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(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NAD+ + H2O
L-2-aminoadipate + NADH
(S)-2-amino-6-oxohexanoate + NAD+ + H2O
L-2-aminoadipate + NADH + H+
-
-
-
?
(S)-2-amino-6-oxohexanoate + NADP+ + H2O
L-2-aminoadipate + NADPH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
alpha-aminoadipate semialdehyde + NAD(P)+ + H2O
L-2-aminoadipate + NAD(P)H + H+
-
-
-
?
alpha-aminoadipate semialdehyde + NAD+ + H2O
alpha-aminoadipate + NADH + H+
-
-
-
-
?
alpha-aminoadipate semialdehyde + NADP+ + H2O
alpha-aminoadipate + NADPH + H+
-
-
-
-
?
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
DELTA1-piperidine 6-carboxylate + NAD+ + H2O
L-alpha-aminoadipate + NADH + H+
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O
L-2-aminoadipate + NAD(P)H + H+
-
-
-
?
L-2-aminoadipate 6-semialdehyde + NAD+ + H2O
L-2-aminoadipate + NADH
L-2-aminoadipate-semialdehyde + NAD+
L-2-aminoadipate + NADH
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
L-alpha-aminoadipate + NAD(P)H + H+
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde + NAD+ + H2O
Nalpha-benzyloxycarbonyl-L-aminoadipate + NADH + H+
S-carboxymethyl-L-cysteine + NADPH
?
-
5% of the activity with L-2-aminoadipate
-
-
?
additional information
?
-
(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NAD+ + H2O
L-2-aminoadipate + NADH
-
-
-
ir
(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NAD+ + H2O
L-2-aminoadipate + NADH
-
-
-
ir
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
-
-
-
-
?
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
-
-
-
-
?
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
-
-
-
-
?
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
-
-
-
?
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
-
-
-
-
?
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
-
-
-
-
?
DELTA1-piperidine 6-carboxylate + NAD+ + H2O
L-alpha-aminoadipate + NADH + H+
-
-
-
-
r
DELTA1-piperidine 6-carboxylate + NAD+ + H2O
L-alpha-aminoadipate + NADH + H+
-
-
-
-
r
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
-
-
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
in presence of ATP + Mg2+
-
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
in presence of ATP + Mg2+
-
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
in presence of ATP + Mg2+
-
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
in presence of ATP + Mg2+
high specificity for L-alpha-aminoadipate-semialdehyde
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
-
-
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
in presence of ATP + Mg2+
-
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
in presence of ATP + Mg2+
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
-
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
key enzyme in the branched pathway for lysine and beta-lactam biosynthesis of filamentous fungi. Nitrate has a strong negative effect on enzyme formation
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
-
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
key enzyme in the branched pathway for lysine and beta-lactam biosynthesis of filamentous fungi. Nitrate has a strong negative effect on enzyme formation
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
presence of ATP required
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
-
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
in presence of ATP
-
-
?
L-2-aminoadipate 6-semialdehyde + NAD+ + H2O
L-2-aminoadipate + NADH
-
-
-
ir
L-2-aminoadipate 6-semialdehyde + NAD+ + H2O
L-2-aminoadipate + NADH
-
-
-
ir
L-2-aminoadipate 6-semialdehyde + NAD+ + H2O
L-2-aminoadipate + NADH
-
-
-
ir
L-2-aminoadipate 6-semialdehyde + NAD+ + H2O
L-2-aminoadipate + NADH
-
-
-
?
L-2-aminoadipate-semialdehyde + NAD+
L-2-aminoadipate + NADH
-
degradative enzyme
-
?
L-2-aminoadipate-semialdehyde + NAD+
L-2-aminoadipate + NADH
-
mammalian degradation of hydroxy-L-lysine via phosphohydrolysine and 2-aminoadipic semialdehyde to 2-aminoadipic acid
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
-
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
in presence of ATP and Mg2+
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
sixth step of lysine biosynthesis
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
-
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
in presence of ATP and Mg2+
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
involved in lysine biosynthetic pathway
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
in presence of ATP and Mg2+
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
involved in lysine biosynthetic pathway
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
-
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
in presence of ATP and Mg2+
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
sixth step of lysine biosynthesis
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
sixth step of lysine biosynthesis
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
alpha-aminoadipate pathway for lysine biosynthesis
-
?
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde + NAD+ + H2O
Nalpha-benzyloxycarbonyl-L-aminoadipate + NADH + H+
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde + NAD+ + H2O
Nalpha-benzyloxycarbonyl-L-aminoadipate + NADH + H+
-
-
-
-
?
additional information
?
-
-
the enzyme catalyzes both the activation of alpha-aminoadipic acid and its reduction to semialdehyde
-
-
?
additional information
?
-
-
not: glutamate delta-semialdehyde DELTA1-pyrroline-5-carboxylate
-
-
?
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(S)-2-amino-6-oxohexanoate + NAD+ + H2O
L-2-aminoadipate + NADH + H+
-
-
-
?
