LYS1 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)

investigation of crystal structure and catalytic mechanism of LYS1: Data are consistent with role for K77 acting as base accepting proton from lysine prior to nucleophilic attack and with role for H96 acting as acid-base catalyst to form imine.
Title: Evidence in support of lysine 77 and histidine 96 as acid-base catalytic residues in saccharopine dehydrogenase from Saccharomyces cerevisiae.

A disulfide bond between cys-205 and cys-249, in the vicinity of the NAD-binding site, is observed in the apoenzyme, while a dithiol is observed in a structure with AMP bound, suggesting preferential binding of the dinucleotide to reduced enzyme.
Title: The oxidation state of active site thiols determines activity of saccharopine dehydrogenase at low pH.

In the direction of lysine formation, once NAD+ and saccharopine bind, a group with a pKa of 6.2 accepts a proton from the secondary amine of saccharopine as it is oxidized.
Title: A proposed proton shuttle mechanism for saccharopine dehydrogenase from Saccharomyces cerevisiae.