Any feedback?
No. of entries
Information on EC 1.2.1.31 - L-aminoadipate-semialdehyde dehydrogenase
for references in articles please use BRENDA:EC1.2.1.31
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.2 Acting on the aldehyde or oxo group of donors
1.2.1 With NAD+ or NADP+ as acceptor
1.2.1.31 L-aminoadipate-semialdehyde dehydrogenase
IUBMB Comments
(S)-2-amino-6-oxohexanoate undergoes a spontaneous dehydration forming the cyclic (S)-2,3,4,5-tetrahydropyridine-2-carboxylate, which serves as a substrate for the hydrogenation reaction.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.2.1.31
- epilepsy
- seizure
- pyridoxine
-
pyridoxine-dependent
-
beta-ars
-
pipecolic
-
alpha2-ars
-
antiepileptic
- phentolamine
-
folinic
- saccharopine
-
alpha-adrenoceptor
-
alpha2-adrenergic
-
seizure-free
-
lysine-restricted
-
rauwolscine
-
alpha1a-ar
- piperideine-6-carboxylate
-
alpha1a
- medicine
showSynonyms
aldh7a1, antiquitin, alpha-ar, aldehyde dehydrogenase 7a1, aasadh, alpha-aar, lys1p, alpha-aasa dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, alpha-aminoadipate-semialdehyde dehydrogenase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-aminoadipate semialdehyde dehydrogenase
-
-
-
-
2-aminoadipic 6-semialdehyde dehydrogenase
2-aminoadipic semialdehyde dehydrogenase
-
-
-
-
Aldh7a1
alpha-AAR
alpha-AASA dehydrogenase
alpha-aminoadipate-semialdehyde dehydrogenase
-
-
-
-
alpha-aminoadipic acid-delta-semialdehyde dehydrogenase
alpha-aminoadipic semialdehyde dehydrogenase
Alpha-AR
-
-
-
-
antiquitin
dehydrogenase, aminoadipate semialdehyde
-
-
-
-
L-alpha-aminoadipate delta-semialdehyde oxidoreductase
-
-
-
-
L-alpha-aminoadipate delta-semialdehyde:NAD oxidoreductase
-
-
-
-
L-alpha-aminoadipate delta-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase
-
-
-
-
L-aminoadipate-semialdehyde dehydrogenase
Nalpha-Z-L-AASA dehydrogenase
Nalpha-Z-L-AASA dehydrogenase
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-2-amino-6-oxohexanoate + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-lysine degradation XI
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-2-aminoadipate-6-semialdehyde:NAD(P)+ 6-oxidoreductase
(S)-2-amino-6-oxohexanoate undergoes a spontaneous dehydration forming the cyclic (S)-2,3,4,5-tetrahydropyridine-2-carboxylate, which serves as a substrate for the hydrogenation reaction.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9067-87-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-2-amino-6-oxohexanoate + NAD+ + H2O
L-2-aminoadipate + NADH + H+
Substrates: -
Products: -
Products: -
?
(S)-2-amino-6-oxohexanoate + NADP+ + H2O
L-2-aminoadipate + NADPH + H+
Substrates: -
Products: -
Products: -
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
Substrates: -
Products: -
Products: -
?
alpha-aminoadipate semialdehyde + NAD(P)+ + H2O
L-2-aminoadipate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
alpha-aminoadipate semialdehyde + NAD+ + H2O
alpha-aminoadipate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
alpha-aminoadipate semialdehyde + NADP+ + H2O
alpha-aminoadipate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O
L-2-aminoadipate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
L-alpha-aminoadipate + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde + NAD+ + H2O
Nalpha-benzyloxycarbonyl-L-aminoadipate + NADH + H+
S-carboxymethyl-L-cysteine + NADPH
?
-
Substrates: 5% of the activity with L-2-aminoadipate
Products: -
Products: -
?
(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NAD+ + H2O
L-2-aminoadipate + NADH
-
Substrates: -
Products: -
Products: -
ir
(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NAD+ + H2O
L-2-aminoadipate + NADH
-
Substrates: -
Products: -
Products: -
ir
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
-
Substrates: -
Products: -
Products: -
?