(S)-2-amino-6-oxohexanoate + NADP+ + H2O
L-2-aminoadipate + NADPH + H+
-
-
-
?
alpha-aminoadipate semialdehyde + NAD(P)+ + H2O
L-2-aminoadipate + NAD(P)H + H+
-
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O
L-2-aminoadipate + NAD(P)H + H+
-
-
-
?
L-2-aminoadipate-semialdehyde + NAD+
L-2-aminoadipate + NADH
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
additional information
?
-
-
the enzyme catalyzes both the activation of alpha-aminoadipic acid and its reduction to semialdehyde
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
key enzyme in the branched pathway for lysine and beta-lactam biosynthesis of filamentous fungi. Nitrate has a strong negative effect on enzyme formation
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
key enzyme in the branched pathway for lysine and beta-lactam biosynthesis of filamentous fungi. Nitrate has a strong negative effect on enzyme formation
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
-
-
-
?
L-2-aminoadipate-semialdehyde + NAD+
L-2-aminoadipate + NADH
-
degradative enzyme
-
?
L-2-aminoadipate-semialdehyde + NAD+
L-2-aminoadipate + NADH
-
mammalian degradation of hydroxy-L-lysine via phosphohydrolysine and 2-aminoadipic semialdehyde to 2-aminoadipic acid
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
-
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
in presence of ATP and Mg2+
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
sixth step of lysine biosynthesis
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
-
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
in presence of ATP and Mg2+
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
involved in lysine biosynthetic pathway
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
in presence of ATP and Mg2+
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
involved in lysine biosynthetic pathway
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
-
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
in presence of ATP and Mg2+
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
sixth step of lysine biosynthesis
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
sixth step of lysine biosynthesis
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
alpha-aminoadipate pathway for lysine biosynthesis
-
?
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Schmidt, H.; Bode, R.; Birnbaum D.
Inhibition of alpha-aminoadipate-semialdehyde dehydrogenase from Trichosporon adeninovorans by lysine and lysine analogues
FEMS Microbiol. Lett.
70
41-44
1990
Blastobotrys adeninivorans
brenda
Chang, Y.F.; Ghosh, P.; Rao, V.V.
L-pipecolic acid metabolism in human liver: L-alpha-aminoadipate delta-semialdehyde oxidoreductase
Biochim. Biophys. Acta
1038
300-305
1990
Homo sapiens
brenda
Samsonova, I.A.; Bttcher, F.; Werner, C.; Bode, R.
Auxotrophic mutants of the yeast Trichosporon adeninovorans
J. Basic Microbiol.
29
675-683
1989
Blastobotrys adeninivorans
brenda
Schmidt, H.; Bode, R.; Samsonova, I.A.; Birnbaum, D.
Isolation and characterization of alpha-aminoadipate-delta-semialdehyde overproducing mutants from yeasts
FEMS Microbiol. Lett.
60
201-204
1989
Meyerozyma guilliermondii, Candida maltosa
-
brenda
Storts, D.R.; Bhattacharjee, J.K.
Properties of revertants of lys2 and lys5 mutants as well as alpha-aminoadipate-semialdehyde dehydrogenase from Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
161
182-186
1989
Saccharomyces cerevisiae
brenda
Ye, Z.H.; Bhattacharjee, J.K.
Lysine biosynthesis pathway and biochemical blocks of lysine auxotrophs of Schizosaccharomyces pombe
J. Bacteriol.
170
5968-5970
1988
Schizosaccharomyces pombe
brenda
Eibel, H.; Philippsen, P.
Identification of the cloned S. cerevisiae LYS2 gene by an integrative transformation approach
Mol. Gen. Genet.
191
66-73
1983
Saccharomyces cerevisiae
brenda
Schmidt, H.; Bode, R.; Lindner, M.; Birnbaum, D.
Lysine biosynthesis in the yeast Candida maltosa: properties of some enzymes and regulation of the biosynthetic pathway
J. Basic Microbiol.
25
675-681
1985
Candida maltosa
-
brenda
Tsai, C.H.; Henderson, L.M.
Degradation of O-phosphohydroxylysine in rat liver. Purification and properties of 2-aminoadipic semialdehyde dehydrogenase
J. Biol. Chem.
249
5790-5792
1974
Rattus norvegicus
brenda
Rodwell, V.W.
delta1-piperideine-6-carboxylic acid and alpha-aminoadipic acid delta-semialdehyde
Methods Enzymol.
17B
188-199
1971
Pseudomonas putida
-
brenda
Calvert, A.F.; Rodwell, V.W.
Metabolism of pipecolic acid in a Pseudomonas species. 3. L-alpha-aminoadipate delta-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase
J. Biol. Chem.
241
409-414
1966
Pseudomonas sp.
brenda
Fleig, U.N.; Pridmore, R.D.; Philippsen, P.
Construction of LYS2 cartridges for use in genetic manipulations of Saccharomyces cerevisiae
Gene
46
237-245
1986
Saccharomyces cerevisiae
brenda
Barnes, D.A.; Thorner, J.
