EC Number   |
General Information |
Reference |
|---|
    1.1.1.25 | evolution |
a three-dimensional structural model of TgSDH predicts a high level of conservation in the core structure of the enzyme |
740978 |
| 1.1.1.25 | evolution |
Escherichia coli constitutively expresses two shikimate dehydrogenase paralogues, AroE and the NAD+ -dependent enzyme quinate/shikimate dehydrogenase (YdiB), sharing 25% sequence identity. While AroE is NADP+-dependent, YdiB uses NADP+ or NAD+. Contrary to AroE, YdiB displays a clear activity on quinate, with either NADP+ or NAD+ as a cofactor in addition to shikimate |
-, 761708 |
| 1.1.1.25 | evolution |
four CsDQD/SDH isozyme proteins are cloned from Camellia sinensis. Three CsDQD/SDH isozymes show 3-dehydroshikimate (3-DHS) reduction and shikimate (SA) oxidation functions with individual differences between the catalytic efficiency of 3-DHS reduction and SA oxidation. Isozyme CsDQD/SDHa has higher catalytic efficiency for 3-DHS reduction than for SA oxidation, isozyme CsDQD/SDHd shows the opposite tendency, and isozyme CsDQD/SDHc has almost equal catalytic efficiency for 3-DHS reduction and SA oxidation. In vitro, Gallic acid (GA) is mainly generated from 3-DHS through nonenzymatic conversion. Isozymes CsDQD/SDHc and CsDQD/ SDHd genes are involved in GA synthesis |
761171 |
| 1.1.1.25 | evolution |
members of the same gene family encode enzymes with either shikimate or quinate dehydrogenase activity. The poplar genome encodes five DQD/SDH-like genes (Poptr1 to Poptr5), which have diverged into two distinct groups based on sequence analysis and protein structure prediction. In vitro biochemical assays prove that Poptr1 and -5 are true DQD/SDHs, whereas Poptr2 and -3 instead have QDH activity with only residual DQD/SDH activity, cf. EC 1.1.1.282 |
-, 740724 |
| 1.1.1.25 | evolution |
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH1 belongs to group I, and clusters with four characterized DQD/SDHs: AtSDH, Poptr1, JrSDH, and NtSDH1, group members share about 75% sequence identity |
740821 |
| 1.1.1.25 | evolution |
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH2 belongs to group II, and clusters with Poptr2 and Poptr3, two characterized DQD/SDHs, and NtSDH2, group members share about 71% sequence identity |
740821 |
| 1.1.1.25 | evolution |
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH3 belongs to group III, group members share about 85% sequence identity, four of them from different species (VvSDH3, CasSDH2, FvSDH1, and EgSDH3) accumulate gallic acid-based tannins |
740821 |
| 1.1.1.25 | evolution |
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH4 belongs to group IV, and clusters with with Poptr5, a DQD/SDH characterized in Populus trichocarpa, group members share about 77% sequence identity |
740821 |
| 1.1.1.25 | evolution |
plant QDHs arose directly from bifunctional dehydroquinate dehydratase-shikimate dehydrogenases (DHQD-SDHs) through different convergent evolutionary events, detailed phylogenetic analysis, overview. Eudicot and conifer QDHs arose early in vascular plant evolution whereas Brassicaceae QDHs emerged late, process of recurrent evolution of QDH. This family of proteins independently evolved NAD+ and NADP+ specificity in eudicots. The acquisition of QDH activity by these proteins is accompanied by the inactivation or functional evolution of the DHQD domain, as verified by enzyme activity assays and as reflected in the loss of key DHQD active site residues |
762145 |
| 1.1.1.25 | 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+ |
762187 |