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
-
Substrates: -
Products: -
Products: -
?
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
Substrates: -
Products: -
Products: -
?
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
-
Substrates: -
Products: -
Products: -
?
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
-
Substrates: -
Products: -
Products: -
?
DELTA1-piperidine 6-carboxylate + NAD+ + H2O
L-alpha-aminoadipate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
DELTA1-piperidine 6-carboxylate + NAD+ + H2O
L-alpha-aminoadipate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: in presence of ATP + Mg2+
Products: -
Products: -
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: in presence of ATP + Mg2+
Products: -
Products: -
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: in presence of ATP + Mg2+
Products: -
Products: -
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: in presence of ATP + Mg2+
Products: high specificity for L-alpha-aminoadipate-semialdehyde
Products: high specificity for L-alpha-aminoadipate-semialdehyde
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: in presence of ATP + Mg2+
Products: -
Products: -
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: key enzyme in the branched pathway for lysine and beta-lactam biosynthesis of filamentous fungi. Nitrate has a strong negative effect on enzyme formation
Products: -
Products: -
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: key enzyme in the branched pathway for lysine and beta-lactam biosynthesis of filamentous fungi. Nitrate has a strong negative effect on enzyme formation
Products: -
Products: -
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: presence of ATP required
Products: -
Products: -
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: in presence of ATP
Products: -
Products: -
?
L-2-aminoadipate 6-semialdehyde + NAD+ + H2O
L-2-aminoadipate + NADH
-
Substrates: -
Products: -
Products: -
ir
L-2-aminoadipate 6-semialdehyde + NAD+ + H2O
L-2-aminoadipate + NADH
-
Substrates: -
Products: -
Products: -
ir
L-2-aminoadipate 6-semialdehyde + NAD+ + H2O
L-2-aminoadipate + NADH
-
Substrates: -
Products: -
Products: -
ir
L-2-aminoadipate 6-semialdehyde + NAD+ + H2O
L-2-aminoadipate + NADH
-
Substrates: -
Products: -
Products: -
?
L-2-aminoadipate-semialdehyde + NAD+
L-2-aminoadipate + NADH
-
Substrates: degradative enzyme
Products: -
Products: -
?
L-2-aminoadipate-semialdehyde + NAD+
L-2-aminoadipate + NADH
-
Substrates: mammalian degradation of hydroxy-L-lysine via phosphohydrolysine and 2-aminoadipic semialdehyde to 2-aminoadipic acid
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: in presence of ATP and Mg2+
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: sixth step of lysine biosynthesis
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: -
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: in presence of ATP and Mg2+
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: involved in lysine biosynthetic pathway
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: in presence of ATP and Mg2+
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: involved in lysine biosynthetic pathway
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: -
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: -
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: in presence of ATP and Mg2+
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: sixth step of lysine biosynthesis
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: sixth step of lysine biosynthesis
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: alpha-aminoadipate pathway for lysine biosynthesis
Products: -
Products: -
?
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde + NAD+ + H2O
Nalpha-benzyloxycarbonyl-L-aminoadipate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde + NAD+ + H2O
Nalpha-benzyloxycarbonyl-L-aminoadipate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes both the activation of alpha-aminoadipic acid and its reduction to semialdehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: glutamate delta-semialdehyde DELTA1-pyrroline-5-carboxylate
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-2-amino-6-oxohexanoate + NAD+ + H2O
L-2-aminoadipate + NADH + H+
Substrates: -
Products: -
Products: -
?
(S)-2-amino-6-oxohexanoate + NADP+ + H2O
L-2-aminoadipate + NADPH + H+
Substrates: -
Products: -
Products: -
?
alpha-aminoadipate semialdehyde + NAD(P)+ + H2O
L-2-aminoadipate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O
L-2-aminoadipate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes both the activation of alpha-aminoadipic acid and its reduction to semialdehyde
Products: -
Products: -
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: key enzyme in the branched pathway for lysine and beta-lactam biosynthesis of filamentous fungi. Nitrate has a strong negative effect on enzyme formation
Products: -
Products: -
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: key enzyme in the branched pathway for lysine and beta-lactam biosynthesis of filamentous fungi. Nitrate has a strong negative effect on enzyme formation
Products: -
Products: -
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
L-2-aminoadipate-semialdehyde + NAD+
L-2-aminoadipate + NADH
-
Substrates: degradative enzyme
Products: -
Products: -
?
