Information on EC 1.2.1.31 - L-aminoadipate-semialdehyde dehydrogenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.2.1.31
-
RECOMMENDED NAME
GeneOntology No.
L-aminoadipate-semialdehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(S)-2-amino-6-oxohexanoate + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
Q4L235
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reduction
Q4L235
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Lysine biosynthesis
-
Lysine degradation
-
lysine degradation II
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
L-2-aminoadipate-6-semialdehyde:NAD(P)+ 6-oxidoreductase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-aminoadipate semialdehyde dehydrogenase
-
-
-
-
2-aminoadipic 6-semialdehyde dehydrogenase
Q4L235
-
2-aminoadipic 6-semialdehyde dehydrogenase
-
-
2-aminoadipic semialdehyde dehydrogenase
-
-
-
-
AAR
Saccharomycopsis fibuligera PD70
Q1W284
-
-
adipic 6-semialdehyde dehydrogenase
-
-
Aldh7a1
P49419
-
Aldh7a1
Q9DBF1
isozyme
alpha-AASA dehydrogenase
-
-
alpha-aminoadipate reductase
-
-
-
-
alpha-aminoadipate reductase
-
-
alpha-aminoadipate reductase
Q1W284
-
alpha-aminoadipate reductase
Saccharomycopsis fibuligera PD70
Q1W284
-
-
alpha-aminoadipate reductase Lys1p
-
-
alpha-aminoadipate-semialdehyde dehydrogenase
-
-
-
-
alpha-aminoadipic acid-delta-semialdehyde dehydrogenase
-
-
alpha-aminoadipic semialdehyde dehydrogenase
-
-
Alpha-AR
-
-
-
-
antiquitin
-
-
dehydrogenase, aminoadipate semialdehyde
-
-
-
-
human U26
Q4L235
-
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
Q4L235
-
L-aminoadipate-semialdehyde dehydrogenase
-
-
L-aminoadipate-semialdehyde dehydrogenase
-
-
Nalpha-Z-L-AASA dehydrogenase
-
-
Nalpha-Z-L-AASA dehydrogenase
Rhodococcus sp. AIU Z-35-1
-
-
-
U26
Q4L235
-
CAS REGISTRY NUMBER
COMMENTARY
9067-87-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
wild-type strain ATCC 11550 and the improved cephalosporin producer strain C10, ATC 48272
-
-
Manually annotated by BRENDA team
PAR-4 wild type and lys mutants
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
wild-type strain NRRL 1951 and a low-penicillin-producing strain Wis 54-1255
-
-
Manually annotated by BRENDA team
strain AIU Z-35-1
-
-
Manually annotated by BRENDA team
Rhodococcus sp. AIU Z-35-1
strain AIU Z-35-1
-
-
Manually annotated by BRENDA team
Saccharomycopsis fibuligera PD70
strain PD70
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
Q9DBF1
-
-
-
?
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
show the reaction diagram
-
-
-
-
-
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
show the reaction diagram
-
-
-
-
-
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
show the reaction diagram
-
-
-
-
-
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
show the reaction diagram
-
-
-
-
-
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
show the reaction diagram
P49419
-
-
-
?
alpha-aminoadipic semialdehyde + NAD+ + H2O
alpha-aminoadipic acid + NADH + H+
show the reaction diagram
Candida maltosa L4
-
-
-
-
-
DELTA1-piperidine 6-carboxylate + NAD+ + H2O
L-2-aminoadipate + NADH
show the reaction diagram
-
-
-
ir
DELTA1-piperidine 6-carboxylate + NAD+ + H2O
L-2-aminoadipate + NADH
show the reaction diagram
-
-
-
ir
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
-
-
-
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
-
-
-
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
-
in presence of ATP + Mg2+
-
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
-
in presence of ATP + Mg2+
-
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
-
in presence of ATP + Mg2+
-
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
-
in presence of ATP + Mg2+
-
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
-
in presence of ATP + Mg2+
high specificity for L-alpha-aminoadipate-semialdehyde
?
L-2-aminoadipate + NADPH
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
Candida maltosa L4
-
in presence of ATP + Mg2+
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
in presence of ATP
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
Q12572
presence of ATP and Mg2+ required
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
-
presence of ATP required
-
-
?
L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O
L-2-aminoadipate + NAD(P)H + H+
show the reaction diagram
Q4L235
-
-
-
-
L-2-aminoadipate 6-semialdehyde + NAD+ + H2O
L-2-aminoadipate + NADH
show the reaction diagram
-
-
-
ir
L-2-aminoadipate 6-semialdehyde + NAD+ + H2O
L-2-aminoadipate + NADH
show the reaction diagram
-
-
-
?
