Cloned (Comment) | Organism |
---|---|
truncated protein E365Term is expressed in Escherichia coli BL21(DE3) Star cells and in Escherichia coli strain BW25113 lacking the alpha-isopropylmalate synthase gene | Neisseria meningitidis |
truncated protein LeuA425 is expressed in Escherichia coli Rosetta 2 cells and in Escherichia coli strain BW25113 lacking the alpha-isopropylmalate synthase gene | Mycobacterium tuberculosis |
Crystallization (Comment) | Organism |
---|---|
truncated protein E365Term, sitting drop vapor diffusion method, using 0.2 M magnesium acetate and 18% (w/v) mPEG 3350 | Neisseria meningitidis |
truncated protein LeuA425, sitting drop vapor diffusion method, using 24% (w/v) PEG 3350 and 275 mM lithium nitrate | Mycobacterium tuberculosis |
Protein Variants | Comment | Organism |
---|---|---|
additional information | the E365Term protein lacks the C-terminal allosteric regulatory domain of the wild type enzyme and is inactive | Neisseria meningitidis |
additional information | the LeuA425 protein lacks the C-terminal allosteric regulatory domain of the wild type enzyme and is inactive | Mycobacterium tuberculosis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.012 | - |
2-oxo-3-methylbutanoate | apparent value, full-length enzyme, in 50 mM HEPES (pH 7.5), at 25°C | Mycobacterium tuberculosis | |
0.03 | - |
2-oxo-3-methylbutanoate | apparent value, full-length enzyme, in 50 mM HEPES (pH 7.5), at 25°C | Neisseria meningitidis | |
0.035 | - |
acetyl-CoA | apparent value, full-length enzyme, in 50 mM HEPES (pH 7.5), at 25°C | Neisseria meningitidis | |
0.136 | - |
acetyl-CoA | apparent value, full-length enzyme, in 50 mM HEPES (pH 7.5), at 25°C | Mycobacterium tuberculosis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | contains two Mn2+ ion | Mycobacterium tuberculosis | |
Mn2+ | contains two Mn2+ ions | Neisseria meningitidis | |
Zn2+ | contains one Zn2+ ion | Mycobacterium tuberculosis | |
Zn2+ | contains one Zn2+ ion | Neisseria meningitidis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WQB3 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WQB3 | - |
- |
Neisseria meningitidis | Q9JZG1 | - |
- |
Purification (Comment) | Organism |
---|---|
Talon metal affinity resin column chromatography and Sephacryl 200 gel filtration | Mycobacterium tuberculosis |
Talon metal affinity resin column chromatography and Sephacryl 200 gel filtration | Neisseria meningitidis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxo-3-methylbutanoate + acetyl-CoA + H2O | - |
Mycobacterium tuberculosis | 3-hydroxy-4-methyl-3-carboxypentanoate + CoA | - |
ir | |
2-oxo-3-methylbutanoate + acetyl-CoA + H2O | - |
Neisseria meningitidis | 3-hydroxy-4-methyl-3-carboxypentanoate + CoA | - |
ir | |
2-oxo-3-methylbutanoate + acetyl-CoA + H2O | - |
Mycobacterium tuberculosis H37Rv | 3-hydroxy-4-methyl-3-carboxypentanoate + CoA | - |
ir |
Subunits | Comment | Organism |
---|---|---|
homodimer | x-ray crystallography | Mycobacterium tuberculosis |
homodimer | x-ray crystallography | Neisseria meningitidis |
Synonyms | Comment | Organism |
---|---|---|
alpha-IPMS | - |
Mycobacterium tuberculosis |
alpha-IPMS | - |
Neisseria meningitidis |
alpha-isopropylmalate synthase I | - |
Mycobacterium tuberculosis |
alpha-isopropylmalate synthase I | - |
Neisseria meningitidis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3.5 | - |
acetyl-CoA | full-length enzyme, in 50 mM HEPES (pH 7.5), at 25°C | Mycobacterium tuberculosis | |
3.5 | - |
2-oxo-3-methylbutanoate | full-length enzyme, in 50 mM HEPES (pH 7.5), at 25°C | Mycobacterium tuberculosis | |
13 | - |
acetyl-CoA | full-length enzyme, in 50 mM HEPES (pH 7.5), at 25°C | Neisseria meningitidis | |
13 | - |
2-oxo-3-methylbutanoate | full-length enzyme, in 50 mM HEPES (pH 7.5), at 25°C | Neisseria meningitidis |