L-2-aminoadipate-semialdehyde + NAD+
L-2-aminoadipate + NADH
-
Substrates: mammalian degradation of hydroxy-L-lysine via phosphohydrolysine and 2-aminoadipic semialdehyde to 2-aminoadipic acid
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: in presence of ATP and Mg2+
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: sixth step of lysine biosynthesis
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: -
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: in presence of ATP and Mg2+
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: involved in lysine biosynthetic pathway
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: in presence of ATP and Mg2+
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: involved in lysine biosynthetic pathway
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: -
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: -
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: in presence of ATP and Mg2+
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: sixth step of lysine biosynthesis
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: sixth step of lysine biosynthesis
Products: -
Products: -
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
Substrates: alpha-aminoadipate pathway for lysine biosynthesis
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
a variety of NAD+ analogues serve as electron acceptor: deamino-NAD+, NADP+, thionicotinamide-NAD+ and 3-acetylpyridine-NAD+
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
Mg2+
Mn2+
additional information
Mn2+
-
optimal concentration: 5 mM, 60% of the maximal activity attained with Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
delta-hydroxylysine
-
competitive with respect to alpha-aminoadipate, non-competitive with respect to both ATP and NADPH
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde
-
-
additional information
-
dehydrogenase activity is not inhibited by Nalpha-Z-L-lysine and Nalpha-benzyloxycarbonyl-L-aminoadipate at pH 5.0 or 7.0
-
carbonyl reagents
-
e.g.: hydroxylamine, KCN, in the presence of substrate
-
L-lysine
-
competitive with respect to alpha-aminoadipate, non-competitive with respect to both ATP and NADPH
S-(beta-aminoethyl)-L-cysteine
-
competitive with respect to alpha-aminoadipate, non-competitive with respect to both ATP and NADPH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.888
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde
-
at pH 5.0
1.34
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde
-
at pH 7.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.6
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde
-
at pH 7.0
50
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde
-
at pH 5.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0072
4.9
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
in 0.2 M Tris-glycine buffer containing 5 mM beta-mercaptoethanol, L-alpha-aminoadipate-semialdehyde reduction
8
-
Nalpha-benzyloxycarbonyl-L-aminoadipate production by cell reaction is optimum at pH 7.0, although the enzyme exhibits optimum activity at pH 8.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
pH 5: about 30% of activity maximum, pH 9: about 40% of activity maximum
6 - 9
-
pH 6: about 10% of activity maximum, pH 9: about 70% of activity maximum
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild-type strain ATCC 11550 and the improved cephalosporin producer strain C10, ATC 48272
-
-
brenda
wild-type strain NRRL 1951 and a low-penicillin-producing strain Wis 54-1255
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the activity peaks during growth-phase preceding the onset of antibiotic production, which coincides with a decrease in enzyme activity, and is lower in high cephalosporin-producing strains
brenda
-
the activity peaks during growth-phase preceding the onset of antibiotic production, which coincides with a decrease in enzyme activity, and is lower in high penicillin-producing strains
brenda
-
no difference in the activity of 2-aminoadipic 6-semialdehyde dehydrogenase activity between normal fed and pyrroloquinoline quinone-deprived animals
