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 (Comment) | Organism |
---|---|
gene Rv0127 or pep2, recombinant overexpression of His-tagged enzyme in Mycobacterium smegmatis | Mycobacterium tuberculosis |
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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten type kinetics | Mycobacterium tuberculosis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required, residues K145, Q309, and D321 are involved in Mg2+ binding | Mycobacterium tuberculosis |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | O07177 | gene Rv0127 | - |
Mycobacterium tuberculosis ATCC 25618 | O07177 | gene Rv0127 | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Mycobacterium smegmatis by nickel affinity chromatography | Mycobacterium tuberculosis |
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 | 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 | Comment | Organism |
---|---|---|
Pep2 | - |
Mycobacterium tuberculosis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Mycobacterium tuberculosis |
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 |