D.; Walsh, C.T.
Biochemistry
34
2455-2463
Active-site mutants of the VanC2 D-alanyl-D-serine ligase, characteristic of one vancomycin-resistant bacterial phenotype, revert towards wild-type D-alanyl-D-alanine ligases
1998
Healy, V.L.; Park, I.S.; Walsh, C.T.
Chem. Biol.
5
197-207
Purification and characterization of VanXYc, a D,D-dipeptidase/D,D-carboxypeptidase in vancomycin-resisitant Enterococcus gallinarium BM4174
2002
Podmore, A.H.B.; Reynolds, P.E.
Eur. J. Biochem.
269
2740-2746
Links to other databases for D-Ala-D-Ser