Chain A, 2-isopropylmalate synthase

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Mechanistic and bioinformatic investigation of a conserved active site helix in α-isopropylmalate synthase from Mycobacterium tuberculosis, a member of the DRE-TIM metallolyase superfamily. [Biochemistry. 2014]
Mechanistic and bioinformatic investigation of a conserved active site helix in α-isopropylmalate synthase from Mycobacterium tuberculosis, a member of the DRE-TIM metallolyase superfamily.
Casey AK, Hicks MA, Johnson JL, Babbitt PC, Frantom PA. Biochemistry. 2014 May 13; 53(18):2915-25. Epub 2014 Apr 22.
Kinetic evidence for interdomain communication in the allosteric regulation of alpha-isopropylmalate synthase from Mycobacterium tuberculosis. [Biochemistry. 2009]
Kinetic evidence for interdomain communication in the allosteric regulation of alpha-isopropylmalate synthase from Mycobacterium tuberculosis.
de Carvalho LP, Frantom PA, Argyrou A, Blanchard JS. Biochemistry. 2009 Mar 10; 48(9):1996-2004.
TubercuList--10 years after. [Tuberculosis (Edinb). 2011]
TubercuList--10 years after.
Lew JM, Kapopoulou A, Jones LM, Cole ST. Tuberculosis (Edinb). 2011 Jan; 91(1):1-7. Epub 2010 Oct 25.

RefSeq protein
See the reference protein sequence for 2-isopropylmalate synthase (NP_218227.3).

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Transcript/Protein Information [PANTHER Classification System]
Transcript/Protein Information
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Evolutionary Trace of Functional Site [Evolutionary Trace of Functio...]
Evolutionary Trace of Functional Site

Chain A, 2-isopropylmalate synthase
Chain A, 2-isopropylmalate synthase
gi|296278396|pdb|3HPZ|A

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Protein