Literature summary for 1.1.1.25 extracted from

Gritsunov, A.; Peek, J.; Diaz Caballero, J.; Guttman, D.; Christendat, D.
Structural and biochemical approaches uncover multiple evolutionary trajectories of plant quinate dehydrogenases (2018), Plant J., 95, 812-822 .

Search for more literature for 1.1.1.25

Cloned(Commentary)

Cloned (Comment)	Organism
expression analysis, phylogenetic analysis	Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment)	Organism
analysis of three-dimensional crystal structure of enzyme DHQD-SDH with shikimate bound in the SDH active site, PDB ID 2GPT. Crystallization of T381G mutant bound with quinate	Arabidopsis thaliana

Protein Variants

Protein Variants	Comment	Organism
additional information	absence of the T381 side chain creates sufficient space in the active site to accommodate the quinate C1-hydroxyl. The K385 and D423 catalytic dyad which interacts with C4-OH and participates in proton transfer during the reduction/oxidation of NADP+/NADPH is retained in the T381G mutant	Arabidopsis thaliana
S338G	site-directed mutagenesis, the mutant is not active with quinate like the wild-type	Arabidopsis thaliana
S338G/T381G	site-directed mutagenesis, the double mutant does not show improved enzymatic activity with quinate compared with the T381G mutant	Arabidopsis thaliana
T381A	site-directed mutagenesis, the mutant accepts quinate as a substrate but is much less efficient than the T381G variant	Arabidopsis thaliana
T381G	site-directed mutagenesis, mutant shows increased activity with quinate compared to wild-type, it catalyzes the oxidation of quinate with a turnover rate of 8.8/s and a KM of 3.33 mM	Arabidopsis thaliana
T381S	site-directed mutagenesis, the mutant accepts quinate as a substrate but is much less efficient than the T381G variant	Arabidopsis thaliana

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Michaelis-Menten kinetics	Arabidopsis thaliana
0.548	-	shikimate	pH and temperature not specified in the publication, mutant S338G	Arabidopsis thaliana
0.604	-	shikimate	pH and temperature not specified in the publication, wild-type enzyme	Arabidopsis thaliana
0.882	-	shikimate	pH and temperature not specified in the publication, mutant S338G/T381G	Arabidopsis thaliana
1.539	-	shikimate	pH and temperature not specified in the publication, mutant T381S	Arabidopsis thaliana
1.613	-	shikimate	pH and temperature not specified in the publication, mutant T381G	Arabidopsis thaliana
2.512	-	shikimate	pH and temperature not specified in the publication, mutant T381A	Arabidopsis thaliana
3.33	-	L-quinate	pH and temperature not specified in the publication, mutant T381G	Arabidopsis thaliana
4.075	-	L-quinate	pH and temperature not specified in the publication, mutant S338G/T381G	Arabidopsis thaliana
4.485	-	L-quinate	pH and temperature not specified in the publication, mutant T381S	Arabidopsis thaliana
5.135	-	L-quinate	pH and temperature not specified in the publication, mutant T381A	Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
shikimate + NADP+	Arabidopsis thaliana	-	3-dehydroshikimate + NADPH + H+	-	r

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q9SQT8	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-quinate + NADP+	activity of T381 enzyme mutants, not of wild-type enzyme, see also EC 1.1.1.282	Arabidopsis thaliana	3-dehydroquinate + NADPH + H+	-	r
shikimate + NADP+	-	Arabidopsis thaliana	3-dehydroshikimate + NADPH + H+	-	r

Synonyms

Synonyms	Comment	Organism
bifunctional DHQD-SDH/QDH	-	Arabidopsis thaliana
DHQD-SDH	-	Arabidopsis thaliana
EMB3004	-	Arabidopsis thaliana
More	cf. EC 4.2.1.10	Arabidopsis thaliana
QDH/SDH	-	Arabidopsis thaliana

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.062	-	L-quinate	pH and temperature not specified in the publication, mutant T381S	Arabidopsis thaliana
0.113	-	L-quinate	pH and temperature not specified in the publication, mutant T381A	Arabidopsis thaliana
6.7	-	L-quinate	pH and temperature not specified in the publication, mutant S338G/T381G	Arabidopsis thaliana
8.8	-	L-quinate	pH and temperature not specified in the publication, mutant T381G	Arabidopsis thaliana
11.8	-	shikimate	pH and temperature not specified in the publication, mutant T381A	Arabidopsis thaliana
22	-	shikimate	pH and temperature not specified in the publication, mutant S338G/T381G	Arabidopsis thaliana
24	-	shikimate	pH and temperature not specified in the publication, mutant T381G	Arabidopsis thaliana
172	-	shikimate	pH and temperature not specified in the publication, mutant T381S	Arabidopsis thaliana
427	-	shikimate	pH and temperature not specified in the publication, mutant S338G	Arabidopsis thaliana
516	-	shikimate	pH and temperature not specified in the publication, wild-type enzyme	Arabidopsis thaliana

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	-	Arabidopsis thaliana
NADPH	-	Arabidopsis thaliana

General Information

General Information	Comment	Organism
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	Arabidopsis thaliana
additional information	only four amino acid residues likely to contribute to specificity for one substrate instead of the other, namely S336, S338, T381 and Y550, all of which would be in the direct vicinity of the quinate C1-hydroxyl. Amino acid S336 has previously been shown by mutational analysis to be critical for shikimate binding. The size of the amino acid side chain at position 381 is a key determinant of substrate specificity	Arabidopsis thaliana

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
0.014	-	L-quinate	pH and temperature not specified in the publication, mutant T381S	Arabidopsis thaliana
0.022	-	L-quinate	pH and temperature not specified in the publication, mutant T381A	Arabidopsis thaliana
1.64	-	L-quinate	pH and temperature not specified in the publication, mutant S338G/T381G	Arabidopsis thaliana
2.64	-	L-quinate	pH and temperature not specified in the publication, mutant T381G	Arabidopsis thaliana
4.7	-	shikimate	pH and temperature not specified in the publication, mutant T381A	Arabidopsis thaliana
14.9	-	shikimate	pH and temperature not specified in the publication, mutant T381G	Arabidopsis thaliana
24.9	-	shikimate	pH and temperature not specified in the publication, mutant S338G/T381G	Arabidopsis thaliana
111.8	-	shikimate	pH and temperature not specified in the publication, mutant T381S	Arabidopsis thaliana
779.2	-	shikimate	pH and temperature not specified in the publication, mutant S338G	Arabidopsis thaliana
854.3	-	shikimate	pH and temperature not specified in the publication, wild-type enzyme	Arabidopsis thaliana

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Release 2023.1 (January 2023)