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Literature summary for 4.2.1.33 extracted from
- Structural studies on the enzyme complex isopropylmalate isomerase (LeuCD) from Mycobacterium tuberculosis (2011), Proteins, 79, 35-49.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of His6-tagged LeuD in Escherichia coli strain BL21(DE3) | Mycobacterium tuberculosis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| small subunit LeuD variants, X-ray diffraction structure determination and analysis at resolutions of 2.0 A for LeuD_1-156, 1.2 A for LeuD_1-168, and 2.5 A for LeuD_1-186, respectively | Mycobacterium tuberculosis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of three C-terminally truncated variants of small subunit LeuD | Mycobacterium tuberculosis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (2S)-2-isopropylmalate + H2O | Mycobacterium tuberculosis | - |
(2R,3S)-3-isopropylmalate | - |
? |  |
| (2S)-2-isopropylmalate + H2O | Mycobacterium tuberculosis H37Rv | - |
(2R,3S)-3-isopropylmalate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | P9WK95 | small subunit LeuD | - |
| Mycobacterium tuberculosis | P9WQF5 | large subunit LeuC | - |
| Mycobacterium tuberculosis H37Rv | P9WK95 | small subunit LeuD | - |
| Mycobacterium tuberculosis H37Rv | P9WQF5 | large subunit LeuC | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (2S)-2-isopropylmalate + H2O | - |
Mycobacterium tuberculosis | (2R,3S)-3-isopropylmalate | - |
? | |
| (2S)-2-isopropylmalate + H2O | - |
Mycobacterium tuberculosis H37Rv | (2R,3S)-3-isopropylmalate | - |
? | |
| additional information | the functional LeuCD complex catalyzes the stereospecific conversion reaction of alpha-isopropylmalate to beta-isopropylmalate, the active site is only completely formed after LeuC and LeuD have assembled | Mycobacterium tuberculosis | ? | - |
? | |
| additional information | the functional LeuCD complex catalyzes the stereospecific conversion reaction of alpha-isopropylmaleate to beta-isopropylmalate, the active site is only completely formed after LeuC and LeuD have assembled. The LeuD residues 30-37 form the substrate discriminating loop, and LeuD residues 70-74 the substrate binding loop | Mycobacterium tuberculosis | ? | - |
? | |
| additional information | the functional LeuCD complex catalyzes the stereospecific conversion reaction of alpha-isopropylmaleate to beta-isopropylmalate, the active site is only completely formed after LeuC and LeuD have assembled. The LeuD residues 30-37 form the substrate discriminating loop, and LeuD residues 70-74 the substrate binding loop | Mycobacterium tuberculosis H37Rv | ? | - |
? | |
| additional information | the functional LeuCD complex catalyzes the stereospecific conversion reaction of alpha-isopropylmalate to beta-isopropylmalate, the active site is only completely formed after LeuC and LeuD have assembled | Mycobacterium tuberculosis H37Rv | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterodimer | IPMI exists as a functional LeuCD complex of two subunits: the large LeuC and the small LeuD subunit, structure determination and modeling, overview | Mycobacterium tuberculosis |
| heterodimer | IPMI exists as a functional LeuCD complex of two subunits: the large LeuC and the small LeuD subunit, structure determination and modeling, overview. Presence of two LeuD subfamilies, structure modeling, overview | Mycobacterium tuberculosis |
| More | structure and oligomeric state of Mtb-LeuD in the crystal structure, overview | Mycobacterium tuberculosis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| IPMI | - |
Mycobacterium tuberculosis |
| isopropylmalate isomerase | - |
Mycobacterium tuberculosis |
| LeuCD | - |
Mycobacterium tuberculosis |
| More | the enzyme belongs to the aconitase superfamily | Mycobacterium tuberculosis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 15 | 95 | - |
Mycobacterium tuberculosis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Mycobacterium tuberculosis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 9.5 | - |
Mycobacterium tuberculosis |
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