1.1.1.25: shikimate dehydrogenase

This is an abbreviated version, for detailed information about shikimate dehydrogenase, go to the full flat file.

Reaction

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

Synonyms

3-dehydroquinate dehydratase/shikimate dehydrogenase, 5-dehydroshikimate reductase, ael1, Af2327, AroE, cgR_0495, cgR_1677, dehydroquinate dehydratase-shikimate dehydrogenase, dehydroshikimic reductase, DHD/SHD, DHQ-SDH, HI0607, More, MtbSD, NADP-dependent shikimate dehydrogenase, qsuD, rifI, SD, SDH, sdhL, shikimate 5-dehydrogenase, shikimate dehydrogenase, shikimate oxidoreductase, shikimate:NADP oxidoreductase, shikimate:NADP+ 5-oxidoreductase, SKDH, tm0346

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

Engineering

Engineering on EC 1.1.1.25 - shikimate dehydrogenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
ENGINEERING
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
T381A
-
site-directed mutagenesis, more than twentyfold decrease in kcat value
T381S
-
site-directed mutagenesis, fourfold decrease in kcat value, slight decrease in Km value
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
D103X
-
site-directed mutagenesis of paralogue HI0607, inactive mutant
K67H
-
site-directed mutagenesis of paralogue HI0607, inactive mutant
D105A
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
D105N
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
K69H
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37C 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 37C 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 37C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
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