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Literature summary for 4.1.99.12 extracted from
- Structural basis for pH dependent monomer-dimer transition of 3,4-dihydroxy 2-butanone-4-phosphate synthase domain from Mycobacterium tuberculosis (2011), J. Struct. Biol., 174, 374-384.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli | Mycobacterium tuberculosis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| three crystal structures of Mtb-DHBPS domain in complex with phosphate and glycerol at pH 6.0, with sulfate at pH 4.0 and with zinc and sulfate at pH 4.0 are determined at 1.8, 2.06 and 2.06 A resolution, respectively | Mycobacterium tuberculosis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | A5U2B7 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| using Ni-NTA chromatography | Mycobacterium tuberculosis |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | between pH 6.0-9.0, gel filtration | Mycobacterium tuberculosis |
| monomer | below pH 5.0 enzyme forms an inactive monomer in solution, gel filtration | Mycobacterium tuberculosis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 3,4-dihydroxy 2-butanone-4-phosphate synthase | - |
Mycobacterium tuberculosis |
| Mtb-DHBPS | - |
Mycobacterium tuberculosis |
| ribA2 | gene name, bi-bifunctional enzyme with DHBPS and GTPCH-II domains at N- and C-termini, respectively | Mycobacterium tuberculosis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Mycobacterium tuberculosis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at, maximal activity | Mycobacterium tuberculosis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 9 | enzyme loses activity below pH 5.0 and above pH 9.0 | Mycobacterium tuberculosis |
| 5 | - |
below pH 5.0 enzyme forms an inactive monomer in solution. The functional activity of Mtb-DHBPS and its dimeric state can be restored by increasing the pH between 6.0 and 9.0 | Mycobacterium tuberculosis |
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Release 2023.1 (January 2023)
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