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53.9
-
30°C, pH 10.0-10.5
0.0046
-
pH 8.8, presence of 2 mM NADP+
0.027
-
pH 9.0, 30°C, recombinant isozyme VvSDH3
0.03
-
pH 9.0, 25°C, with NADP+
0.0326
-
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
0.0326
-
pH 9.0, temperature not specified in the publication
0.03746
-
pH not specified in the publication, 25°C
0.0375
-
pH not specified in the publication, 25°C, with NADP+
0.0425
-
with NADP+, pH 9.0, 25°C
0.05
-
pH 7.0, 25°C, recombinant AroE
0.0502
-
pH 7.0, 25°C, with NADP+
0.0527
-
pH 8.8, 25°C, with NADP+
0.0527
-
pH 8.8, temperature not specified in the publication
0.065
-
with NADP+, pH 9.0, 20°C
0.07
-
pH 9.0, 30°C, recombinant isozyme VvSDH1
0.073
-
pH 7.0, 25°C, with NADP+
0.0786
-
in the presence of 2 mM NAD+
0.0786
-
pH 8.8, presence of 2 mM NAD+
0.101
-
pH and temperature not specified in the publication
0.105
-
in the presence of 2 mM NADP+
0.105
-
pH 8.8, presence of 2 mM NADP+
0.12
-
pH and temperature not specified in the publication
0.13
-
pH 9.0, 25°C, recombinant wild-type enzyme
0.131
-
pH 7.5, 22°C, mutant K385N/D423N
0.14
-
with NADP+, pH 9.0, 30°C
0.1468
-
pH 9.0, 30°C, recombinant isozyme VvSDH4
0.148
-
pH 8.0, 60°C, recombinant enzyme
0.148
-
with NADP+, pH 8.0, 25°C
0.155
-
pH 7.0, 30°C, recombinant isozyme VvSDH1
0.17
-
with NADP+, pH 7.3, 87°C
0.178
-
pH 8.8, 25°C, with NADP+
0.2
-
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADP+
0.218
-
pH and temperature not specified in the publication
0.223
-
pH 8.5, 22°C, with NADP+, isozyme Poptr1
0.223
-
with NADP+, pH 8.5, 22°C, recombinant His-tagged Poptr1
0.239
-
pH and temperature not specified in the publication
0.263
-
pH 7.5, 22°C, mutant K385A
0.273
-
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADP+
0.279
-
pH and temperature not specified in the publication
0.311
-
with NADP+, pH 7.0, 25°C
0.321
-
with NADP+, pH 8.5, 22°C, recombinant His-tagged Poptr1
0.346
-
pH 8.5, 22°C, with NADP+, isozyme Poptr5
0.346
-
with NAD+, pH 8.5, 22°C, recombinant His-tagged Poptr1
0.351
-
pH 8.8, presence of 2 mM NAD+
0.422
-
pH 7.0, 30°C, recombinant isozyme VvSDH3
0.427
-
with NAD+, pH 8.5, 22°C, recombinant His-tagged Poptr1
0.459
-
mutant T381S, 22°C
0.47
-
pH 7.5, 22°C, mutant K385N
0.548
-
pH and temperature not specified in the publication, mutant S338G
0.555
-
pH 7.5, 22°C, mutant D423N
0.556
-
mutant T381A, 22°C
0.604
-
pH and temperature not specified in the publication, wild-type enzyme
0.611
-
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with NADP+
0.626
-
mutant H335A, 22°C
0.685
-
pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant
0.685
-
pH 8.8, 22°C, with NADP+
0.882
-
pH and temperature not specified in the publication, mutant S338G/T381G
1.022
-
mutant T407A, 22°C
1.03
-
pH 7.5, 22°C, mutant Y550A
1.06
-
pH 7.5, 22°C, mutant Y550F
1.09
-
mutant T422S, 22°C
1.539
-
pH and temperature not specified in the publication, mutant T381S
1.613
-
pH and temperature not specified in the publication, mutant T381G
2.05
-
pH 9.0, 30°C, EcDQD/SDH2, shikimate oxidation
2.05
-
pH 9.0, temperature not specified in the publication
2.512
-
pH and temperature not specified in the publication, mutant T381A
3.64
-
pH 9.0, 30°C, EcDQD/SDH3, shikimate oxidation
