Sequence of LYS1_YEAST
EC Number:1.5.1.7
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
saccharopine dehydrogenase (NAD+, L-lysine-forming)
P38998
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
373
41465
Reaction
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH + H+
Other sequences found for EC No. 1.5.1.7
General information:
Sequence
0 MAAVTLHLRA ETKPLEARAA LTPTTVKKLI AKGFKIYVED SPQSTFNINE YRQAGAIIVP
60 AGSWKTAPRD RIIIGLKEMP ETDTFPLVHE HIQFAHCYKD QAGWQNVLMR FIKGHGTLYD
120 LEFLENDQGR RVAAFGFYAG FAGAALGVRD WAFKQTHSDD EDLPAVSPYP NEKALVKDVT
180 KDYKEALATG ARKPTVLIIG ALGRCGSGAI DLLHKVGIPD ANILKWDIKE TSRGGPFDEI
240 PQADIFINCI YLSKPIAPFT NMEKLNNPNR RLRTVVDVSA DTTNPHNPIP IYTVATVFNK
300 PTVLVPTTAG PKLSVISIDH LPSLLPREAS EFFSHDLLPS LELLPQRKTA PVWVRAKKLF
360 DRHCARVKRS SRL
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
185121
Churcher C.M.,Bowman S.,Badcock K.,Bankier A.T.,Brown D.,Chillingworth T.,Connor R.,Devlin K.,Gentles S.,Hamlin N.,Harris D.E.,Horsnell T.,Hunt S.,Jagels K.,Jones M.,Lye G.,Moule S.,Odell C.,Pearson D.,Rajandream M.A.,Rice P.,Rowley N.,Skelton J.,Smith V.,Walsh S.V.,Whitehead S.,Barrell B.G.
The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.
Nature
387
84-87
1997
185122
Engel S.R.,Dietrich F.S.,Fisk D.G.,Binkley G.,Balakrishnan R.,Costanzo M.C.,Dwight S.S.,Hitz B.C.,Karra K.,Nash R.S.,Weng S.,Wong E.D.,Lloyd P.,Skrzypek M.S.,Miyasato S.R.,Simison M.,Cherry J.M.
The reference genome sequence of Saccharomyces cerevisiae: Then and now.
G3 (Bethesda)
4
389-398
2014
185124
Ogawa H.,Fujioka M.
Purification and characterization of saccharopine dehydrogenase from baker's yeast.
J. Biol. Chem.
253
3666-3670
1978
185125
Ogawa H.,Hase T.,Fujioka M.
Amino acid sequence of a peptide containing an essential cysteine residue of yeast saccharopine dehydrogenase (L-lysine-forming).
Biochim. Biophys. Acta
623
225-228
1980
185126
Saunders P.P.,Broquist H.P.
Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. IV. Saccharopine dehydrogenase.
J. Biol. Chem.
241
3435-3440
1966
185127
Fujioka M.,Nakatani Y.
A kinetic study of saccharopine dehydrogenase reaction.
Eur. J. Biochem.
16
180-186
1970
185128
Ogawa H.,Okamoto M.,Fujioka M.
Chemical modification of the active site sulfhydryl group of saccharopine dehydrogenase (L-lysine-forming).
J. Biol. Chem.
254
7030-7035
1979
185129
Fujioka M.,Takata Y.,Ogawa H.,Okamoto M.
The inactivation of saccharopine dehydrogenase (L-lysine-forming) by diethyl pyrocarbonate.
J. Biol. Chem.
255
937-942
1980
185130
Ogawa H.,Fujioka M.
The reaction of pyridoxal 5'-phosphate with an essential lysine residue of saccharopine dehydrogenase (L-lysine-forming).
J. Biol. Chem.
255
7420-7425
1980
185131
Ramos F.,Dubois E.,Pierard A.
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
1988
185132
Geraghty M.T.,Bassett D.,Morrell J.C.,Gatto G.J. Jr.,Bai J.,Geisbrecht B.V.,Hieter P.,Gould S.J.
Detecting patterns of protein distribution and gene expression in silico.
Proc. Natl. Acad. Sci. U.S.A.
96
2937-2942
1999
185133
Bassett D.,Morrell J.C.,Gatto G.J. Jr.,Bai J.,Geisbrecht B.V.,Hieter P.,Gould S.J.
Proc. Natl. Acad. Sci. U.S.A.
102
516-516
2005
185134
Ghaemmaghami S.,Huh W.-K.,Bower K.,Howson R.W.,Belle A.,Dephoure N.,O'Shea E.K.,Weissman J.S.
Global analysis of protein expression in yeast.
Nature
425
737-741
2003
185135
Xu H.,West A.H.,Cook P.F.
Overall kinetic mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae.
Biochemistry
45
12156-12166
2006
185136
Van Damme P.,Lasa M.,Polevoda B.,Gazquez C.,Elosegui-Artola A.,Kim D.S.,De Juan-Pardo E.,Demeyer K.,Hole K.,Larrea E.,Timmerman E.,Prieto J.,Arnesen T.,Sherman F.,Gevaert K.,Aldabe R.
N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
Proc. Natl. Acad. Sci. U.S.A.
109
12449-12454
2012
185137
Yofe I.,Weill U.,Meurer M.,Chuartzman S.,Zalckvar E.,Goldman O.,Ben-Dor S.,Schuetze C.,Wiedemann N.,Knop M.,Khmelinskii A.,Schuldiner M.
One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy.
Nat. Methods
13
371-378
2016
185138
Al-Saryi N.A.,Al-Hejjaj M.Y.,van Roermund C.W.T.,Hulmes G.E.,Ekal L.,Payton C.,Wanders R.J.A.,Hettema E.H.
Two NAD-linked redox shuttles maintain the peroxisomal redox balance in Saccharomyces cerevisiae.
Sci. Rep.
7
11868-11868
2017
185139
Andi B.,Xu H.,Cook P.F.,West A.H.
Crystal structures of ligand-bound saccharopine dehydrogenase from Saccharomyces cerevisiae.
Biochemistry
46
12512-12521
2007
185140
Burk D.L.,Hwang J.,Kwok E.,Marrone L.,Goodfellow V.,Dmitrienko G.I.,Berghuis A.M.
Structural studies of the final enzyme in the alpha-aminoadipate pathway-saccharopine dehydrogenase from Saccharomyces cerevisiae.
J. Mol. Biol.
373
745-754
2007
185141
Kumar V.P.,Thomas L.M.,Bobyk K.D.,Andi B.,Cook P.F.,West A.H.
Evidence in support of lysine 77 and histidine 96 as acid-base catalytic residues in saccharopine dehydrogenase from Saccharomyces cerevisiae.
Biochemistry
51
857-866
2012
