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Literature summary for 2.1.2.1 extracted from
- Unusual structural, functional, and stability properties of serine hydroxymethyltransferase from Mycobacterium tuberculosis (2003), J. Biol. Chem., 278, 40793-40805.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| SHM1 | Mycobacterium tuberculosis |
| SHM2 | Mycobacterium tuberculosis |
General Stability
| General Stability | Organism |
|---|---|
| guanidinium chloride-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations, SHM1 | Mycobacterium tuberculosis |
| guanidinium chloride-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations, SHM2 | Mycobacterium tuberculosis |
| urea-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations. The enzyme-bound pyridoxal 5'-phosphate gets dissociated from the enzyme on treatment with about 1.25 M urea, SHM1 | Mycobacterium tuberculosis |
| urea-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations. The enzyme-bound pyridoxal 5'-phosphate gets dissociated from the enzyme on treatment with about 1.25 M urea, SHM2 | Mycobacterium tuberculosis |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 45000 | - |
2 * 45000, SHM1, SDS-PAGE | Mycobacterium tuberculosis |
| 45500 | - |
2 * 45500, SHM2, SDS-PAGE | Mycobacterium tuberculosis |
| 87100 | - |
SHM2, gel filtration | Mycobacterium tuberculosis |
| 91200 | - |
SHM1, gel filtration | Mycobacterium tuberculosis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | P9WGI7 | - |
- |
| Mycobacterium tuberculosis | P9WGI9 | - |
- |
| Mycobacterium tuberculosis H37Rv | P9WGI7 | - |
- |
| Mycobacterium tuberculosis H37Rv | P9WGI9 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| SHM1 | Mycobacterium tuberculosis |
| SHM2 | Mycobacterium tuberculosis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | SHM1 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme | Mycobacterium tuberculosis | ? | - |
? |  |
| additional information | SHM2 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme | Mycobacterium tuberculosis | ? | - |
? | |
| additional information | SHM2 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme | Mycobacterium tuberculosis H37Rv | ? | - |
? | |
| additional information | SHM1 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme | Mycobacterium tuberculosis H37Rv | ? | - |
? | |
| tetrahydrofolate + L-Ser | - |
Mycobacterium tuberculosis | 5,10-methylenetetrahydrofolate + glycine | - |
r | |
| tetrahydrofolate + L-Ser | - |
Mycobacterium tuberculosis H37Rv | 5,10-methylenetetrahydrofolate + glycine | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 45000, SHM1, SDS-PAGE | Mycobacterium tuberculosis |
| dimer | 2 * 45500, SHM2, SDS-PAGE | Mycobacterium tuberculosis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| glycine hydroxymethyltransferrase | - |
Mycobacterium tuberculosis |
| serine hydroxymethyltransferase | - |
Mycobacterium tuberculosis |
| SHM1 | - |
Mycobacterium tuberculosis |
| SHM2 | - |
Mycobacterium tuberculosis |
| SHMT1 | - |
Mycobacterium tuberculosis |
| SHMT2 | - |
Mycobacterium tuberculosis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
transition temperature of SHM1 | Mycobacterium tuberculosis |
| 69 | - |
transition temperature of SHM1 | Mycobacterium tuberculosis |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
transition of SHM2 is between pH 6.5 and 11 and centered at about pH 8.0 | Mycobacterium tuberculosis |
| 9 | - |
native SHM2 dimer dissociates into monomer | Mycobacterium tuberculosis |
| 9.25 | - |
transition of SHM1 is between pH 8 and 11 and centered at about pH 9.25 | Mycobacterium tuberculosis |
| 10.5 | - |
resistant to alkaline denaturation up to, SHM1 | Mycobacterium tuberculosis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | SHM1 contains 1 mol per mol of enzyme dimer | Mycobacterium tuberculosis | |
| pyridoxal 5'-phosphate | SHM2 contains 2 mol per mol of enzyme dimer | Mycobacterium tuberculosis | |
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