brenda
-
no difference in the activity of 2-aminoadipic 6-semialdehyde dehydrogenase activity between normal fed and pyrroloquinoline quinone-deprived animals
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
the catalytically active oligomer of ALDH7A1 is assembled on demand in response to cofactor availability
malfunction
-
alpha-AASA dehydrogenase deficiency results in the accumulation of pathognomonic alpha-aminoadipic semialdehyde (in cerebrospinal fluid, plasma and urine) and pipecolic acid (cerebrospinal fluid and plasma) in affected patients
malfunction
mutations in the ALDH7A1 gene can cause the autosomal recessive metabolic disease pyridoxine-dependent epilepsy (PDE), which is characterized by seizure activity within days of birth. Although PDE symptoms can be mitigated with high doses of pyridoxine (vitamin B6) and a lysine-restricted diet, many patients have long-lasting and untreatable cognitive disability. The molecular basis of PDE is thought to be due to a buildup of DELTA1-piperideine-6-carboxylate, the cyclic form of the aldehyde substrate of ALDH7A1
metabolism
human aldehyde dehydrogenase 7A1 (ALDH7A1) catalyzes the final step in lysine catabolism, the NAD+-dependent oxidation of alpha-aminoadipate semialdehyde to alpha-aminoadipate
Show AA Sequence and Transmembrane Helices (2415 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
155000
additional information
wild-type ALDH7A1 in the absence of any substrates is subjected to SEC-MALS-SAXS analysis using three nominal loading concentrations in the range of 2-8 mg/ml (18-72 microM by dimer Mr). Results of the MALS experiment show the average in-solution Mr increases from 134 kDa to 158 kDa with increasing protein load concentration, consistent with a concentration-dependent dimer-tetramer equilibrium. For reference, the dimer Mr is 111 kDa. Wild-type ALDH7A1 in the absence of any substrates is subjected to SEC-MALS-SAXS analysis using three nominal loading concentrations in the range of 2-8 mg/ml (18-72 microM by dimer Mr). Results of the MALS experiment show the average in-solution Mr increases from 134 kDa to 158 kDa with increasing protein load concentration, consistent with a concentration-dependent dimer-tetramer equilibrium
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
ALDH7A1 forms a dimer-of-dimers tetramer both in crystallo and in solution. NAD+-binding promotes assembly of the ALDH7A1 tetramer and enhances ALDH7A1 tetramerization at micromolar enzyme concentrations. The apoenzyme is mainly dimeric. NAD+-bound ALDH7A1 is predominantly tetrameric. The tetramer is the active form of the enzyme. The catalytically active oligomer of ALDH7A1 is assembled on demand in response to cofactor availability. The major peaks correspond to Mr of 110 kDa and 184 kDa, which are both below the theoretical Mr of the tetramer (222 kDa), consistent with an intermediate exchange regime in which free dimer exists in solution simultaneously with a dimer-tetramer equilibrium. The minor species at 2.7S (54 kDa) likely represents a monomer (theoretical Mr of 56 kDa)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
additional information
side-chain modification
-
the 150-kDa Lys2p is posttranslational modified in the presence of coenzyme A and Candida albicans lys2 mutant extract as a source of phosphopantetheinyl transferase
side-chain modification
-
the lys5 gene product is functionally active and can recognize apo-Lys2, transferring a 4'-phosphopantetheinyl moiety to the conserved serine residue in the peptidyl carrier domain of the protein
side-chain modification
-
Lys5 is a specific posttranslational modification catalyst, using coenzyme A as a cosubstrate to phosphopantetheinylate Ser880 of the Lys2 activating it for catalysis
additional information
-
specific amino acid residues, namely G882 and S884 of the Lys2p activation domain are required, the phosphopantetheinyl transferase is required for the activation of Lys2p and not for its alpha-aminoadipate reductase activity
additional information
-
homolog of the yeast Lys5 gene encodes alpha-aminoadipate dehydrogenase phosphopantetheinyl transferase activity, 26% identity and 44% similarity to the yeast counterpart
additional information
-
Lys5 demonstrates phosphopantetheinyl transferase activity toward the 14-kDa Lys2 peptidyl carrier protein fragment, with a Km of 0.001 mM and a turnover number of 3/min
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G874ade/874R/874K
-
lys arg double mutation in strain G874 isolated after a second induced mutagenesis in ade mutant G846
G983ade/983K
-
lys mutation in strain G983 isolated after a second induced mutagenesis in ade mutant G846, enzyme activity detectable
C125I
-
mutant enzyme shows no alpha-aminoadipate reductase activity
D126E
-
mutant enzyme shows no alpha-aminoadipate reductase activity
D94E
-
mutant enzyme shows no alpha-aminoadipate reductase activity
E173D
-
mutant enzyme shows no alpha-aminoadipate reductase activity
F93W
-
mutant enzyme shows no alpha-aminoadipate reductase activity
F95W
-
mutant enzyme shows no alpha-aminoadipate reductase activity
G124A
-
mutant enzyme shows no alpha-aminoadipate reductase activity
G79A
-
mutant enzyme shows no alpha-aminoadipate reductase activity
G910A
-
mutant enzyme shows no alpha-aminoadipate reductase activity
K172R
-
mutant enzyme shows no alpha-aminoadipate reductase activity
K177R
-
mutant enzyme shows no alpha-aminoadipate reductase activity
N96D
-
mutant enzyme shows no alpha-aminoadipate reductase activity
P81A
-
mutant enzyme shows no alpha-aminoadipate reductase activity
R80K
-
mutant enzyme shows no alpha-aminoadipate reductase activity
S913A
-
mutant enzyme shows no alpha-aminoadipate reductase activity
S913T
-
mutant enzyme shows no alpha-aminoadipate reductase activity
additional information
-
alpha-AASA dehydrogenase deficiency is characterised by increases of alpha-aminoadipic semialdehyde in urine, plasma and cerebrospinal fluid
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
activity is significantly decreased in acidic pH regions, yet the difference in activity is maximum at pH 5.0. The dehydrogenase is unstable in alkaline pH regions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
additional information
-
enzyme activity at 10°C is less than 10% of the maximum activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of 10 mM 2-mercaptoethanol and protease inhibitors e.g.: 5 mM EDTA, 1 mM phenylmethylsulfonyl fluoride to the crude extract improves stability
-
freezing-thawing, frozen enzyme loses 10-20% of activity during each freeze-thaw cycle
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.02 mM potassium phosphate buffer, pH 7.0, 5 mM 2-mercaptoethanol, 3 months
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial, using column chromatography on DEAE-cellulose, gel filtration, hydrolxylapatite and Reactive Red-120 agarose
-
using ammonium sulfate fractionation and column chromatography on CM-Sephadex
-
using protamine sulfate treatment, ammonium sulfate fractionation and treatment with calcium phosphate gel
using protamine sulfate treatment, ammonium sulfate fractionation and treatment with calcium phosphate gel
-
using protamine sulfate treatment, ammonium sulfate fractionation and treatment with calcium phosphate gel
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA is cloned from a human fetal library, library is constructed in a modified pBluescript II SK+ vector, cDNA insert is sequenced
cloning of lys2, the cloned gene encodes a functional alpha-aminoadipate reductase as shown by complementation of a Penicillium chrysogenum lys2 mutant, the aminoacid sequence shows strong homology with the alpha-aminoadipate reductase encoded by lys2 genes of Candida albicans, Schizosaccharomyces pombe, Saccharomyces cerevisiae and Penicillium chrysogenum
-
expression in Escherichia coli as an active enzyme. Exhibits significant alpha-aminoadipate reductase activity without the addition of CoA and Lys7p PPTase from Schizosaccharomyces pombe
-
LYS2 gene codes for alpha-aminoadipate reductase, construction and use of LYS2 cartridges
-