L-2-aminoadipate 6-semialdehyde + NAD+ + H2O
L-2-aminoadipate + NADH
show the reaction diagram
-
-
-
ir
L-2-aminoadipate 6-semialdehyde + NAD+ + H2O
L-2-aminoadipate + NADH
show the reaction diagram
-
-
-
ir
L-2-aminoadipate-semialdehyde + NAD+
L-2-aminoadipate + NADH
show the reaction diagram
-
degradative enzyme
-
?
L-2-aminoadipate-semialdehyde + NAD+
L-2-aminoadipate + NADH
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
in presence of ATP and Mg2+
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
in presence of ATP and Mg2+
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
in presence of ATP and Mg2+
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
sixth step of lysine biosynthesis
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
sixth step of lysine biosynthesis
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
sixth step of lysine biosynthesis
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
alpha-aminoadipate pathway for lysine biosynthesis
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
involved in lysine biosynthetic pathway
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
Candida maltosa L4
-
in presence of ATP and Mg2+, involved in lysine biosynthetic pathway
-
?
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde + NAD+ + H2O
Nalpha-benzyloxycarbonyl-L-aminoadipate + NADH + H+
show the reaction diagram
Rhodococcus sp., Rhodococcus sp. AIU Z-35-1
-
-
-
-
?
S-carboxymethyl-L-cysteine + NADPH
?
show the reaction diagram
-
5% of the activity with L-2-aminoadipate
-
-
?
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
L-alpha-aminoadipate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
not: glutamate delta-semialdehyde DELTA1-pyrroline-5-carboxylate
-
-
-
additional information
?
-
-
the enzyme catalyzes both the activation of alpha-aminoadipic acid and its reduction to semialdehyde
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-2-aminoadipate + NADPH + H+
L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
show the reaction diagram
-
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 6-semialdehyde + NAD(P)+ + H2O
L-2-aminoadipate + NAD(P)H + H+
show the reaction diagram
Q4L235
-
-
-
-
L-2-aminoadipate-semialdehyde + NAD+
L-2-aminoadipate + NADH
show the reaction diagram
-
degradative enzyme
-
?
L-2-aminoadipate-semialdehyde + NAD+
L-2-aminoadipate + NADH
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
in presence of ATP and Mg2+
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
in presence of ATP and Mg2+
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
in presence of ATP and Mg2+
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
sixth step of lysine biosynthesis
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
sixth step of lysine biosynthesis
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
sixth step of lysine biosynthesis
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
alpha-aminoadipate pathway for lysine biosynthesis
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
-
involved in lysine biosynthetic pathway
-
?
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
Candida maltosa L4
-
in presence of ATP and Mg2+, involved in lysine biosynthetic pathway
-
?
additional information
?
-
-
the enzyme catalyzes both the activation of alpha-aminoadipic acid and its reduction to semialdehyde
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
P49419
required
NAD+
Q9DBF1
-
NADH
-
can replace NADPH with lower activity and higher Km
NADH
-
reaction not observed
pyrroloquinoline quinone
Q4L235
PQQ
pyrroloquinoline quinone
-
PQQ, in discussion
pyrroloquinoline quinone
-
PQQ, in discussion
additional information
-
a variety of NAD+ analogues serve as electron acceptor: deamino-NAD+, NADP+, thionicotinamide-NAD+ and 3-acetylpyridine-NAD+
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
stimulates
Cu2+
-
stimulates
Cu2+
-
inhibits
Mg2+
-
required for activity
Mg2+
-
stimulates
Mg2+
-
required for activity
Mg2+
-
required for activity; stimulates
Mg2+
-
absolue requiremnt, optimal concentration: 10 mM
MgCl2
Q12572
required
Mn2+
-
stimulates
Mn2+
-
stimulates
Mn2+
-
optimal concentration: 5 mM, 60% of the maximal activity attained with Mg2+
additional information
-
no metal cofactor required
additional information
-
no metal cofactor required
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acetaldehyde
-
-
alpha-aminoadipate
-
-
alpha-aminoadipate
Q1W284
inhibitory effect can be reversed by adding methionine
ATP
-
30% inhibition at 1 mM
ATP
-
30% inhibition at 1 mM
Butyraldehyde
-
-
Carbonyl reagents
-
e.g.: hydroxylamine, KCN, in the presence of substrate
-
Carbonyl reagents
-
e.g.: hydroxylamine, KCN, in the presence of substrate
-
delta-hydroxylysine
-
