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Literature summary for 2.7.1.175 extracted from
- Synthesis of alpha-glucan in mycobacteria involves a hetero-octameric complex of trehalose synthase TreS and maltokinase Pep2 (2013), ACS Chem. Biol., 8, 2245-2255.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2, overview | Mycobacterium tuberculosis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene Rv0127 or pep2, recombinant overexpression of His-tagged enzyme in Mycobacterium smegmatis | Mycobacterium tuberculosis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D321A | site-directed mutagenesis, the Mg2+ binding residue mutant is inactive | Mycobacterium tuberculosis |
| K145A | site-directed mutagenesis, the Mg2+ binding residue mutant is inactive | Mycobacterium tuberculosis |
| Q309A | site-directed mutagenesis, the Mg2+ binding residue mutant is inactive | Mycobacterium tuberculosis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten type kinetics | Mycobacterium tuberculosis |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required, residues K145, Q309, and D321 are involved in Mg2+ binding | Mycobacterium tuberculosis |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 52000 | - |
- |
Mycobacterium tuberculosis |
| 452900 | - |
TreS-Pep2 complex, sequence calculation | Mycobacterium tuberculosis |
| 470000 | - |
TreS-Pep2 complex, ultracentrifugation, Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2 | Mycobacterium tuberculosis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + maltose | Mycobacterium tuberculosis | - |
ADP + alpha-maltose-1-phosphate | - |
? | |
| ATP + maltose | Mycobacterium tuberculosis ATCC 25618 | - |
ADP + alpha-maltose-1-phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | O07177 | gene Rv0127 | - |
| Mycobacterium tuberculosis ATCC 25618 | O07177 | gene Rv0127 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Mycobacterium smegmatis by nickel affinity chromatography | Mycobacterium tuberculosis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + maltose | - |
Mycobacterium tuberculosis | ADP + alpha-maltose-1-phosphate | - |
? | |
| ATP + maltose | - |
Mycobacterium tuberculosis ATCC 25618 | ADP + alpha-maltose-1-phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2 | Mycobacterium tuberculosis |
| trimer or tetramer | x * 52000, ultracentrifugation | Mycobacterium tuberculosis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Pep2 | - |
Mycobacterium tuberculosis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Mycobacterium tuberculosis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Mycobacterium tuberculosis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the enzyme PepS is involved in the cytoplasmic GlgE-pathway that converts trehalose to alpha(1->4),alpha(1->6)-linked glucan in 4 steps | Mycobacterium tuberculosis |
| additional information | stoichiometry of the TreS-Pep2 complex, analytical ultracentrifugation, overview | Mycobacterium tuberculosis |
| physiological function | the cell envelope of Mycobacterium tuberculosis, the bacillus causing tuberculosis, is coated by an alpha-glucan-containing capsule that has been implicated in persistence. Maltokinase Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2. Synthesis of alpha-glucan in mycobacteria involves the heterooctameric complex in the GlgE pathway. The complex formation may act as part of a regulatory mechanism of the GlgE pathway, which overall must avoid accumulation of toxic pathway intermediates, such as maltose-1-phosphate, and optimize the use of scarce nutrients | Mycobacterium tuberculosis |
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