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Literature summary for 4.2.1.33 extracted from

  • Lee, E.H.; Lee, K.; Hwang, K.Y.
    Structural characterization and comparison of the large subunits of IPM isomerase and homoaconitase from Methanococcus jannaschii (2014), Acta Crystallogr. Sect. D, 70, 922-931.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3) Star cells Methanocaldococcus jannaschii

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapour-diffusion methodand hanging-drop vapour diffusion at 20°C, structures of oxidized and reduced forms of the large subunit of isopropylmalate isomerase (ox-MJ0499 and red-MJ0499, respectively) are reported at 1.8 and 2.7 A resolution, respectively. Significant large conformational changes are observed in the active site of red-MJ0499 when compared with ox-MJ0499 Methanocaldococcus jannaschii

Metals/Ions

Metals/Ions Comment Organism Structure
Iron-sulfur cluster the structure of the protein has unbound Fe-S clusters and contains a fourth cysteine in the active site Methanocaldococcus jannaschii

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii P81291 large subunit of 3-isopropylmalate dehydratase
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Methanocaldococcus jannaschii DSM 2661 P81291 large subunit of 3-isopropylmalate dehydratase
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Purification (Commentary)

Purification (Comment) Organism
-
Methanocaldococcus jannaschii

Synonyms

Synonyms Comment Organism
isopropylmalate isomerase
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Methanocaldococcus jannaschii
leuC
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Methanocaldococcus jannaschii
MJ0499 gene name, large subunit of 3-isopropylmalate dehydratase Methanocaldococcus jannaschii