1x0l

Structural highlights

Function

HICDH_THET2 Catalyzes the NAD(+)-dependent conversion of homoisocitrate to alpha-ketoadipate. In addition, has high activity with citrate, but is inactive with 3-isopropylmalate.^{[1] [2]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

1. ↑ Miyazaki J, Kobashi N, Nishiyama M, Yamane H. Characterization of homoisocitrate dehydrogenase involved in lysine biosynthesis of an extremely thermophilic bacterium, Thermus thermophilus HB27, and evolutionary implication of beta-decarboxylating dehydrogenase. J Biol Chem. 2003 Jan 17;278(3):1864-71. Epub 2002 Nov 8. PMID:12427751 doi:http://dx.doi.org/10.1074/jbc.M205133200
2. ↑ Suzuki Y, Asada K, Miyazaki J, Tomita T, Kuzuyama T, Nishiyama M. Enhancement of the latent 3-isopropylmalate dehydrogenase activity of promiscuous homoisocitrate dehydrogenase by directed evolution. Biochem J. 2010 Oct 11;431(3):401-10. PMID:20735360 doi:10.1042/BJ20101246