2.7.1.71: shikimate kinase
This is an abbreviated version!
For detailed information about shikimate kinase, go to the full flat file.
Word Map on EC 2.7.1.71
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2.7.1.71
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chorismate
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shikimate-3-phosphate
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chrysanthemi
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oseltamivir
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dahp
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5-enolpyruvylshikimate
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3-deoxy-d-arabino-heptulosonate
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dehydroquinate
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7-phosphate
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drug development
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synthesis
- 2.7.1.71
- chorismate
-
shikimate-3-phosphate
- chrysanthemi
- oseltamivir
- dahp
-
5-enolpyruvylshikimate
-
3-deoxy-d-arabino-heptulosonate
- dehydroquinate
- 7-phosphate
- drug development
- synthesis
Reaction
Synonyms
adenosine triphosphate: shikimate-3-phosphotransferase, AroK, AroL, AtSK1, AtSK2, kinase (phosphorylating), shikimate, kinase, shikimate (phosphorylating), MtSK, OsSK1, OsSK2, OsSK3, Rv2539c, shikimate kinase II, shikimate kinase-like 1, SK I, SK II, SK1, SK2, SKI, SKII, SKL1, type I shikimate kinase, aroK-encoded, type II shikimate kinase
ECTree
2.7.1.71 shikimate kinaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.1.71 - shikimate kinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
K138N
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
K87R
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
L233F
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
N234K
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
R120K
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
S152N
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
S251N
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
T230S
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
C13S
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enzymatically active mutant, turnover-number is 65% of that of the wild-type enzyme
C162S
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turnover-number is 1.14fold higher than that of the wild-type enzyme
K15M
E114A
site-directed mutagensis, the mutant shows 82% of wlld-type activity
F48Y
site-directed mutagensis, the mutant shows 40% of wlld-type activity
M10A
site-directed mutagensis, the mutant shows 38% of wlld-type activity
R132A
site-directed mutagensis, the mutant shows 5% of wlld-type activity
R57A
site-directed mutagensis, the mutant shows 2% of wlld-type activity
R57K
site-directed mutagensis, the mutant shows 2% of wlld-type activity
K15I
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K15R
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R110A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
T17I
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T17R
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information
K15M
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inactive mutant enzyme, increased thermostability and affinity for ATP when compared to the wild-type enzyme, the organization of the P-loop and flanking regions is heavily disturbed
additional information
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inactivation of the aroK gene in an shikimate-producing Escherichia coli strain DHPYA-T7. In this strain, the aroL, ptsHIcrr and ydiB genes are deleted, and the tktA, glk, aroE and aroB genes are overexpressed. Accumulation of shikimate increases 2.69fold after aroK gene deletion and 1.29fold after antisense RNA interference. The activity of shikimate kinase in the knockout strain DHPYAAS-T7 is 0.21fold of that in the antisense strain DHPYAS-T7, while the accumulation of shikimate is 1.5fold in the knockout strain DHPYAAS-T7 compared to that in the antisense strain DHPYAS-T7
additional information
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inactivation of the aroK gene in an shikimate-producing Escherichia coli strain DHPYA-T7. In this strain, the aroL, ptsHIcrr and ydiB genes are deleted, and the tktA, glk, aroE and aroB genes are overexpressed. Accumulation of shikimate increases 2.69fold after aroK gene deletion and 1.29fold after antisense RNA interference. The activity of shikimate kinase in the knockout strain DHPYAAS-T7 is 0.21fold of that in the antisense strain DHPYAS-T7, while the accumulation of shikimate is 1.5fold in the knockout strain DHPYAAS-T7 compared to that in the antisense strain DHPYAS-T7
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