Ketol-acid reductoisomerase
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
'''Ketol-acid reductoisomerase''' (KARI) is a bifunctional enzyme which catalizes two steps in the biosynthesis of branched-chain amino acids. KARI catalyzes the isomerization of alkyls and the NADPH-dependent reduction of a 2-ketoacid<ref>PMID:15654896</ref>. There are two forms of KARI. A short form – '''Class I''' – found in fungi and most bacteria and a long form (see also [[Arnold lab: coenzyme specificity]]) – '''Class II''' – found in plants. | '''Ketol-acid reductoisomerase''' (KARI) is a bifunctional enzyme which catalizes two steps in the biosynthesis of branched-chain amino acids. KARI catalyzes the isomerization of alkyls and the NADPH-dependent reduction of a 2-ketoacid<ref>PMID:15654896</ref>. There are two forms of KARI. A short form – '''Class I''' – found in fungi and most bacteria and a long form (see also [[Arnold lab: coenzyme specificity]]) – '''Class II''' – found in plants. | ||
| + | == 3D Structures of Ketol-acid reductoisomerase == | ||
| + | [[Ketol-acid reductoisomerase 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
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**[[4xdy]] – KARI + NADPH + Mg – archea<br /> | **[[4xdy]] – KARI + NADPH + Mg – archea<br /> | ||
**[[4xdz]] – IaKARI + NADPH + Mg <br /> | **[[4xdz]] – IaKARI + NADPH + Mg <br /> | ||
| - | **[[5w3k]], [[6aqj]] – SaKARI + NADPH + Mg – Staphyloccocus aureus<br /> | + | **[[5w3k]], [[6aqj]] – SaKARI + NADPH + Mg – ''Staphyloccocus aureus''<br /> |
| + | **[[6bul]], [[6c55]], [[6c5n]] – SaKARI + NADPH + Mg + hydroxyoxamate inhibitor<br /> | ||
**[[4kqx]] – SeKARI + NAD + Mg + hydroxyl-isopropyloxamate <br /> | **[[4kqx]] – SeKARI + NAD + Mg + hydroxyl-isopropyloxamate <br /> | ||
| + | **[[6jcw]] – KARI + Mg – ''Saccharolobus solfataricus'' – Cryo EM<br /> | ||
| + | **[[6jx2]] – KARI + NADPH + Mg – ''Corynebacterium glutamicum''<br /> | ||
*KARI class II | *KARI class II | ||
Revision as of 07:38, 17 October 2019
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3D Structures of Ketol-acid reductoisomerase
Updated on 17-October-2019
References
- ↑ Tyagi R, Lee YT, Guddat LW, Duggleby RG. Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site. FEBS J. 2005 Jan;272(2):593-602. PMID:15654896 doi:http://dx.doi.org/10.1111/j.1742-4658.2004.04506.x
