Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.282 extracted from

  • Garcia, S.; Flores, N.; De Anda, R.; Hernandez, G.; Gosset, G.; Bolivar, F.; Escalante, A.
    The role of the ydiB gene, which encodes quinate/shikimate dehydrogenase, in the production of quinic, dehydroshikimic and shikimic acids in a PTS- strain of Escherichia coli (2016), J. Mol. Microbiol. Biotechnol., 27, 11-21.
    View publication on PubMed
Search for more literature for 1.1.1.282

Application

Application Comment Organism
synthesis enzyme YdiB displays a clear activity on quinate, with either NADP+ or NAD+ as a cofactor in addition to shikimate, making this enzyme an important candidate for quinate production. Production of shikimate, quinate, 3-dehydroshikimate and other aromatic derivatives in strain PB12.SA22 during batch culture fermentation Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
gene ydiB, recombinant overexpression in Escherichia coli strain PB12 causing a 500% increase in the molar yield of quinate and results in a 152% increase in quinate (mol/mol) relative to shikimate, with a sharp decrease in shikimate production. Transcriptomic analysis of PB12.SA22 and ydiB derivative strains Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information construction of an enzyme ydiB- knockout mutant JM101 strain. Fermentation processes for the production of shikimate in overproducing strains of Escherichia coli result in the simultaneous synthesis of quinic acid and 3-dehydroshikimic acid. The production of high amounts of these byproducts significantly reduces the yield of shikimate, and more importantly, the presence of quinate impairs the efficiency of shikimate extraction from supernatant cultures, reducing its purity and increasing downstream processing costs. The inactivation of the ydiB gene increases the molar proportion of shikimate and 3-dehydroshikimate with respect to quinate, showing a molar ratio of 0.81/0.05/0.14 (mol/mol/mol) of shikimate/quinate/3-dehydroshikimate. In this derivative strain, quinate production is 6.17% relative to shikimate (mol/mol), indicating that the inactivation of ydiB is a suitable strategy to reduce quinate production below 10% (mol/mol) relative to ahkimate in culture fermentations for shikimate production Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-quinate + NAD+ Escherichia coli
-
 3-dehydroquinate + NADH + H+
-
 ?
L-quinate + NAD+ Escherichia coli JM101
-
 3-dehydroquinate + NADH + H+
-
 ?
additional information Escherichia coli the synthesis of quinate results from the reduction of 3-dehydroquinate by YdiB before its conversion to 3-dehydroshikimate. In Escherichia coli strain W3110.shik, YdiB, rather than AroE, catalyzes the oxidation of shikimate to 3-dehydroshikimate and the reduction of 3-dehydroquinate to quinate ?
-
 ?
additional information Escherichia coli JM101 the synthesis of quinate results from the reduction of 3-dehydroquinate by YdiB before its conversion to 3-dehydroshikimate. In Escherichia coli strain W3110.shik, YdiB, rather than AroE, catalyzes the oxidation of shikimate to 3-dehydroshikimate and the reduction of 3-dehydroquinate to quinate ?
-
 ?
shikimate + NAD+ Escherichia coli
-
 3-dehydroshikimate + NADH + H+
-
 ?
shikimate + NAD+ Escherichia coli JM101
-
 3-dehydroshikimate + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli JM101
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-quinate + NAD+
-
 Escherichia coli 3-dehydroquinate + NADH + H+
-
 ?
L-quinate + NAD+
-
 Escherichia coli JM101 3-dehydroquinate + NADH + H+
-
 ?
additional information the synthesis of quinate results from the reduction of 3-dehydroquinate by YdiB before its conversion to 3-dehydroshikimate. In Escherichia coli strain W3110.shik, YdiB, rather than AroE, catalyzes the oxidation of shikimate to 3-dehydroshikimate and the reduction of 3-dehydroquinate to quinate Escherichia coli ?
-
 ?
additional information the synthesis of quinate results from the reduction of 3-dehydroquinate by YdiB before its conversion to 3-dehydroshikimate. In Escherichia coli strain W3110.shik, YdiB, rather than AroE, catalyzes the oxidation of shikimate to 3-dehydroshikimate and the reduction of 3-dehydroquinate to quinate Escherichia coli JM101 ?
-
 ?
shikimate + NAD+
-
 Escherichia coli 3-dehydroshikimate + NADH + H+
-
 ?
shikimate + NAD+
-
 Escherichia coli JM101 3-dehydroshikimate + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
quinate/shikimate dehydrogenase
-
 Escherichia coli
YdiB
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Escherichia coli
NADH
-
 Escherichia coli