LYS2 gene codes for alpha-aminoadipate reductase, LYS2 genes encodes a protein with 49.9% identity to the Saccharomyces cerevisiae, 51.3% identity to the Schizosaccharomyces pombe and 48.12% identity to the Candida albicans alpha-aminoadipate reductases
-
LYS2 gene codes for alpha-aminoadipate reductase, LYS2 ORF exhibits 63% identity at the nucleotide level and 56.2% identity at the aminoacid level to the LYS2 gene of Saccharomyces cerevisiae
-
Lys5 and Lys2 cloned from Saccharomyces cerevisiae DNA, overexpressed in Escherichia coli, and purified, Lys5/Lys2 pair is a two component system in which Lys5 covalently primes Lys2, allowing alpha-aminoadipate reductase activity by holo-Lys2 with catalytic cycles of autoaminoacylation and reductive clevage
-
one-step homologous recombination in Saccharomyces cerevisiae, expression of the human gene in the yeast rescues the lys5 knockout phenotype
-
two genes, lys1+ and lys7+ are required for the synthesis of the enzyme, some regions of the enzyme sequence are similar to the sequence of Saccharomyces cerevisiae, e.g. Schizosaccharomyces pombe enzyme residues 345 through 385, and 449 through 470
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increased intracellular free lysine induces the transcriptional upregulation of the enzyme gene
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
alpha-AASA dehydrogenase deficiency results in pyridoxine dependent epilepsy. Patients show pathogenic mutations in the ALDH7A1 gene. Increase of alpha-AASA in urine of patients with alpha-AASA dehydrogenase deficiency makes this biomarker preferable towards the measurement of pipecolic acid, which shows non-specificity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Candida maltosa, Meyerozyma guilliermondii
-
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
Candida albicans, Saccharomyces cerevisiae
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
Hapsidospora chrysogena
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
Hapsidospora chrysogena, 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
Pharmacol. Rev.
59
125-150
2007
Homo sapiens (P49419)
brenda
Alnouti, Y.; Klaassen, C.D.
Tissue distribution, ontogeny, and regulation of aldehyde dehydrogenase (Aldh) enzymes mRNA by prototypical microsomal enzyme inducers in mice
Toxicol. Sci.
101
51-64
2008
Mus musculus (Q9DBF1)
brenda
Isobe, K.; Fukuda, N.; Nagasawa, S.
Analysis of selective production of Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde and Nalpha-benzyloxycarbonyl-L-aminoadipic acid by Rhodococcus sp. AIU Z-35-1
J. Biosci. Bioeng.
105
152-156
2008
Rhodococcus sp. (in: high G+C Gram-positive bacteria), Rhodococcus sp. (in: high G+C Gram-positive bacteria) AIU Z-35-1
brenda
Struys, E.A; Jakobs, C.
Alpha-aminoadipic semialdehyde is the biomarker for pyridoxine dependent epilepsy caused by alpha-aminoadipic semialdehyde dehydrogenase deficiency
Mol. Genet. Metab.
91
405
2007
Homo sapiens
brenda
Struys, E.A.; Jakobs, C.
Metabolism of lysine in alpha-aminoadipic semialdehyde dehydrogenase-deficient fibroblasts: evidence for an alternative pathway of pipecolic acid formation
FEBS Lett.
584
181-186
2010
Homo sapiens
brenda
Korasick, D.A.; White, T.A.; Chakravarthy, S.; Tanner, J.J.
NAD+ promotes assembly of the active tetramer of aldehyde dehydrogenase 7A1
FEBS Lett.
592
3229-3238
2018
Homo sapiens (P49419)
brenda
Arruda, P.; Barreto, P.
Lysine catabolism through the saccharopine pathway enzymes and intermediates involved in plant responses to abiotic and biotic stress
Front. Plant Sci.
11
587
2020
Arabidopsis thaliana
brenda
Coughlin, C.R.; Tseng, L.A.; Abdenur, J.E.; Ashmore, C.; Boemer, F.; Bok, L.A.; Boyer, M.; Buhas, D.; Clayton, P.T.; Das, A.; Dekker, H.; Evangeliou, A.; Feillet, F.; Footitt, E.J.; Gospe, S.M.; Hartmann, H.; Kara, M.; Kristensen, E.; Lee, J.; Lilje, R.; Longo, N.; Lunsing, R.J.; Mills, P.; Papadopoulou, M.T.
Consensus guidelines for the diagnosis and management of pyridoxine-dependent epilepsy due to alpha-aminoadipic semialdehyde dehydrogenase deficiency
J. Inherit. Metab. Dis.
44
178-192
2021
Homo sapiens (P49419)
brenda
EXTERNAL LINKS (specific for EC-Number 1.2.1.31)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
