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Literature summary for 1.1.1.24 extracted from

  • Tahara, K.; Nishiguchi, M.; Funke, E.; Miyazawa, S.I.; Miyama, T.; Milkowski, C.
    Dehydroquinate dehydratase/shikimate dehydrogenases involved in gallate biosynthesis of the aluminum-tolerant tree species Eucalyptus camaldulensis (2020), Planta, 253, 3 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.24

Cloned(Commentary)

Cloned (Comment) Organism
gene EcDQD/SDH4a, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL, quantitative real-time RT-PCR enzyme expression analysis Eucalyptus camaldulensis
gene EcDQD/SDH4b, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL, quantitative real-time RT-PCR enzyme expression analysis Eucalyptus camaldulensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0537
-
 NAD+ pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation Eucalyptus camaldulensis
0.102
-
 NADH pH 7.5, 30°C, EcDQD/SDH4a, quinate formation Eucalyptus camaldulensis
0.164
-
 L-quinate pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation Eucalyptus camaldulensis
1.4
-
 3-dehydroquinate pH 7.5, 30°C, EcDQD/SDH4a, quinate formation Eucalyptus camaldulensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-quinate + NAD+ Eucalyptus camaldulensis
-
 3-dehydroquinate + NADH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Eucalyptus camaldulensis A0A5H2WXM2
-
-
Eucalyptus camaldulensis A0A5H2X0F8
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by glutathione affinity chromatography and tag cleavage through thrombin Eucalyptus camaldulensis

Source Tissue

Source Tissue Comment Organism Textmining
leaf highest expression level Eucalyptus camaldulensis
-
additional information comparison of EcDQD/SDH, UGT84A25a/b, and UGT84A26a/b expression patterns in Eucalyptus camaldulensis, relative EcDQD/SDH mRNA levels in the leaves, stems, and roots are plotted against the relative UGT84A25a/b and UGT84A26a/b mRNA levels in the same samples, and determination of concentrations of the metabolites in the different tissues, overview Eucalyptus camaldulensis
-
root
-
 Eucalyptus camaldulensis
-
stem lowest expression level Eucalyptus camaldulensis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-quinate + NAD+
-
 Eucalyptus camaldulensis 3-dehydroquinate + NADH + H+
-
 r
L-quinate + NADP+ low activity Eucalyptus camaldulensis 3-dehydroquinate + NADPH + H+
-
 r
additional information product analysis by GC-MS Eucalyptus camaldulensis ?
-
-

Synonyms

Synonyms Comment Organism
QDH
-
 Eucalyptus camaldulensis
quinate dehydrogenase
-
 Eucalyptus camaldulensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Eucalyptus camaldulensis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
127
-
 L-quinate pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation Eucalyptus camaldulensis
139
-
 NAD+ pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation Eucalyptus camaldulensis
281
-
 3-dehydroquinate pH 7.5, 30°C, EcDQD/SDH4a, quinate formation Eucalyptus camaldulensis
298
-
 NADH pH 7.5, 30°C, EcDQD/SDH4a, quinate formation Eucalyptus camaldulensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 quinate formation activity Eucalyptus camaldulensis
9
-
 quinate oxidation Eucalyptus camaldulensis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Eucalyptus camaldulensis
NADH
-
 Eucalyptus camaldulensis

General Information

General Information Comment Organism
evolution plant SDH enzymes are fused to dehydroquinate dehydratases (DQDs, EC 4.2.1.10) to form bifunctional DQD/SDH enzymes. The DQD activity is observed for EcDQD/SDH1, 2, and 3, but not for EcDQD/SDH4a. Among the active enzymes, EcDQD/SDH1 exhibits the highest DQD activity, followed by EcDQD/SDH2 (about 50% of the EcDQD/SDH1 activity) and EcDQD/SDH3 (about 5% of the EcDQD/SDH1 activity). For shikimate formation from 3-DHS as well as shikimate oxidation to 3-DHS, measurable catalytic activities are detected for EcDQD/SDH1-3, but the activities of EcDQD/SDH2 and 3 are less than 20% of those of EcDQD/SDH1. Regarding the cofactor, EcDQD/SDH1-3 have a clear preference for NADPH/NADP+ over NADH/ NAD+. In contrast, EcDQD/SDH4a and b lack shikimate formation activity. For the reverse reaction, the conversion of shikimate to 3-DHS, EcDQD/SDH4a and b display low enzymatic activity with a preference for NAD+ as the cofactor. Both EcDQD/SDH2 and 3 exhibit relatively high gallate formation activity, in contrast to the low activity of EcDQD/SDH1. The preferred cofactor in this reaction is NADP+. The reversible quinate formation from 3-DHQ is catalyzed only by EcDQD/SDH4a/b, with NADH/NAD+ as the preferred cofactor. The reaction specificity of EcDQD/SDH4a confirms the sequence-based prediction that EcDQD/SDH4a is a functional QDH enzyme. This enzyme should be renamed EcQDHa and its closest relative, EcDQD/SDH4b, should be renamed EcQDHb. The EcDQD/SDH4a and EcDQD/SDH4b genes may represent allelic variants encoding enzymes with 99.2% amino acid identity Eucalyptus camaldulensis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
200.7
-
 3-dehydroquinate pH 7.5, 30°C, EcDQD/SDH4a, quinate formation Eucalyptus camaldulensis
774.4
-
 L-quinate pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation Eucalyptus camaldulensis
2588.5
-
 NAD+ pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation Eucalyptus camaldulensis
2921.6
-
 NADH pH 7.5, 30°C, EcDQD/SDH4a, quinate formation Eucalyptus camaldulensis