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Literature summary for 2.7.1.71 extracted from
- The role of the C8 proton of ATP in the catalysis of shikimate kinase and adenylate kinase (2012), BMC Biochem., 13, 15.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of N-termminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) | Mycobacterium tuberculosis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K15I | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Mycobacterium tuberculosis |
| K15R | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Mycobacterium tuberculosis |
| R110A | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Mycobacterium tuberculosis |
| R117 | site-directed mutagenesis, inactive mutant | Mycobacterium tuberculosis |
| T17I | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Mycobacterium tuberculosis |
| T17R | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Mycobacterium tuberculosis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state kinetics, analysis of wild-type an dmutant enzymes, overview | Mycobacterium tuberculosis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + shikimate | Mycobacterium tuberculosis | - |
ADP + 3-phosphoshikimate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | - |
gene aroK | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 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
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + shikimate = ADP + 3-phosphoshikimate | phosphoryl transfer mechanism of shikimate kinase, overview | Mycobacterium tuberculosis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 101.9 | - |
pH 6.8, 37°C | Mycobacterium tuberculosis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + shikimate | - |
Mycobacterium tuberculosis | ADP + 3-phosphoshikimate | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 37 | assay at | Mycobacterium tuberculosis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.8 | - |
assay at | Mycobacterium tuberculosis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| 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
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
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