Information on EC 2.7.1.71 - shikimate kinase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
2.7.1.71
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RECOMMENDED NAME
GeneOntology No.
shikimate kinase
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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chorismate biosynthesis from 3-dehydroquinate
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Metabolic pathways
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Phenylalanine, tyrosine and tryptophan biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
ATP:shikimate 3-phosphotransferase
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SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AroK
-
-
-
-
AroL
-
-
-
-
AtSK1
Q8GY88
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AtSK2
Q8GY88
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kinase (phosphorylating), shikimate
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-
-
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kinase, shikimate (phosphorylating)
-
-
-
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OsSK1
Q5NTH4
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OsSK2
Q5NTH3
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OsSK3
Q7X7H9
-
shikimate kinase II
-
-
-
-
SKI
-
-
-
-
SKII
-
-
-
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type I shikimate kinase, aroK-encoded
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-
CAS REGISTRY NUMBER
COMMENTARY
9031-51-0
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
two isozymes, AtSK1 and AtSK2, AatSK1 is heat-inducible
UniProt
Manually annotated by BRENDA team
gene aroK
-
-
Manually annotated by BRENDA team
shikimate kinase II; strain K12
-
-
Manually annotated by BRENDA team
shikimic acid kinase I
-
-
Manually annotated by BRENDA team
strain K12; two isoenzymes: SK1 and SK2
-
-
Manually annotated by BRENDA team
Escherichia coli DHPYA-T7
gene aroK
-
-
Manually annotated by BRENDA team
Escherichia coli K12
strain K12
-
-
Manually annotated by BRENDA team
Hansenula henricii
-
-
-
Manually annotated by BRENDA team
; strain 26695
Uniprot
Manually annotated by BRENDA team
; strain SS1
-
-
Manually annotated by BRENDA team
strain 26695
Uniprot
Manually annotated by BRENDA team
enzyme aggregate contains 5 activities: EC 1.1.1.25, EC 2.7.1.71, EC 4.2.1.10, EC 4.2.3.4 and EC 2.5.1.19
-
-
Manually annotated by BRENDA team
enzyme aggregate contains 5 activities: EC 1.1.1.25, EC 2.7.1.71, EC 4.2.1.10, EC 4.2.3.4 and EC 2.5.1.19
-
-
Manually annotated by BRENDA team
enzyme aggregate contains 5 activities: EC 1.1.1.25, EC 2.7.1.71, EC 4.2.1.10, EC 4.2.3.4 and EC 2.5.1.19
-
-
Manually annotated by BRENDA team
enzyme aggregate contains 5 activities: EC 1.1.1.25, EC 2.7.1.71, EC 4.2.1.10, EC 4.2.3.4 and EC 2.5.1.19
-
-
Manually annotated by BRENDA team
ARO 1; enzyme aggregate contains 5 activities: EC 1.1.1.25, EC 2.7.1.71, EC 4.2.1.10, EC 4.2.3.4 and 2.5.1.19
-
-
Manually annotated by BRENDA team
enzyme aggregate contains 5 activities: EC 1.1.1.25, EC 2.7.1.71, EC 4.2.1.10, EC 4.2.3.4 and 2.5.1.19
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-
Manually annotated by BRENDA team
Saccharomycopsis lipolytica
enzyme aggregate contains 5 activities: EC 1.1.1.25, EC 2.7.1.71, EC 4.2.1.10, EC 4.2.3.4 and EC 2.5.1.19
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Manually annotated by BRENDA team
enzyme aggregate contains 5 activities: EC 1.1.1.25, EC 2.7.1.71, EC 4.2.1.10, EC 4.2.3.4 and EC 2.5.1.19
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-
Manually annotated by BRENDA team
serotype 5b
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-
Manually annotated by BRENDA team
Shigella flexneri 8401
serotype 5b
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-
Manually annotated by BRENDA team
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
23
-
ATP
-
pH 7.0, 25C, mutant enzyme C13S
35
-
ATP
-
pH 7.0, 25C, wild-type enzyme
40
-
ATP
-
pH 7.0, 25C, mutant enzyme C162S
23
-
shikimate
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pH 7.0, 25C, mutant enzyme C13S
35
-
shikimate
-
pH 7.0, 25C, wild-type enzyme
40
-
shikimate
-
pH 7.0, 25C, mutant enzyme C162S
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0055
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3-methoxy-4-[[2-([2-methoxy-4-[(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenoxy]methyl)benzyl]oxy]benzaldehyde
-
in 100 mM TrisHCl (pH 8.0), 50 mM KCl, 5 mM MgCl2, 2 mM ATP, 2 mM phosphoenolpyruvate, 0.7 mM NADH, 3 U/ml proteinase K, 2.5 U/ml lactate dehydrogenase, and 2 mM shikimate, at 25C
0.0064
-
5-bromo-2-(5-[[1-(3,4-dichlorophenyl)-3,5-dioxo-4-pyrazolidinylidene]methyl]-2-furyl)benzoic acid
-
in 100 mM TrisHCl (pH 8.0), 50 mM KCl, 5 mM MgCl2, 2 mM ATP, 2 mM phosphoenolpyruvate, 0.7 mM NADH, 3 U/ml proteinase K, 2.5 U/ml lactate dehydrogenase, and 2 mM shikimate, at 25C
0.0049
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NSC162535
P56073
pH 7.5, 25C
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pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9.5
-
pH 6.0: about 50% of maximal activity, pH 9.5: optimum
6.2
9
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pH 6.2: about 20% of maximal activity in Tris propane buffer, pH 7.8: about 30% of maximal activity, pH 9.0: optimum
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Escherichia coli (strain K12)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the enzyme is fully unfolded in 4 M urea
-
unfolding of the enzyme by guanidinium chloride, in the absence of ligands there is a loss of structure over the range of 1-3 M guanidinium chloride
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differential scanning calorimetry experiments for evaluaton of the stability and unfolding of each of the enzyme mutants, overview
P56073
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, protein concentration 1 mg/ml in 0.05% M Tris-HCl buffer, pH 7.5, 10 mM MgCl2, 0.1 M NaCl, 1 mM DTT, 10% loss of activity after 1 week, 90% loss of activity after 2 months
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-20C, 50% glycerol, aggregate containing 5 activities: EC 1.1.1.25, EC 2.7.1.71, EC 4.2.1.10, 5-dehydroquinate synthase and 3-enoyl-pyruvylshikimate 5-phosphate synthase is stable for at least 1 month
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4C, 50% glycerol, aggregate containing 5 activities: EC 1.1.1.25, EC 2.7.1.71, EC 4.2.1.10, 5-dehydroquinate synthase and 3-enoyl-pyruvylshikimate 5-phosphate synthase is stable for at least 19 days
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-18C, 30% v/v glycerol, stable for several months with gradual loss of activity
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-20C, in presence of 15% glycerol, stable for up to 4 weeks without loss of activity
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Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the enzyme is fully unfolded in 4 M urea. Approximately 95% of the enzyme activity can be recovered on dilution of the urea from 4 to 0.36 M. Refolding occurs in at least four kinetic phases, the slowest of which corresponds with the regain of shikimate binding and enzyme activity
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when the enzyme is unfolded by incubation in 4 M urea, addition of NaCl or Na2SO4 leads to relatively slow refolding of the enzyme. The refolded enzyme can bind shikimate, though more weakly than the native enzyme. The refolded enzyme does not appear to be capable of binding nucleotides, nor does it possess detectable catalytic activity. The refolding process brought about by addition of salt in the presence of 4 M urea is not associated with any change in the fluorescence of the probe 8-anilino-1-naphthalenesulfonic acid
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