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Literature summary for 1.1.1.282 extracted from

  • Guo, J.; Carrington, Y.; Alber, A.; Ehlting, J.
    Molecular characterization of quinate and shikimate metabolism in Populus trichocarpa (2014), J. Biol. Chem., 289, 23846-23858.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.282

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His6-tagged isozymes in Escherichia coli strain M15 Populus trichocarpa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Populus trichocarpa
0.321
-
 L-quinate with NAD+, isozyme Poptr3, pH 8.5, 22°C Populus trichocarpa
0.334
-
 L-quinate with NAD+, isozyme Poptr2, pH 8.5, 22°C Populus trichocarpa
0.392
-
 shikimate with NAD+, isozyme Poptr3, pH 8.5, 22°C Populus trichocarpa
0.833
-
 shikimate with NAD+, isozyme Poptr2, pH 8.5, 22°C Populus trichocarpa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-quinate + NAD+ Populus trichocarpa
-
 3-dehydroquinate + NADH + H+
-
 ?
additional information Populus trichocarpa the enzyme preferentially uses quinate as a substrate in vitro like a quinate dehydrogenase, EC 1.1.1.24, with only residual shikimate dehydrogenase, SDH, activity, cf. EC 1.1.1.25 ?
-
 ?
shikimate + NAD+ Populus trichocarpa
-
 3-dehydroshikimate + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Populus trichocarpa
-
 trees grown in a field at the University of Victoria
-
Populus trichocarpa Nisqually-1
-
 trees grown in a field at the University of Victoria
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged isozymes from Escherichia coli strain M15 by nickel affinity chromatography Populus trichocarpa

Source Tissue

Source Tissue Comment Organism Textmining
bark Poptr3 and Poptr4 Populus trichocarpa
-
leaf Poptr4 Populus trichocarpa
-
additional information Poptr4 shows a distinct expression pattern with predominant expression in leaves, seedlings, and stomata and some expression in bark and differentiating tissues. Isozyme expression profiles, overview Populus trichocarpa
-
root Poptr2 and Poptr3 are highly expressed in roots and root tips, respectively Populus trichocarpa
-
seedling Poptr4 Populus trichocarpa
-
stem Poptr3 is highly expressed in bark and some vascular tissues Populus trichocarpa
-
stoma Poptr4 Populus trichocarpa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-quinate + NAD+
-
 Populus trichocarpa 3-dehydroquinate + NADH + H+
-
 ?
additional information the enzyme preferentially uses quinate as a substrate in vitro like a quinate dehydrogenase, EC 1.1.1.24, with only residual shikimate dehydrogenase, SDH, activity, cf. EC 1.1.1.25 Populus trichocarpa ?
-
 ?
shikimate + NAD+
-
 Populus trichocarpa 3-dehydroshikimate + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
Poptr2
-
 Populus trichocarpa
Poptr3
-
 Populus trichocarpa
Poptr4
-
 Populus trichocarpa
SDH/QDH
-
 Populus trichocarpa
shikimate/quinate dehydrogenase
-
 Populus trichocarpa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Populus trichocarpa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5 9.5
-
 Populus trichocarpa

Cofactor

Cofactor Comment Organism Structure
additional information no activity with NADP+ Populus trichocarpa
NAD+
-
 Populus trichocarpa

General Information

General Information Comment Organism
evolution members of the same gene family encode enzymes with either shikimate or quinate dehydrogenase activity. Plant SDHs are generally more similar to bacterial SDH/QDH YdiB (25-30% similarity) than to bacterial SDH AroE (21-28%) Populus trichocarpa
metabolism reactions comprising the shikimate/quinate cycle, overview Populus trichocarpa
additional information the enzymes have Gly residues instead of Ser residues in the active sites. The Ser-to-Gly conversion ompared to SDHs may generate extra space in the inferred Poptr isozymes active sites that can accommodate the hydroxyl group at the C1 position of quinate Populus trichocarpa
physiological function quinate and its derivatives are protective secondary metabolites, quinate is an astringent feeding deterrent that can be formed in a single step reaction from 3-dehydroquinate catalyzed by quinate dehydrogenase Populus trichocarpa