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Literature summary for 1.1.1.282 extracted from

  • Benach, J.; Lee, I.; Edstrom, W.; Kuzin, A.P.; Chiang, Y.; Acton, T.B.; Montelione, G.T.; Hunt, J.F.
    The 2.3-┼ crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase (2003), J. Biol. Chem., 278, 19176-19182.
    View publication on PubMed

Application

Application Comment Organism
pharmacology enzymes of the shikimate pathway has been promoted as a target for the development of antimicrobial agents Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
ydiB gene, expression in Escherichia coli BL21(DE3) Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-dehydroshikimate + NAD(P)H + H+ Escherichia coli YdiB catalyzes the reduction of 3-dehydroshikimate to shikimate as part of the shikimate pathway shikimate + NAD(P)+
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6D5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+ reaction mechanism, in which an aspartate acts as the general acid/base catalyst during the hydride transfer Escherichia coli
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+ reaction mechanism, in which an aspartate acts as the general acid/base catalyst during the hydride transfer Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-dehydroshikimate + NAD(P)H + H+ YdiB catalyzes the reduction of 3-dehydroshikimate to shikimate as part of the shikimate pathway Escherichia coli shikimate + NAD(P)+
-
?
L-quinate + NAD(P)+ detailed strucure of YdiB, specificity for binding NAD+/NADH over NADP+/NADPH Escherichia coli 3-dehydroquinate + NAD(P)H + H+
-
r
shikimate + NAD(P)+ detailed strucure of YdiB, catalytic mechanism, specificity for binding NAD+/NADH over NADP+/NADPH Escherichia coli 3-dehydroshikimate + NAD(P)H + H+
-
r

Subunits

Subunits Comment Organism
homodimer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
More YdiB is a class A NAD(P)+-dependent oxidoreductase Escherichia coli

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
25
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10.6
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+ NAD+ binding site, bound very tightly, NAD+ is bound to the Rossmann domain in an elongated fashion with the nicotinamide ring in the pro-R conformation, specificity for binding NAD+ over NADP+ Escherichia coli
NADH specificity for binding NADH over NADPH Escherichia coli
NADP+ specificity for binding NAD+ over NADP+ Escherichia coli
NADPH specificity for binding NADH over NADPH Escherichia coli