2-isopropylmalate synthase
From Proteopedia
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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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== 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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== 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 /> | ||
- | **[[3fig]] – MtLeuA + leucine + Zn<br /> | + | **[[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
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3D structures of 2-isopropylmalate synthase
Updated on 19-December-2016
References
- ↑ 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