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Literature summary for 4.2.1.168 extracted from

  • Cook, P.; Holden, H.
    GDP-4-keto-6-deoxy-D-mannose 3-dehydratase, accommodating a sugar substrate in the active site (2008), J. Biol. Chem., 283, 4295-4303.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
H188N mutant with bound GDP-perosamine, to 1.7 A resolution. The sugar analog is trapped in the active site as an external aldimine. The active site is positioned between the two subunits of the dimer. The diphosphoryl groups of the ligand are anchored to the protein via Arg219 and Arg331, the hydroxyl groups of the hexose only lie within hydrogen bonding distance to ordered water molecules. The hexose moiety of the ligand adopts a boat rather than the typically observed chair conformation Escherichia coli

Protein Variants

Protein Variants Comment Organism
H188K mutant protein cannot catalyze the dehydration step Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli Q9F118
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GDP-4-dehydro-alpha-D-rhamnose + L-glutamate
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Escherichia coli GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + 2-oxoglutarate + ammonia
-
?
GDP-D-perosamine + L-glutamate
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Escherichia coli GDP-4-dehydro-3,6-dideoxymannose + 2-oxoglutarate + ammonia wild-type ColD is able to catalyze the production of GDP-4-keto-3,6-dideoxymannose using GDP-perosamine instead of GDP-4-keto-6-deoxymannose as a substrate ?