Ligand GDP-4-amino-4,6-dideoxy-alpha-D-mannose
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Basic Ligand Information
Molecular Structure

C16H26N6O14P2
GDP-4-amino-4,6-dideoxy-alpha-D-mannose
PMFIPWCEUCAMAY-YVXBHLEUSA-N
GDP-alpha-D-perosamine, GDP-D-perosamine
Show all BRENDA pathways known for GDP-4-amino-4,6-dideoxy-alpha-D-mannose
Roles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)
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10-formyltetrahydrofolate + GDP-alpha-D-perosamine = tetrahydrofolate + GDP-N-formyl-alpha-D-perosamine
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acetyl-CoA + GDP-4-amino-4,6-dideoxy-alpha-D-mannose = CoA + GDP-4-acetamido-4,6-dideoxy-alpha-D-mannose
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In Vivo Product in Enzyme-catalyzed Reactions (3 results)
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GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate = GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
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GDP-4-dehydro-6-deoxy-D-mannose + L-glutamate = GDP-alpha-D-perosamine + 2-oxoglutarate
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GDP-4-dehydro-6-deoxy-D-mannose + L-glutamate = GDP-D-perosamine + 2-oxoglutarate
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Substrate in Enzyme-catalyzed Reactions (3 results)
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10-formyltetrahydrofolate + GDP-alpha-D-perosamine = tetrahydrofolate + GDP-N-formyl-alpha-D-perosamine
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acetyl-CoA + GDP-4-amino-4,6-dideoxy-alpha-D-mannose = CoA + GDP-4-acetamido-4,6-dideoxy-alpha-D-mannose
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GDP-D-perosamine + L-glutamate = GDP-4-dehydro-3,6-dideoxymannose + 2-oxoglutarate + ammonia
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Product in Enzyme-catalyzed Reactions (3 results)
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GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate = GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
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GDP-4-dehydro-6-deoxy-D-mannose + L-glutamate = GDP-alpha-D-perosamine + 2-oxoglutarate
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GDP-4-dehydro-6-deoxy-D-mannose + L-glutamate = GDP-D-perosamine + 2-oxoglutarate
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Inhibitor in Enzyme-catalyzed Reactions (1 result)
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substrate inhibition by GDP-alpha-D-perosamine is evident above 0.25 mM
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3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)
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Enzyme Kinetic Parameters
kcat Value (Turnover Number) (1 result)
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0.54
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mutant enzyme D78A/F142A, at pH 8.0, temperature not specified in the publication
KM Value (2 results)
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0.46
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mutant enzyme D78A/F142A, at pH 8.0, temperature not specified in the publication
References & Links
Literature References (4)
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Identification of the GDP-N-acetyl-d-perosamine producing enzymes from Escherichia coli O157:H7
2008
Albermann, C.; Beuttler, H.
FEBS Lett.
582
479-484
GDP-4-keto-6-deoxy-D-mannose 3-dehydratase, accommodating a sugar substrate in the active site
2008
Cook, P.; Holden, H.
J. Biol. Chem.
283
4295-4303
Biochemical Characterization of WbkC, an N-Formyltransferase from Brucella melitensis
2017
Riegert, A.S.; Chantigian, D.P.; Thoden, J.B.; Tipton, P.A.; Holden, H.M.
Biochemistry
56
3657-3668
Genetic organisation of the lipopolysaccharide O-antigen biosynthesis region of Brucella melitensis 16M (wbk)
2000
Godfroid, F.; Cloeckaert, A.; Taminiau, B.; Danese, I.; Tibor, A.; De Bolle, X.; Mertens, P.; Letesson, J.
Res. Microbiol.
151
655-668
Links to other databases for GDP-4-amino-4,6-dideoxy-alpha-D-mannose