2-isopropylmalate synthase

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(New page: <StructureSection load='3fig' size='340' side='right' caption='Caption for this structure' scene=''> == Function == '''2-isopropylmalate synthase''' (LeuA) or '''α-isopropylmalate synt...)
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<StructureSection load='4ov9' size='340' side='right' caption='2-isopropylmalate synthase complex with leucine, glycerol and Zn+2 ion (grey) (PDB code [[3fig]])' scene=''>
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<StructureSection load='3fig' size='340' side='right' caption='Caption for this structure' scene=''>
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== Function ==
== 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<ref>PMID:16846242</ref>.
'''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<ref>PMID:16846242</ref>.
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== Disease ==
 
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== Relevance ==
 
== Structural highlights ==
== Structural highlights ==
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**[[3hpz]] – MtLeuA + bromopyruvate + Zn<br />
**[[3hpz]] – MtLeuA + bromopyruvate + Zn<br />
**[[3hq1]] – MtLeuA + citrate + Zn<br />
**[[3hq1]] – MtLeuA + citrate + Zn<br />
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**[[3fig]] – MtLeuA + leucine + Zn<br />
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**[[3fig]] – MtLeuA (mutant) + leucine + Zn<br />
**[[1sr9]] – MtLeuA + ketovaline + Zn<br />
**[[1sr9]] – MtLeuA + ketovaline + Zn<br />
**[[3eeg]] – LeuA – ''Cytophaga hutchinsonii''<br />
**[[3eeg]] – LeuA – ''Cytophaga hutchinsonii''<br />

Revision as of 10:50, 19 December 2016

2-isopropylmalate synthase complex with leucine, glycerol and Zn+2 ion (grey) (PDB code 3fig)

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3D structures of 2-isopropylmalate synthase

Updated on 19-December-2016

References

  1. de Carvalho LP, Blanchard JS. Kinetic and chemical mechanism of alpha-isopropylmalate synthase from Mycobacterium tuberculosis. Biochemistry. 2006 Jul 25;45(29):8988-99. PMID:16846242 doi:http://dx.doi.org/10.1021/bi0606602

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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