4kp1 | pdb_00004kp1
From Proteopedia
Crystal structure of IPM isomerase large subunit from methanococcus jannaschii (MJ0499)
Function
[LEUC_METJA] Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate.[1]
About this Structure
4kp1 is a 1 chain structure. Full crystallographic information is available from OCA.
Reference
- Lee EH, Lee K, Hwang KY. Structural characterization and comparison of the large subunits of IPM isomerase and homoaconitase from Methanococcus jannaschii. Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):922-31. doi:, 10.1107/S1399004713033762. Epub 2014 Mar 19. PMID:24699638 doi:https://dx.doi.org/10.1107/S1399004713033762
- ↑ Drevland RM, Waheed A, Graham DE. Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in Methanocaldococcus jannaschii. J Bacteriol. 2007 Jun;189(12):4391-400. Epub 2007 Apr 20. PMID:17449626 doi:https://dx.doi.org/10.1128/JB.00166-07
