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1.1.1.25: shikimate dehydrogenase (NADP+)

This is an abbreviated version!
For detailed information about shikimate dehydrogenase (NADP+), go to the full flat file.

Word Map on EC 1.1.1.25

Reaction

shikimate
+
NADP+
=
3-dehydroshikimate
+
NADPH
+
H+

Synonyms

3-dehydroquinate dehydratase/shikimate dehydrogenase, 5-dehydroshikimate reductase, 5-dehydroshikimic reductase, ael1, Af2327, AroE, bifunctional dehydroquinate dehydratase-shikimate dehydrogenase, bifunctional DHQD-SDH/QDH, cgR_0495, cgR_1677, ChlreSDH, CsDQD/SDH, dehydroquinate dehydratase-shikimate dehydrogenase, dehydroquinate dehydratase/shikimate dehydrogenase, dehydroshikimic reductase, DHD/SHD, DHQ-SDH, DHQD-SDH, DHS reductase, DQD/SDH, EcDQD, EcDQD/SDH, EcDQD/SDH1, EcDQD/SDH2, EcDQD/SDH3, EcoSDH, EcSDH, EMB3004, HI0607, HpSDH, More, MtbSD, MtbSDH, NAD+-dependent enzyme quinate/shikimate dehydrogenase, NADP-dependent shikimate dehydrogenase, NADP-shikimate dehydrogenase, PgSDH, PhypaSDH, PintaSDH, Poptr1, Poptr5, PoptrSDH1, QDH/SDH, qsuD, quinate/shikimate dehydrogenase, RhobaSDH, rifI, SaSDH, SD, SDH, sdhL, SelmoSDH, ShDH, shikimate 5-dehydrogenase, shikimate dehydrogenase, shikimate oxidoreductase, shikimate:NADP oxidoreductase, shikimate:NADP+ 5-oxidoreductase, shikimate:NADP+ oxidoreductase, SKDH, TgSDH, tm0346, VvSDH1, VvSDH2, VvSDH3, VvSDH4, YdiB

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.25 shikimate dehydrogenase (NADP+)

Engineering

Engineering on EC 1.1.1.25 - shikimate dehydrogenase (NADP+)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D423A
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, inactive mutant
D423N
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
H335A
-
site-directed mutagenesis, tenfold decrease in kcat value
K385A
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
K385N
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
K385N/D423N
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
N406A
-
site-directed mutagenesis, very strong decrease in kcat value
Q578L
-
site-directed mutagenesis, sixtyfold decrease in kcat value
Q582L
-
site-directed mutagenesis, very strong decrease in kcat value
S336A
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
S338A
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
S338G
site-directed mutagenesis, the mutant is not active with quinate like the wild-type
S338G/T381G
site-directed mutagenesis, the double mutant does not show improved enzymatic activity with quinate compared with the T381G mutant
T381A
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
T381S
T407A
-
site-directed mutagenesis, 6.5fold decrease in kcat value, increase in Km-value
T422S
-
site-directed mutagenesis, tenfold decrease in kcat value
Y550A
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
Y550F
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
G338S/G381T/D483N/L484R/D485T
site-directed mutagenesis, mutant MTCsDQD/SDHb has a similar reduction activity of 3-DHS and had six times higher oxidation activity of SA than wild-type isozyme CsDQD/SDHb, suggesting that the mutation of residues Ser338 and NRT to Gly and DI/LD in the SDH unit is the reason for the low activity of CsDQD/SDHb, respectively
A243G
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
D195E
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
N149D
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
N149D/V152F
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
S131A
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
S131A/L135A
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
S131A/L135A/N149D/V152F
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
S131A/N149D/V152F
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
D103X
-
site-directed mutagenesis of paralogue HI0607, inactive mutant
K67H
-
site-directed mutagenesis of paralogue HI0607, inactive mutant
K69A
-
site-directed mutagenesis, the mutant shows significantly reduced the catalytic efficiency compared to wild-type enzyme
Q237A
-
site-directed mutagenesis
Q237K
-
site-directed mutagenesis
Q237N
-
site-directed mutagenesis
Y210A
-
site-directed mutagenesis
Y210S
-
site-directed mutagenesis
A213L
site-directed mutagenesis, analysis of substrate and cofactor binding compared to wild-type enzyme
D105A
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
D105N
K69H
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
K69I
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
K69Q
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
S275G
-
site-directed mutagenesis, the mutant shows only slightly reduced maximum activity with shikimate compared with wild-type PoptrSDH1
S275G/T318G
-
site-directed mutagenesis, the double mutant is well expressed in Escherichia coli and shows bona fide QDH activity besides its original SDH activity, which is severely reduced. Although the Ser275Gly/Thr318Gly double mutant is clearly sufficient to confer gain of activity with quinate, its activity is lower than the QDH activities of PintaQDH and PoptrQDH2 activity
T318G
-
site-directed mutagenesis, the Thr318Gly mutant yields only a very small amount of enzyme when recombinantly expressed in Escherichia coli
Y211F
results in a remarkable reduction in enzyme activity, leads to a significant decrease in kcat (345fold) and a minor increase in the Km (3fold) for shikimate. Tyr211 may play a major role in the catalytic process and a minor role in the initial substrate binding
additional information