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Information on EC 2.7.1.71 - shikimate kinase and Organism(s) Helicobacter pylori and UniProt Accession P56073

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Helicobacter pylori
UNIPROT: P56073 not found.
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The taxonomic range for the selected organisms is: Helicobacter pylori
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
shikimate kinase, shikimate kinase ii, atsk1, atsk2, ossk1, ossk2, shikimate kinase-like 1, type ii shikimate kinase, ossk3, atp:shikimate 3-phosphotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AroL
-
-
-
-
kinase (phosphorylating), shikimate
-
-
-
-
kinase, shikimate (phosphorylating)
-
-
-
-
shikimate kinase II
-
-
-
-
SKI
-
-
-
-
SKII
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:shikimate 3-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9031-51-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + shikimate
ADP + 3-phosphoshikimate
show the reaction diagram
ATP + shikimate
ADP + shikimate 3-phosphate
show the reaction diagram
ATP + shikimate
ADP + 3-phosphoshikimate
show the reaction diagram
-
-
-
-
?
ATP + shikimate
ADP + shikimate 3-phosphate
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + shikimate
ADP + 3-phosphoshikimate
show the reaction diagram
ATP + shikimate
ADP + shikimate 3-phosphate
show the reaction diagram
fifth step in the shikimate pathway
-
-
?
ATP + shikimate
ADP + 3-phosphoshikimate
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3R,4R,5R)-3,4-dihydroxy-5-(3-methoxybenzyloxy)cyclohex-1-ene-1-carboxylic acid
-
(3R,4R,5R)-3,4-dihydroxy-5-(3-methylbenzyloxy)cyclohex-1-ene-1-carboxylic acid
-
(3R,4R,5R)-3,4-dihydroxy-5-(4-methylbenzyloxy)cyclohex-1-ene-1-carboxylic acid
-
(3R,4R,5R)-3,4-dihydroxy-5-(naphthyl-2-yl)methoxycyclohex-1-ene-1-carboxylic acid
-
(3R,4R,5R)-5-(3-fluorobenzyloxy)-3,4-dihydroxycyclohex-1-ene-1-carboxylic acid
-
(3R,4R,5R)-5-(benzo[b]thiophen-5-yl)methoxy-3,4-dihydroxycyclohex-1-ene-1-carboxylic acid
-
(3R,4R,5R)-5-benzyloxy-3,4-dihydroxycyclohex-1-ene-1-carboxylic acid
-
(3R,4S,5R)-5-(4-benzyl-1H-1,2,3-triazol-1-yl)-3,4-dihydroxycyclohex-1-ene-1-carboxylic acid
-
(3R,4S,5R)-5-(4-phenoxymethyl-1H-1,2,3-triazol-1-yl)-3,4-dihydroxycyclohex-1-ene-1-carboxylic acid
-
(3S)-3-aminoshikimic acid
competitive reversible inhibitor
NSC162535
selective inhibitor, identification and binding analysis with enzyme mutant E144A by virtual docking analysis, isothermal titration calorimetry, and crystals structure analysis revealing an induced-fit mechanism, inactivation mechanism, detailed overview. Binding kinetics of wild-type and mutant enzymes
sodium (3R,4R,5R)-3,4-dihydroxy-5-((perfluorophenyl)methoxy)-cyclohex-1-ene-1-carboxylate
-
sodium (3R,4R,5R)-3,4-dihydroxy-5-(3-nitrobenzyloxy)cyclohex-1-ene-1-carboxylate
-
sodium (3S,4R,5R)-3-amino-5-(benzo[b]thiophen-5-yl)-methoxy-4-hydroxycyclohex-1-ene-carboxylate
-
sodium (3S,4S,5R)-3-amino-4-hydroxy-5-(naphth-2-yl)-metoxycyclohex-1-ene-carboxylate
-
(1R,4R,6S,10S)-6,10-dihydroxy-4-methyl-2-oxabicyclo[4.3.1]dec-7-ene-8-carboxylic acid
-
-
(1R,4S,6S,10S)-6,10-dihydroxy-4-methyl-2-oxabicyclo[4.3.1]dec-7-ene-8-carboxylic acid
-
-
(1R,6S,10S)-4-benzyloxymethyl-6,10-dihydroxy-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
-
(1R,6S,10S)-4-butyl-6,10-dihydroxy-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
