LYS12 cDNA ORF clone, Saccharomyces cerevisiae S288C

The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.
Churcher C, Bowman S, Badcock K, Bankier A, Brown D, Chillingworth T, Connor R, Devlin K, Gentles S, Hamlin N, Harris D, Horsnell T, Hunt S, Jagels K, Jones M, Lye G, Moule S, Odell C, Pearson D, Rajandream M, Rice P, Rowley N, Skelton J, Smith V, Barrell B
Nature387(6632 Suppl)84-7(1997 May)

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

This pH independence of the chemical reaction over the range 5.5-9.5 is consistent with the much slower conformational change that would effectively perturb the observed pK values for catalytic groups to lower and higher pH
Title: Evidence for an induced conformational change in the catalytic mechanism of homoisocitrate dehydrogenase for Saccharomyces cerevisiae: Characterization of the D271N mutant enzyme.

Data suggest that K206 of homoisocitrate dehydrogenase acts as a general base in the hydride transfer step of the wild-type enzyme but as a general acid in the Y150F mutant enzyme, replacing Y150 in the tautomerization reaction.
Title: Site-directed mutagenesis as a probe of the acid-base catalytic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae.

kinetic mechanism in toward oxidative decarboxylation of isocitrate, based on initial velocity studies in absence & presence of dead-end inhibitors, suggests random addition of NAD & isocitrate with Mg2+ binding before isocitrate in rapid equilibrium
Title: Complete kinetic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae.