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
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shikimate-3-phosphate
- chrysanthemi
- oseltamivir
- dahp
-
5-enolpyruvylshikimate
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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
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General Information
General Information on EC 2.7.1.71 - shikimate kinase
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evolution
malfunction
metabolism
physiological function
additional information
AtSK2 belongs to the nucleoside monophosphate kinase family
evolution
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the enzyme is a member of the nucleoside monophosphate kinases (NMP kinases) family, which show large conformational changes during catalysis
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aroK gene inactivation in DHPYA-T7 leads to high shikimate accumulation, especially when this inactivation is caused by chromosomal deletion
malfunction
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mutations of the conserved threonine residues associated with the labile C8-H cause the enzymes to lose their saturation kinetics over the concentration range tested
malfunction
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an enzyme-defective mutant exhibits an albino phenotype and has dramatically reduced chlorophyll content
malfunction
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aroK gene inactivation in DHPYA-T7 leads to high shikimate accumulation, especially when this inactivation is caused by chromosomal deletion
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shikimate kinase catalyzes an intermediate step in the shikimate pathway to aromatic amino acid biosynthesis
metabolism
shikimate kinase catalyzes the fifth step of the shikimate pathway for biosynthesis of aromatic amino acids
metabolism
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shikimate kinase is the fifth enzyme in the shikimate pathway
metabolism
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the enzyme catalyzes the fifth step in the shikimate pathway
metabolism
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shikimate kinase-like 1 does not function as shikimate kinase enzyme in the shikimate pathway but is involved in auxin-related pathways during chloroplast development
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he phosphate binding domain in the apo-enzyme is fairly rigid and largely protected from solvent access, even at relatively high temperatures. The shikimate binding domain is highly flexible, the apo-enzyme tends to exhibit large conformational changes to permit LID closure after the shikimate binding. The nucleotide binding domain is initially conformationally rigid, which seems to favour the initial orientation of ADP/ATP, but becomes highly flexible at temperatures above 30°C, which may permit domain rotation. Part of the LID domain, including the phosphate binding site, is partially rigid, while another part is highly flexible and accessible to the solvent, mide H/D exchange and mass spectrometry
physiological function
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shikimate kinase is vital for the survival of Mycobacterium tuberculosis
physiological function
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the Group 2 kinase, shikimate kinase, is controlled by the C8-H of ATP, relationship between the role C8-H of ATP in the reaction mechanism and the ATP concentration as they influence the saturation kinetics of the enzyme activity, regulatory mechanism, overview. The kinase enzyme achieves 2500fold variation in KM through a combination of the various conserved push and pull mechanisms associated with the release of C8-H, the proton transfer cascades unique to the class of kinase in question and the resultant/concomitant creation of a pentavalent species from the gamma-phosphate group of ATP
physiological function
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the enzyme is essential for chloroplast development in Arabidopsis thaliana
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comparative modeling approach, molecular dynamics calculations using the Escherichia coli structure as template, prediction of in silico and disordered regions, enzyme structure analysis and modeling, overview
additional information
detailed structure-activity relationship analysis, overview. The critical conserved residues D33, F48, R57, R116, and R132 interact with shikimate. A characteristic three-layer architecture and a conformationally elastic region consisting of F48, R57, R116, and R132 are occupied by shikimate
additional information
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detailed structure-activity relationship analysis, overview. The critical conserved residues D33, F48, R57, R116, and R132 interact with shikimate. A characteristic three-layer architecture and a conformationally elastic region consisting of F48, R57, R116, and R132 are occupied by shikimate
additional information
mechanism of thermal regulation, computational analysis of AtSK1 and AtSK2 structural variation, overview
additional information
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mechanism of thermal regulation, computational analysis of AtSK1 and AtSK2 structural variation, overview
additional information
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modeling of the shikimate-binding pocket with main residues involved in intermolecular interactions with shikimate, overview
additional information
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shikimate binding to the enzyme, docking analysis, conformation of ternary dead-end enzyme-shikimate-ADP complex, molecular dynamics simulation of a fully hydrated model of the docked complex, overview
additional information
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comparative modeling approach, molecular dynamics calculations using the Escherichia coli structure as template, prediction of in silico and disordered regions, enzyme structure analysis and modeling, overview
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