3.64
-
pH 9.0, temperature not specified in the publication
4.2
-
pH 8.8, presence of 2 mM NAD+
4.466
-
mutant Q582L, 22°C
6.2
-
pH 7.5, 22°C, mutant S338A
7.12
-
mutant N406A, 22°C
8.74
-
pH 7.5, 22°C, mutant S336A
0.0017
-
mutant S67A, 20°C, pH 9.0
0.0028
-
mutant Q262A, 20°C, pH 9.0
0.0029
-
wild type enzyme, 20°C, pH 9.0
0.0032
-
mutant S22A, 20°C, pH 9.0
0.0032
-
mutant Y39F, 20°C, pH 9.0
0.02
-
pH 9, 20°C, cosubstrate NAD+
0.12
-
pH 9, 20°C, cosubstrate NADP+
0.187
-
with NADP+, pH 7.0, 30°C
0.199
-
mutant T106A, 20°C, pH 9.0
0.26
-
with NAD+, pH 8.6, 30°C
0.392
-
with NAD+, isozyme Poptr3, pH 8.5, 22°C
0.513
-
mutant K71A, 20°C, pH 9.0
0.7
0.8
pH 10, 20°C, cosubstrate NADP+, both forms of quinate (shikimate) dehydrogenase
0.82
-
pH and temperature not specified in the publication, enzyme PintaQDH with NADP+
0.833
-
with NAD+, isozyme Poptr2, pH 8.5, 22°C
1.299
-
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
2.18
-
pH 8.8, 25°C, with NADP+
3.38
-
pH 8.8, 25°C, with NAD+
4.2
-
in the presence of 2 mM NAD+
5.25
-
pH 10, (-)-enantiomer, cosubstrate NAD+
10.16
-
pH 7.5, 30°C, with NAD+
40.07
-
mutant D107A, 20°C, pH 9.0
55.88
-
pH 10.0-10.5, 30°C, with NAD+
0.26
-
pH 6.5, 25°C, with potassium ferricyanide or a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol as electron acceptor
0.0009
-
pH 8.0, 37°C, recombinant GST-tagged enzyme, with 4-coumaroyl-CoA
0.0631
-
mutant Y40A, pH 6.5, temperature not specified in the publication
0.153
-
wild-type, pH 6.5, temperature not specified in the publication
0.1558
-
pH 7.5, 37°C, with feruloyl-CoA
0.332
-
pH 7.0, 30°C, with 4-coumaroyl-CoA
0.59
-
with 4-coumaroyl-CoA
0.678
-
mutant S38A, pH 6.5, temperature not specified in the publication
0.9
-
with 4-coumaroyl-CoA, pH 8.0, 37°C
2.235
-
pH 7.0, 30°C, with cinnamoyl-CoA
2.473
-
cosubstrate caffeoyl-CoA, pH 7.0, 25°C
2.69
-
cosubstrate caffeoyl-CoA, pH 7.0, 25°C
6.495
-
pH 7.0, 30°C, with caffeoyl-CoA
22.38
-
pH 7.0, 30°C, with feroyl-CoA
26.13
-
pH 7.0, 30°C, with sinapoyl-CoA
0.75
-
pH 6.6, 30°C, cosubstrate: p-coumaroyl-CoA
2.473
-
cosubstrate caffeoyl-CoA, pH 7.0, 25°C
2.69
-
cosubstrate caffeoyl-CoA, pH 7.0, 25°C
5.579
-
cosubstrate 4-coumaroyl-CoA, pH not specified in the publication, 30°C
0.000153
-
at pH 7.6 and 25°C
0.039
-
at pH 7.7 and 25°C
0.039
-
enzyme mutant E114A, pH 7.5, 25°C
0.06
-
in 100 mM Tris-HClKOH buffer, pH 7.5, 50 mM KCl, 5 mM MgCl2, 1.6 mM shikimic acid, 2.5 mM ATP, 1 mM phosphoenolpyruvate, 0.1 mM NADH, 2.5 units of pyruvate kinase/ml, and 2.7 units of lactate dehydrogenase/ml, at 25°C
0.06
-
wild-type enzyme, pH 7.5, 25°C
0.075
-
pH 7.0, 25°C, mutant enzyme C13S
0.135
-
enzyme mutant M10A, pH 7.5, 25°C
0.147
-
at pH 7.5 and 25°C
0.2
-
isoenzyme SK2, at 5 mM ATP
0.28
-
pH 7.0, 25°C, mutant enzyme C162S
0.291
-
enzyme mutant F48Y, pH 7.5, 25°C
0.362
-
at pH 7.5 and 25°C
0.3994
-
at pH 7.6 and 25°C
0.544
-
at pH 7.7 and 25°C
0.65
-
at pH 7.6 and 25°C
5
-
above, isoenzyme SK1, at 5 mM
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Partial purification and properties of p-hydroxycinnamoyl-CoA: shikimate-p-hydroxy-cinnamoyl transferase from higher plants
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Partial purification and characterization of hydroxycinnamoyl CoA:transferase from apple and date fruits
