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Literature summary for 5.1.3.20 extracted from

  • Morrison, J.P.; Read, J.A.; Coleman, W.G., Jr.; Tanner, M.E.
    Dismutase activity of ADP-L-glycero-D-manno-heptose 6-epimerase: evidence for a direct oxidation/reduction mechanism (2005), Biochemistry, 44, 5907-5915.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP-beta-D-manno-hexadialdose the intermediate ADP-beta-D-manno-hexadialdose undergoes dismutation into equal amounts of ADP-beta-D-mannuronic acid and ADP-beta-D-mannose Escherichia coli ADP-beta-D-mannuronic acid + ADP-beta-D-mannose
-
?
ADP-D-glycero-D-manno-heptose direct C-6'‘ oxidation/reduction mechanism Escherichia coli ADP-L-glycero-D-manno-heptose
-
?

Synonyms

Synonyms Comment Organism
ADP-L,D-hep 6-epimerase
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Escherichia coli
hldD
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Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADP+ bound to the enzyme, involved in catalysis Escherichia coli