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Literature summary extracted from

  • Manikandan, K.; Geerlof, A.; Zozulya, A.V.; Svergun, D.I.; Weiss, M.S.
    Structural studies on the enzyme complex isopropylmalate isomerase (LeuCD) from Mycobacterium tuberculosis (2011), Proteins, 79, 35-49.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.33 expression of His6-tagged LeuD in Escherichia coli strain BL21(DE3) Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.33 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

EC Number Protein Variants Comment Organism
4.2.1.33 additional information construction of three C-terminally truncated variants of small subunit LeuD Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.33 (2S)-2-isopropylmalate + H2O Mycobacterium tuberculosis
-
 (2R,3S)-3-isopropylmalate
-
 ?
4.2.1.33 (2S)-2-isopropylmalate + H2O Mycobacterium tuberculosis H37Rv
-
 (2R,3S)-3-isopropylmalate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.33 Mycobacterium tuberculosis P9WK95 small subunit LeuD
-
4.2.1.33 Mycobacterium tuberculosis P9WQF5 large subunit LeuC
-
4.2.1.33 Mycobacterium tuberculosis H37Rv P9WK95 small subunit LeuD
-
4.2.1.33 Mycobacterium tuberculosis H37Rv P9WQF5 large subunit LeuC
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.33 (2S)-2-isopropylmalate + H2O
-
 Mycobacterium tuberculosis (2R,3S)-3-isopropylmalate
-
 ?
4.2.1.33 (2S)-2-isopropylmalate + H2O
-
 Mycobacterium tuberculosis H37Rv (2R,3S)-3-isopropylmalate
-
 ?
4.2.1.33 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 ?
-
 ?
4.2.1.33 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 ?
-
 ?
4.2.1.33 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 ?
-
 ?
4.2.1.33 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

EC Number Subunits Comment Organism
4.2.1.33 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
4.2.1.33 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
4.2.1.33 More structure and oligomeric state of Mtb-LeuD in the crystal structure, overview Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
4.2.1.33 IPMI
-
 Mycobacterium tuberculosis
4.2.1.33 isopropylmalate isomerase
-
 Mycobacterium tuberculosis
4.2.1.33 LeuCD
-
 Mycobacterium tuberculosis
4.2.1.33 More the enzyme belongs to the aconitase superfamily Mycobacterium tuberculosis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4.2.1.33 15 95
-
 Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.33 7.5
-
 assay at Mycobacterium tuberculosis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.2.1.33 4 9.5
-
 Mycobacterium tuberculosis