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Purification, cloning, and properties of an acyltransferase controlling shikimate and quinate ester intermediates in phenylpropanoid metabolism
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The enzymic conversion of hydroxycinnamic acids to p-coumarylquinic and chlorogenic acids in tomato fruits
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22
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Shikimate kinase isoenzymes in Salmonella typhimurium
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Alicyclic acid metabolism in plants. 12. Partial purification and some properties of shikimate kinase from Phaseolus mungo seedlings
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67
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A thermostable shikimate 5-dehydrogenase from the archaeon Archaeoglobus fulgidus
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238
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The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode
2003
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185
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Site-directed mutagenesis of the active site region in the quinate/shikimate 5-dehydrogenase YdiB of Escherichia coli
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7162-7169
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Broad-specificity quinate (shikimate) dehydrogenase from Pinus taeda needles
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38
923-928
Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution
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Padyana, A.K.; Burley, S.K.
Structure
11
1005-1013
Bacillus subtilis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase revisited: resolution of two long-standing enigmas
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390
583-590
Engineering plants with increased levels of the antioxidant chlorogenic acid
2004
Niggeweg, R.; Michael, A.J.; Martin, C.
Nat. Biotechnol.
22
746-754
Crystallographic studies of shikimate binding and induced conformational changes in Mycobacterium tuberculosis shikimate kinase
2004
Dhaliwal, B.; Nichols, C.E.; Ren, J.; Lockyer, M.; Charles, I.; Hawkins, A.R.; Stammers, D.K.
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574
49-54
Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase
2005
Cheng, W.C.; Chang, Y.N.; Wang, W.C.
J. Bacteriol.
187
8156-8163
Structure of Arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase and implications for metabolic channeling in the shikimate pathway
2006
Singh, S.A.; Christendat, D.
Biochemistry
45
10406
Purification and properties of NADP-dependent shikimate dehydrogenase from Gluconobacter oxydans IFO 3244 and its application to enzymatic shikimate production
2006
Adachi, O.; Ano, Y.; Toyama, H.; Matsushita, K.
Biosci. Biotechnol. Biochem.
70
2786-2789
Biochemical characterization and inhibitor discovery of shikimate dehydrogenase from Helicobacter pylori
2006
Han, C.; Wang, L.; Yu, K.; Chen, L.; Hu, L.; Chen, K.; Jiang, H.; Shen, X.
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273
4682-4692
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