-
(1R,6S,10S)-4-cyclopropylmethyl-6,10-dihydroxy-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
-
(1R,6S,10S)-4-ethoxymethyl-6,10-dihydroxy-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
-
(1R,6S,10S)-4-ethyl-6,10-dihydroxy-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
-
(1R,6S,10S)-4-hydroxylmethyl-6,10-dihydroxy-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
-
(1R,6S,10S)-6,10-dihydroxy-2-oxabicyclo[4.3.1]dec-7-ene-8-carboxylic acid
-
-
(1R,6S,10S)-6,10-dihydroxy-2-oxabicyclo[4.3.1]deca-4,7-diene-8-carboxylic acid
-
-
(1R,6S,10S)-6,10-dihydroxy-4-methyl-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
-
(1R,6S,10S)-6,10-dihydroxy-4-propyl-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
-
(3R,4R,5R)-3,4-dihydroxy-5-(naphthalen-2-ylmethoxy)cyclohex-1-ene-1-carboxylic acid
-
-
(3R,4R,5R)-3,4-dihydroxy-5-[(3-nitrobenzyl)oxy]cyclohex-1-ene-1-carboxylic acid
-
reversible competitive inhibitor
(3R,4R,5R)-5-(1-benzothiophen-5-ylmethoxy)-3,4-dihydroxycyclohex-1-ene-1-carboxylic acid
-
reversible competitive inhibitor
(3R,4S,5R)-5-bis(3-bromo-1H-indol-5-yl)methylamino-3,4-dihydroxycyclohex-1-eno-1-carboxylic acid
-
-
3-methoxy-4-[[2-([2-methoxy-4-[(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenoxy]methyl)benzyl]oxy]benzaldehyde
-
noncompetitive inhibitor with respect to both shikimate and MgATP
5-bromo-2-(5-[[1-(3,4-dichlorophenyl)-3,5-dioxo-4-pyrazolidinylidene]methyl]-2-furyl)benzoic acid
-
competitive inhibitor toward shikimate and noncompetitive inhibitor with respect to MgATP
sodium (3R,4S,5R)-3,4-dihydroxy-5-[[(1H-indol-5-yl)methyl]amino]cyclohex-1-ene-1-carboxylate
-
-
sodium (3R,4S,5R)-3,4-dihydroxy-5-[[(naphthalen-2-yl)methyl]amino]cyclohex-1-ene-1-carboxylate
-
-
sodium (3R,4S,5R)-5-di(naphth-2-yl)methylamino-3,4-dihydroxycyclohex-1-eno-1-carboxylate
-
-
sodium (3R,4S,5R)-5-[bis[(1-benzothiophen-5-yl)methyl]amino]-3,4-dihydroxycyclohex-1-ene-1-carboxylate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.101 - 0.231
ATP
0.039 - 0.291
shikimate
0.039
shikimate
-
at pH 7.7 and 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.116
shikimate
-
at pH 7.7 and 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
(3R,4R,5R)-3,4-dihydroxy-5-(3-methoxybenzyloxy)cyclohex-1-ene-1-carboxylic acid
at pH 7.7 and 25°C
0.0021
(3R,4R,5R)-3,4-dihydroxy-5-(3-methylbenzyloxy)cyclohex-1-ene-1-carboxylic acid
at pH 7.7 and 25°C
0.0109
(3R,4R,5R)-3,4-dihydroxy-5-(4-methylbenzyloxy)cyclohex-1-ene-1-carboxylic acid
at pH 7.7 and 25°C
0.0018
(3R,4R,5R)-3,4-dihydroxy-5-(naphthyl-2-yl)methoxycyclohex-1-ene-1-carboxylic acid
at pH 7.7 and 25°C
0.00128
(3R,4R,5R)-5-(3-fluorobenzyloxy)-3,4-dihydroxycyclohex-1-ene-1-carboxylic acid
at pH 7.7 and 25°C
0.00056
(3R,4R,5R)-5-(benzo[b]thiophen-5-yl)methoxy-3,4-dihydroxycyclohex-1-ene-1-carboxylic acid
at pH 7.7 and 25°C
0.003
(3R,4R,5R)-5-benzyloxy-3,4-dihydroxycyclohex-1-ene-1-carboxylic acid
at pH 7.7 and 25°C
0.095
(3R,4S,5R)-5-(4-benzyl-1H-1,2,3-triazol-1-yl)-3,4-dihydroxycyclohex-1-ene-1-carboxylic acid
at pH 7.7 and 25°C
0.067
(3R,4S,5R)-5-(4-phenoxymethyl-1H-1,2,3-triazol-1-yl)-3,4-dihydroxycyclohex-1-ene-1-carboxylic acid
at pH 7.7 and 25°C
0.041
sodium (3R,4R,5R)-3,4-dihydroxy-5-((perfluorophenyl)methoxy)-cyclohex-1-ene-1-carboxylate
at pH 7.7 and 25°C
0.00046
sodium (3R,4R,5R)-3,4-dihydroxy-5-(3-nitrobenzyloxy)cyclohex-1-ene-1-carboxylate
at pH 7.7 and 25°C
0.535
