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Literature summary 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-Å 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

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

Cloned(Commentary)

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.282 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

EC Number Organism UniProt Comment Textmining
1.1.1.282 Escherichia coli P0A6D5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.282
-
 Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.282 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
a
1.1.1.282 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.282 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)+
-
 ?
1.1.1.282 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
1.1.1.282 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

EC Number Subunits Comment Organism
1.1.1.282 homodimer
-
 Escherichia coli

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.282 25
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.282 10.6
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.282 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
1.1.1.282 NADH specificity for binding NADH over NADPH Escherichia coli
1.1.1.282 NADP+ specificity for binding NAD+ over NADP+ Escherichia coli
1.1.1.282 NADPH specificity for binding NADH over NADPH Escherichia coli