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Literature summary extracted from

  • Kenyon, C.P.; Roth, R.L.
    The role of the C8 proton of ATP in the catalysis of shikimate kinase and adenylate kinase (2012), BMC Biochem., 13, 15.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.71 expression of N-termminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.71 K15I site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Mycobacterium tuberculosis
2.7.1.71 K15R site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Mycobacterium tuberculosis
2.7.1.71 R110A site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Mycobacterium tuberculosis
2.7.1.71 R117 site-directed mutagenesis, inactive mutant Mycobacterium tuberculosis
2.7.1.71 T17I site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Mycobacterium tuberculosis
2.7.1.71 T17R site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.71 additional information
-
 additional information steady-state kinetics, analysis of wild-type an dmutant enzymes, overview Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.71 ATP + shikimate Mycobacterium tuberculosis
-
 ADP + 3-phosphoshikimate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.71 Mycobacterium tuberculosis
-
 gene aroK
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.71 recombinant N-termminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by immobilized metal affinity chromatography and dialysis Mycobacterium tuberculosis

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.71 ATP + shikimate = ADP + 3-phosphoshikimate phosphoryl transfer mechanism of shikimate kinase, overview Mycobacterium tuberculosis
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.1.71 101.9
-
 pH 6.8, 37°C Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.71 ATP + shikimate
-
 Mycobacterium tuberculosis ADP + 3-phosphoshikimate
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.71 30 37 assay at Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.71 6.8
-
 assay at Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.71 ATP the adenyl moiety of ATP plays a direct role in the regulation of ATP binding and/or phosphoryl transfer, role of the C8 proton of ATP and conserved Thr residues interacting with the C8-H in the catalysis of shikimate kinase, mechanism, overview Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.7.1.71 malfunction 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 Mycobacterium tuberculosis
2.7.1.71 physiological function 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 Mycobacterium tuberculosis