sodium (3S,4R,5R)-3-amino-5-(benzo[b]thiophen-5-yl)-methoxy-4-hydroxycyclohex-1-ene-carboxylate
at pH 7.7 and 25°C
0.8
sodium (3S,4S,5R)-3-amino-4-hydroxy-5-(naphth-2-yl)-metoxycyclohex-1-ene-carboxylate
Ki above 0.8 mM, at pH 7.7 and 25°C
0.465
(1R,4S,6S,10S)-6,10-dihydroxy-4-methyl-2-oxabicyclo[4.3.1]dec-7-ene-8-carboxylic acid
-
at pH 7.7 and 25°C
0.068
(1R,6S,10S)-4-benzyloxymethyl-6,10-dihydroxy-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
at pH 7.7 and 25°C
0.012
(1R,6S,10S)-4-butyl-6,10-dihydroxy-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
at pH 7.7 and 25°C
0.01
(1R,6S,10S)-4-cyclopropylmethyl-6,10-dihydroxy-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
at pH 7.7 and 25°C
0.005
(1R,6S,10S)-4-ethoxymethyl-6,10-dihydroxy-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
at pH 7.7 and 25°C
0.0155
(1R,6S,10S)-4-ethyl-6,10-dihydroxy-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
at pH 7.7 and 25°C
0.038
(1R,6S,10S)-4-hydroxylmethyl-6,10-dihydroxy-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
at pH 7.7 and 25°C
0.047
(1R,6S,10S)-6,10-dihydroxy-2-oxabicyclo[4.3.1]dec-7-ene-8-carboxylic acid
-
at pH 7.7 and 25°C
0.104
(1R,6S,10S)-6,10-dihydroxy-2-oxabicyclo[4.3.1]deca-4,7-diene-8-carboxylic acid
-
at pH 7.7 and 25°C
0.0545
(1R,6S,10S)-6,10-dihydroxy-4-methyl-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
at pH 7.7 and 25°C
0.0092
(1R,6S,10S)-6,10-dihydroxy-4-propyl-2-oxabicyclo[4.3.1]deca-4(Z),7-diene-8-carboxylic acid
-
at pH 7.7 and 25°C
0.0018
(3R,4R,5R)-3,4-dihydroxy-5-(naphthalen-2-ylmethoxy)cyclohex-1-ene-1-carboxylic acid
-
at pH 7.7 and 25°C
0.00056
(3R,4R,5R)-5-(1-benzothiophen-5-ylmethoxy)-3,4-dihydroxycyclohex-1-ene-1-carboxylic acid
-
at pH 7.7 and 25°C
0.0087
(3R,4S,5R)-5-bis(3-bromo-1H-indol-5-yl)methylamino-3,4-dihydroxycyclohex-1-eno-1-carboxylic acid
-
at pH 7.7 and 25°C
0.00948
3-methoxy-4-[[2-([2-methoxy-4-[(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenoxy]methyl)benzyl]oxy]benzaldehyde
0.00219
5-bromo-2-(5-[[1-(3,4-dichlorophenyl)-3,5-dioxo-4-pyrazolidinylidene]methyl]-2-furyl)benzoic acid
0.455
sodium (3R,4S,5R)-3,4-dihydroxy-5-[[(1H-indol-5-yl)methyl]amino]cyclohex-1-ene-1-carboxylate
-
at pH 7.7 and 25°C
0.181
sodium (3R,4S,5R)-3,4-dihydroxy-5-[[(naphthalen-2-yl)methyl]amino]cyclohex-1-ene-1-carboxylate
-
at pH 7.7 and 25°C
0.0003
sodium (3R,4S,5R)-5-di(naphth-2-yl)methylamino-3,4-dihydroxycyclohex-1-eno-1-carboxylate
-
at pH 7.7 and 25°C
0.0052
sodium (3R,4S,5R)-5-[bis[(1-benzothiophen-5-yl)methyl]amino]-3,4-dihydroxycyclohex-1-ene-1-carboxylate
-
at pH 7.7 and 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0049
NSC162535
Helicobacter pylori
pH 7.5, 25°C
0.0055
3-methoxy-4-[[2-([2-methoxy-4-[(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenoxy]methyl)benzyl]oxy]benzaldehyde
Helicobacter pylori
-
in 100 mM Tris–HCl (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 25°C
0.0064
5-bromo-2-(5-[[1-(3,4-dichlorophenyl)-3,5-dioxo-4-pyrazolidinylidene]methyl]-2-furyl)benzoic acid
Helicobacter pylori
-
in 100 mM Tris–HCl (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 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
shikimate kinase catalyzes the fifth step of the shikimate pathway for biosynthesis of aromatic amino acids
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
