2-isopropylmalate synthase

Function 2-isopropylmalate synthase (LeuA) or α-isopropylmalate synthase catalyzes the reversible conversion of 3-methyl-2-oxobutanoate and acetyl-CoA to 2-isopropylmalate. LeuA participates in the biosynthesis of leucine and pyruvate metabolism. Structural highlights LeuA structure is composed of 2 major domains - the catalytic N-terminal and the regulatory C-terminal. The 2 domains are separated by subdomains I and II and a short flexible hinge region between the 2 subdomains. The catalytic domain binds the substrate and the Zn+2 ion.

spinqualitylabelsall models 2-isopropylmalate synthase complex with leucine, glycerol and Zn+2 ion (grey) (PDB code 3fig) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

3D structures of 2-isopropylmalate synthase3D structures of 2-isopropylmalate synthase

Updated on 19-December-2016

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• 2-isopropylmalate synthase
  • 4ov4 – LbLeuA + ketoisovalerate + Zn – Leptospira biflexa
    
  • 4ov9 – LbLeuA + 2-isopropylmalate + Zn
    
  • 3hps – MtLeuA + isoketocaproate + leucine + Zn - Mycobacterium tuberculosis
    
  • 3hpz – MtLeuA + bromopyruvate + Zn
    
  • 3hq1 – MtLeuA + citrate + Zn
    
  • 3fig – MtLeuA (mutant) + leucine + Zn
    
  • 1sr9 – MtLeuA + ketovaline + Zn
    
  • 3eeg – LeuA – Cytophaga hutchinsonii
    
• 2-isopropylmalate synthase catalytic domain
  • 3rmj – LeuA + Mg + Mn – Neisseria meningitidis
    
  • 3u6w – MtLeuA + ketovaline + Mn
    
  • 3hpx – MtLeuA (mutant) + Ni
    
• 2-isopropylmalate synthase regulatory domain
  • 3f6h, 3f6g – EcLeuA + isoleucine + Zn – Escherichia coli