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Literature summary for 1.1.1.282 extracted from

  • Ossipov, V.; Bonner, C.; Ossipova, S.; Jensen, R.
    Broad-specificity quinate (shikimate) dehydrogenase from Pinus taeda needles (2000), Plant Physiol. Biochem., 38, 923-928.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
L-quinate competitive inhibitor with respect to shikimate Pinus taeda
shikimate competitive inhibitor with respect to L-quinate Pinus taeda

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.001
-
NADP+ pH 10, 20┬░C, cosubstrate shikimate, both forms of quinate (shikimate) dehydrogenase Pinus taeda
0.005 0.012 NADPH pH 10, 20┬░C, cosubstrate dehydroquinate, both forms of quinate (shikimate) dehydrogenase Pinus taeda
0.007
-
NADP+ pH 10, 20┬░C, cosubstrate L-quinate, both forms of quinate (shikimate) dehydrogenase Pinus taeda
0.7 0.8 shikimate pH 10, 20┬░C, cosubstrate NADP+, both forms of quinate (shikimate) dehydrogenase Pinus taeda
1
-
dehydroquinate pH 10, 20┬░C, cosubstrate NADPH, form P1 of quinate (shikimate) dehydrogenase Pinus taeda
3.4 3.6 L-quinate pH 10, 20┬░C, cosubstrate NADP+, both forms of quinate (shikimate) dehydrogenase Pinus taeda
5.3
-
dehydroquinate pH 10, 20┬░C, cosubstrate NADPH, form P2 of quinate (shikimate) dehydrogenase Pinus taeda

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
two forms of the bifunctional quinate (shikimate) dehydrogenase, gel filtration Pinus taeda
53000
-
two forms of the bifunctional quinate (shikimate) dehydrogenase, gel filtration Pinus taeda

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-dehydroquinate + NADPH + H+ Pinus taeda may be responsible for the synthesis of quinic acid from the intermediate compound of the shikimate pathway, dehydroquinic acid L-quinate + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Pinus taeda
-
20 years old
-

Purification (Commentary)

Purification (Comment) Organism
3000fold, two forms of the bifunctional quinate (shikimate) dehydrogenase: P1 and P2 Pinus taeda

Source Tissue

Source Tissue Comment Organism Textmining
needle from current-year shoots of 20 years old trees, the youngest basal parts of needles Pinus taeda
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/min/mg] Comment Organism
additional information
-
-
Pinus taeda

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-dehydroquinate + NADPH + H+ may be responsible for the synthesis of quinic acid from the intermediate compound of the shikimate pathway, dehydroquinic acid Pinus taeda L-quinate + NADP+
-
?
L-quinate + NADP+ both quinate and shikimate dehydrogenase activities are catalyzed by a single broad-specificity quinate (shikimate) dehydrogenase with a common substrate binding site, the velocity is 2fold greater with quinate than with shikimate Pinus taeda 3-dehydroquinate + NADPH + H+
-
r
shikimate + NADP+ both quinate and shikimate dehydrogenase activities are catalyzed by a single broad-specificity quinate (shikimate) dehydrogenase with a common substrate binding site, the velocity is 2fold lower with shikimate than with quinate Pinus taeda 3-dehydroshikimate + NADPH + H+
-
r

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
20
-
assay at Pinus taeda

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.7
-
back reaction, dehydroquinate or dehydroshikimate and NADPH as substrates Pinus taeda
10.3
-
quinate or shikimate and NADP+ as substrates Pinus taeda

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Pinus taeda
NADPH
-
Pinus taeda