detailed structure-activity relationship analysis, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method using containing 0.2 M lithium sulfate, 30% (wt/vol) PEG 8000, and 0.1 M sodium acetate buffer (pH 6.5), at 20°C
hanging-drop vapor diffusion method. 1.8 A crystal structure of shikimate kinase. The crystal structure shows a three-layer alpha/beta fold consisting of a central sheet of five parallel beta-strands flanked by seven alpha-helices. An HpSK-shikimate-PO4 complex is also determined and refined to 2.3 A, revealing induced-fit movement from an open to a closed form on substrate binding
wild-type dimeric enzyme, wild-type enzyme in complex with products ADP and shikimate 3-phosphate, enzyme mutant R57A, and enzyme mutant E114A in complex with selective inhibitor NSC162535, hanging drop vapour ddiffusion metho, 50 mg/ml protein in 40 mM Tris-HCl, pH 7.0, containing 100 mM NaCl mixed with an equal volume of reservoir solution and equilibrated against 0.06 ml of reservoir solution, containing 0.2 M Li2SO4, 30% w/v PEG 8000, and 0.1 M sodium acetate, pH 6.5 for the apo-enzyme, or containing 0.1 M HEPES sodium salt, pH 7.5, 0.1 M sodium acetate, 18% w/v PEG 8000, 2% w/v 2-propanol, and 5 mM shikimate and 5 mM MgATP for the product complex enzyme, or containing 0.1 M HEPES sodium salt, pH 8.0, 8% w/v 2-propanol and 18% w/v PEG 4000 for enzyme mutant R57A, or containing 0.1 M HEPES sodium salt, pH 6.7, and 1.2 M potassium sodium tartrate tetrahydrate for the enzyme mutant E114A with inhibitor, X-ray diffraction structure determination and analysis at 1.8 A, 2.3 A, 2.4 A, and 2.53 A resolution, respectively, molecular replacement
molecular modeling and docking of inhibitors. The active site is rather roomy and deep, forming an L-shape channel on the surface of the protein, and compound 3-methoxy-4-[[2-([2-methoxy-4-[(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenoxy]methyl)benzyl]oxy]benzaldehyde prefers the corner area of L-shape channel, while compound 5-bromo-2-(5-[[1-(3,4-dichlorophenyl)-3,5-dioxo-4-pyrazolidinylidene]methyl]-2-furyl)benzoic acid binds the short arm of the channel in the binding interactions
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D33A
site-directed mutagensis, inactive mutant
D33E
site-directed mutagensis, inactive mutant
E114A
site-directed mutagensis, the mutant shows 82% of wlld-type activity
F48A
site-directed mutagensis, inactive mutant
F48Y
site-directed mutagensis, the mutant shows 40% of wlld-type activity
M10A
site-directed mutagensis, the mutant shows 38% of wlld-type activity
R116A
site-directed mutagensis, inactive mutant
R116K
site-directed mutagensis, inactive mutant
R132A
site-directed mutagensis, the mutant shows 5% of wlld-type activity
R132K
site-directed mutagensis, inactive mutant
R57A
site-directed mutagensis, the mutant shows 2% of wlld-type activity
R57K
site-directed mutagensis, the mutant shows 2% of wlld-type activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
differential scanning calorimetry experiments for evaluaton of the stability and unfolding of each of the enzyme mutants, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized-nickel ion chromatography and Superdex-75 gel filtration
immobilized-nickel ion affinity chromatography and Sephacryl S-100 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 cells
expressed in Escherichia coli BL21(DE3) cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cheng, W.C.; Chang, Y.N.; Wang, W.C.
Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase
J. Bacteriol.
187
8156-8163
2005
Helicobacter pylori (P56073), Helicobacter pylori
Manually annotated by BRENDA team
Han, C.; Zhang, J.; Chen, L.; Chen, K.; Shen, X.; Jiang, H.
Discovery of Helicobacter pylori shikimate kinase inhibitors: bioassay and molecular modeling
Bioorg. Med. Chem.
15
656-662
2007
Helicobacter pylori, Helicobacter pylori SS1
Manually annotated by BRENDA team
Cheng, W.C.; Chen, Y.F.; Wang, H.J.; Hsu, K.C.; Lin, S.C.; Chen, T.J.; Yang, J.M.; Wang, W.C.
Structures of Helicobacter pylori shikimate kinase reveal a selective inhibitor-induced-fit mechanism
PLoS ONE
7
e33481
2012
Helicobacter pylori (P56073), Helicobacter pylori
Manually annotated by BRENDA team
Prado, V.; Lence, E.; Vallejo, J.A.; Beceiro, A.; Thompson, P.; Hawkins, A.R.; Gonzalez-Bello, C.
Study of the phosphoryl-transfer mechanism of shikimate kinase by NMR spectroscopy
Chemistry
22
2758-2768
2016
Helicobacter pylori (P56073), Helicobacter pylori, Mycobacterium tuberculosis (P9WPY3), Mycobacterium tuberculosis
Manually annotated by BRENDA team
Prado, V.; Lence, E.; Maneiro, M.; Vazquez-Ucha, J.C.; Beceiro, A.; Thompson, P.; Hawkins, A.R.; Gonzalez-Bello, C.
Targeting the motion of shikimate kinase: development of competitive inhibitors that stabilize an inactive open conformation of the enzyme
J. Med. Chem.
59
5471-5487
2016
Helicobacter pylori (P56073), Helicobacter pylori, Mycobacterium tuberculosis (P9WPY3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPY3)
Manually annotated by BRENDA team
Hsu, K.C.; Cheng, W.C.; Chen, Y.F.; Wang, W.C.; Yang, J.M.
Pathway-based screening strategy for multitarget inhibitors of diverse proteins in metabolic pathways
PLoS Comput. Biol.
9
e1003127
2013
Helicobacter pylori (P56073), Helicobacter pylori
Manually annotated by BRENDA team
Prado, V.; Lence, E.; Thompson, P.; Hawkins, A.R.; Gonzalez-Bello, C.
Freezing the dynamic gap for selectivity motion-based design of inhibitors of the shikimate kinase enzyme
Chemistry
22
17988-18000
2016
Helicobacter pylori, Mycobacterium tuberculosis
Manually annotated by BRENDA team
Yao, J.; Wang, X.; Luo, H.; Gu, P.
Understanding the catalytic mechanism and the nature of the transition state of an attractive drug-target enzyme (shikimate kinase) by quantum mechanical/molecular mechanical (QM/MM) studies
Chemistry
23
16380-16387
2017
Helicobacter pylori (P56073), Helicobacter pylori
Manually annotated by BRENDA team
Pernas, M.; Blanco, B.; Lence, E.; Thompson, P.; Hawkins, A.; Gonzlez-Bello, C.
Synthesis of rigidified shikimic acid derivatives by ring-closing metathesis to imprint inhibitor efficacy against shikimate kinase enzyme
Org. Chem. Front.
6
2514-2528
2019
Helicobacter pylori, Mycobacterium tuberculosis (P9WPY3), Mycobacterium tuberculosis H37Rv (P9WPY3)
-
Manually annotated by BRENDA team