Saccharopine dehydrogenase [NAD+, L-lysine-forming] (P38998)

Identification
NameSaccharopine dehydrogenase [NAD+, L-lysine-forming]
Synonyms
  • SDH
  • Lysine--2-oxoglutarate reductase
Gene NameLYS1
Enzyme Class
Biological Properties
General FunctionInvolved in oxidoreductase activity
Specific FunctionCatalyzes the NAD(+)-dependent cleavage of saccharopine to L-lysine and 2-oxoglutarate
Cellular LocationCytoplasm
SMPDB Pathways
lysine metabolismPW002420 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Lysine biosynthesisec00300 Map00300
Lysine degradationec00310 Map00310
SMPDB Reactions
Saccharopine + NAD + water → NADH + hydron + Oxoglutaric acid + L-Lysine
KEGG Reactions
NAD + water + Saccharopine ↔ NADH + Oxoglutaric acid + hydron + L-Lysine
Metabolites
YMDB IDNameView
YMDB00019SaccharopineShow
YMDB00110NADShow
YMDB00143NADHShow
YMDB00153Oxoglutaric acidShow
YMDB00330L-LysineShow
YMDB00412NAD(+)Show
YMDB00426NADPHShow
YMDB00862hydronShow
YMDB00890waterShow
GO Classification
Component
Not Available
Function
oxidoreductase activity
catalytic activity
Process
oxidation reduction
metabolic process
Gene Properties
Chromosome Locationchromosome 9
LocusYIR034C
Gene Sequence>1122 bp ATGGCTGCCGTCACATTACATCTAAGAGCTGAAACTAAACCCCTAGAGGCACGTGCTGCC TTAACACCTACCACGGTTAAAAAACTGATAGCTAAGGGCTTCAAAATATATGTAGAGGAC AGTCCACAATCTACTTTCAATATTAACGAATATCGTCAAGCAGGTGCCATTATAGTGCCT GCAGGTTCATGGAAAACCGCTCCACGCGACAGAATCATTATAGGTTTGAAGGAAATGCCT GAAACCGATACTTTCCCTCTAGTCCACGAACACATCCAGTTTGCTCACTGCTACAAAGAC CAAGCTGGGTGGCAAAATGTCCTTATGAGATTTATTAAGGGACACGGTACTCTATATGAT TTGGAATTTTTGGAAAATGACCAAGGTAGAAGAGTTGCTGCCTTTGGATTTTACGCTGGG TTCGCAGGTGCAGCCCTTGGTGTAAGAGACTGGGCATTCAAGCAAACGCATTCTGACGAT GAAGACTTGCCTGCAGTGTCGCCTTACCCCAATGAAAAGGCGTTGGTTAAAGATGTTACC AAAGATTATAAAGAAGCCTTAGCCACCGGCGCCAGAAAGCCAACCGTGTTAATCATTGGT GCGCTAGGAAGATGTGGTTCCGGTGCCATCGATCTGTTGCACAAAGTTGGTATTCCAGAT GCTAACATATTAAAATGGGATATCAAAGAAACTTCCCGTGGTGGTCCCTTTGACGAAATT CCACAAGCTGATATTTTCATCAATTGTATATATCTATCGAAGCCAATTGCTCCTTTCACT AACATGGAGAAACTGAATAATCCTAACAGAAGACTAAGGACCGTGGTGGACGTATCAGCA GACACTACCAACCCTCACAACCCCATCCCAATATACACTGTGGCTACTGTGTTTAACAAA CCTACCGTTCTGGTACCTACCACTGTCGGGCCTAAATTATCTGTCATCTCTATTGATCAC TTGCCTTCTTTGCTGCCAAGAGAAGCTTCAGAATTTTTCTCTCATGATCTTTTACCATCT TTAGAGCTCCTACCTCAAAGAAAAACTGCTCCTGTCTGGGTTAGAGCCAAGAAATTGTTC GATAGACATTGCGCTCGTGTTAAAAGATCTTCAAGATTGTAG
Protein Properties
Pfam Domain Function
Protein Residues373
Protein Molecular Weight41464.39844
Protein Theoretical pI9.56
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Saccharopine dehydrogenase [NAD+, L-lysine-forming] MAAVTLHLRAETKPLEARAALTPTTVKKLIAKGFKIYVEDSPQSTFNINEYRQAGAIIVP AGSWKTAPRDRIIIGLKEMPETDTFPLVHEHIQFAHCYKDQAGWQNVLMRFIKGHGTLYD LEFLENDQGRRVAAFGFYAGFAGAALGVRDWAFKQTHSDDEDLPAVSPYPNEKALVKDVT KDYKEALATGARKPTVLIIGALGRCGSGAIDLLHKVGIPDANILKWDIKETSRGGPFDEI PQADIFINCIYLSKPIAPFTNMEKLNNPNRRLRTVVDVSADTTNPHNPIPIYTVATVFNK PTVLVPTTAGPKLSVISIDHLPSLLPREASEFFSHDLLPSLELLPQRKTAPVWVRAKKLF DRHCARVKRSSRL
References
External Links
ResourceLink
Saccharomyces Genome Database LYS1
Uniprot IDP38998
Uniprot NameLYS1_YEAST
GenBank Gene IDX77362
Genebank Protein ID453184
General Reference
  • Fujioka, M., Nakatani, Y. (1970). "A kinetic study of saccharopine dehydrogenase reaction." Eur J Biochem 16:180-186.4318475
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • 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., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Nature 387:84-87.9169870
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Fujioka, M., Takata, Y., Ogawa, H., Okamoto, M. (1980). "The inactivation of saccharopine dehydrogenase (L-lysine-forming) by diethyl pyrocarbonate." J Biol Chem 255:937-942.6985909
  • Ogawa, H., Okamoto, M., Fujioka, M. (1979). "Chemical modification of the active site sulfhydryl group of saccharopine dehydrogenase (L-lysine-forming)." J Biol Chem 254:7030-7035.378997
  • Ogawa, H., Fujioka, M. (1978). "Purification and characterization of saccharopine dehydrogenase from baker's yeast." J Biol Chem 253:3666-3670.418069
  • Ogawa, H., Fujioka, M. (1980). "The reaction of pyridoxal 5'-phosphate with an essential lysine residue of saccharopine dehydrogenase (L-lysine-forming)." J Biol Chem 255:7420-7425.6771291
  • Ogawa, H., Hase, T., Fujioka, M. (1980). "Amino acid sequence of a peptide containing an essential cysteine residue of yeast saccharopine dehydrogenase (L-lysine-forming)." Biochim Biophys Acta 623:225-228.6769500
  • Saunders, P. P., Broquist, H. P. (1966). "Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. IV. Saccharopine dehydrogenase." J Biol Chem 241:3435-3440.4287986
  • Ramos, F., Dubois, E., Pierard, A. (1988). "Control of enzyme synthesis in the lysine biosynthetic pathway of Saccharomyces cerevisiae. Evidence for a regulatory role of gene LYS14." Eur J Biochem 171:171-176.3123231