Genetic manipulation of Saccharomyces cerevisiae by use of the LYS2 Gene
Mol. Cell. Biol.
6
2828-2838
1986
Saccharomyces cerevisiae
brenda
Ford, R.A.; Bhattacharjee, J.K.
Molecular properties of the lys1+ gene and the regulation of.alpha-aminoadipate reductase in Schizosaccharomyces pombe
Curr. Genet.
28
131-137
1995
Saccharomyces cerevisiae, Schizosaccharomyces pombe
brenda
Suvarna, K.; Seah, L.; Bhattacherjee, V.; Bhattacharjee, J.K.
Molecular analysis of the LYS2 gene of Candida albicans: homology to peptide antibiotic synthetases and the regulation of the.alpha-aminoadipate reductase
Curr. Genet.
33
268-275
1998
Saccharomyces cerevisiae, Candida albicans
brenda
Casqueiro, J.; Gutierrez, S.; Banuelos, O.; Fierro, F.; Velasco, J.; Martin, J.F.
Characterization of the lys2 gene of Penicillium chrysogenum encoding.alpha-aminoadipic acid reductase
Mol. Gen. Genet.
259
549-556
1998
Penicillium chrysogenum
brenda
Ehmann, D.E.; Gehring, A.M.; Walsh, C.T.
Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5
Biochemistry
38
6171-6177
1999
Saccharomyces cerevisiae
brenda
Praphanphoj, V.; Sacksteder, K.A.; Gould, S.J.; Thomas, G.H.; Geraghty, M.T.
Identification of the.alpha-Aminoadipic Semialdehyde Dehydrogenase-Phosphopantetheinyl Transferase Gene, the Human Ortholog of the Yeast LYS5 Gene
Mol. Genet. Metab.
72
336-342
2001
Homo sapiens
brenda
Hijarrubia, M.J.; Aparicio, J.F.; Casqueiro, J.; Martin, J.F.
Characterization of the lys2 gene of Acremonium chrysogenum encoding a functional.alpha-aminoadipate activating and reducing enzyme
Mol. Gen. Genet.
264
755-762
2001
Acremonium chrysogenum
brenda
Guo, S.; Evans, S.A.; Wilkes, M.B.; Bhattacharjee, J.K.
Novel posttranslational activation of the LYS2-encoded.alpha-aminoadipate reductase for biosynthesis of lysine and site-directed mutational analysis of conserved amino acid residues in the activation domain of Candida albicans
J. Bacteriol.
183
7120-7125
2001
Candida albicans
brenda
Hijarrubia, M.J.; Aparicio, J.F.; Martin, J.F.
Nitrate regulation of alpha-aminoadipate reductase formation and lysine inhibition of its activity in Penicillium chrysogenum and Acremonium chrysogenum
Appl. Microbiol. Biotechnol.
59
270-277
2002
Acremonium chrysogenum, Penicillium chrysogenum
brenda
Hijarrubia, M.J.; Aparicio, J.F.; Martin, J.F.
Domain structure characterization of the multifunctional alpha-aminoadipate reductase from Penicillium chrysogenum by limited proteolysis. Activation of alpha-aminoadipate does not require the peptidyl carrier protein box or the reduction domain
J. Biol. Chem.
278
8250-8256
2003
Penicillium chrysogenum
brenda
Alberti, A.; Ferrero, I.; Lodi, T.
LYS2 gene and its mutation in Kluyveromyces lactis
Yeast
20
1171-1175
2003
Kluyveromyces lactis (Q8NJ21)
brenda
Guo, S.; Bhattacharjee, J.K.
Posttranslational activation, site-directed mutation and phylogenetic analyses of the lysine biosynthesis enzymes alpha-aminoadipate reductase Lys1p (AAR) and the phosphopantetheinyl transferase Lys7p (PPTase) from Schizosaccharomyces pombe
Yeast
21
1279-1288
2004
Schizosaccharomyces pombe
brenda
Wang, L.; Jil, C.; Xu, Y.; Xu, J.; Dai, J.; Wu, Q.; Wu, M.; Zou, X.; Sun, L.; Gu, S.; Xie, Y.; Mao, Y.
Cloning and characterization of a novel human homolog of mouse U26, a putative PQQ-dependent AAS dehydrogenase
Mol. Biol. Rep.
32
47-53
2005
Homo sapiens (Q4L235), Homo sapiens
brenda
Felton, L.M.; Anthony, C.
Biochemistry: role of PQQ as a mammalian enzyme cofactor?
Nature
433
E10
2005
Mammalia
brenda
Rucker, R.; Storms, D.; Sheets, A.; Tchaparian, E.; Fascetti, A.
Biochemistry: Is pyrroloquinoline quinone a vitamin?
Nature
433
E10-1
2005
Mus musculus, Rattus norvegicus
brenda
Marchitti, S.A.; Deitrich, R.A.; Vasiliou, V.
Neurotoxicity and metabolism of the catecholamine-derived 3,4-dihydroxyphenylacetaldehyde and 3,4-dihydroxyphenylglycolaldehyde: the role of aldehyde dehydrogenase
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