competitive with respect to alpha-aminoadipate, non-competitive with respect to both ATP and NADPH
Disulfiram
P49419
0.01 mM
EDTA
-
no inhibition observed
EDTA
-
5 mM, 75% inhibition
Fe2+
-
-
-
glutamate
-
competitive inhibitor with respect to alpha-aminoadipate
HSO3-
-
in presence of substrate
HSO3-
-
in presence of substrate
hydroxylamine
-
in presence of substrate
hydroxylamine
-
in presence of substrate
imidazole
-
20% inhibition at 1 mM
KCN
-
strongly inhibits, 75% inhibition
KCN
-
in presence of substrate
L-aspartate
-
competitive inhibitor with respect to alpha-aminoadipate
L-lysine
-
competitive with respect to alpha-aminoadipate, non-competitive with respect to both ATP and NADPH
L-lysine
-
20% inhibition at 50 mM
L-lysine
-
54% inhibition at 1 mM and 80% inhibition at 4 mM
L-lysine
-
70% inhibition at 50 mM
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde
-
-
S-(beta-aminoethyl)-L-cysteine
-
competitive with respect to alpha-aminoadipate, non-competitive with respect to both ATP and NADPH
S-(beta-aminoethyl)-L-cysteine
-
92% inhibition at 1 mM
Sodium diphosphate
-
-
additional information
-
dehydrogenase activity is not inhibited by Nalpha-Z-L-lysine and Nalpha-benzyloxycarbonyl-L-aminoadipate at pH 5.0 or 7.0
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
10 mM, activates
ATP
-
presence of ATP required
dithiothreitol
-
10 mM, activates
L-cysteine
-
10 mM, activates
additional information
Q1W284
growth on medium containing lysine as the sole nitrogen source
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.02
-
2-aminoadipic semialdehyde
-
-
0.2
-
alpha-aminoadipate
-
-
0.2
-
alpha-aminoadipate
-
NAD+
0.78
-
alpha-aminoadipate
-
-
1.3
-
ATP
-
pH 8, 30C
0.002
-
DELTA1-piperidine 6-carboxylate
-
-
0.002
-
DELTA1-piperidine 6-carboxylate
-
-
1.4
-
L-2-Aminoadipate
-
pH 8, 30C
0.181
-
L-2-aminoadipate 6-semialdehyde
-
-
3.8
-
MgCl2
-
-
0.454
-
NAD+
-
-
0.38
-
NADH
-
-
0.1
-
NADPH
-
-
0.16
-
NADPH
-
pH 8, 30C
0.62
-
NADPH
-
of Lys2
0.888
-
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde
-
at pH 5.0
1.34
-
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde
-
at pH 7.0
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
11.2
-
alpha-aminoadipate semialdehyde
-
production from holo-lys2
66
-
L-2-Aminoadipate
-
pH 8, 30C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.65
-
delta-hydroxylysine
-
-
4.2
-
L-aspartate
-
-
1.5
-
L-glutamate
-
-
8.6
-
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde
-
at pH 7.0
50
-
Nalpha-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde
-
at pH 5.0
0.007
-
S-(beta-aminoethyl)-L-cysteine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00077
-
-
cytosol fraction
0.0063
-
-
5 mM L-lysine as supplement during growth of the enzyme
0.0072
-
-
-
0.0072
-
-
no supplement added during growth of the enzyme
0.00996
-
-
wild type
0.0102
-
-
lysine auxotropic mutant G16
0.0105
-
-
lysine auxotropic mutant G12
0.0108
-
-
lysine auxotropic mutants G108 and G358
0.0114
-
-
lysine auxotropic mutant G285
0.0138
-
-
10 mM amitrole as supplement during growth of the enzyme
1.44
-
-
-
4.9
-
-
after purification, gel fraction
4.9
-
-
after purification, gel fraction
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7.5
-
-
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
8.1
-
-
L-alpha-aminoadipate-semialdehyde reduction
8.2
-
-
L-alpha-aminoadipate-semialdehyde reduction
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
highest expression
Manually annotated by BRENDA team
Q4L235
; fetal brain cDNA library; mRNA expression
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Q4L235
; mRNA expression
Manually annotated by BRENDA team
Q4L235
colon adenocarcinoma, CX-1; colon adenocarcinoma, GI-112
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
Q4L235
; mRNA expression
Manually annotated by BRENDA team
Q4L235
; high mRNA expression
Manually annotated by BRENDA team
-
peripheral blood
Manually annotated by BRENDA team
Q4L235
peripheral blood leukocyte
Manually annotated by BRENDA team
Q4L235
; high mRNA expression
Manually annotated by BRENDA team
-
; no difference in the activity of 2-aminoadipic 6-semialdehyde dehydrogenase activity between normal fed and pyrroloquinoline quinone-deprived animals
Manually annotated by BRENDA team
Q9DBF1
isozyme Aldh8a1 mRNA expression is highest in liver
Manually annotated by BRENDA team
Q4L235
; mRNA expression
Manually annotated by BRENDA team
Q4L235
lung carcinoma, GI-117; lung carcinoma, LX-1
Manually annotated by BRENDA team
Q4L235
; mRNA expression
Manually annotated by BRENDA team
Q4L235
ovarian carcinoma, GI-102
Manually annotated by BRENDA team
Q4L235
; high mRNA expression
Manually annotated by BRENDA team
Q4L235
mRNA expression
Manually annotated by BRENDA team
Q4L235
; mRNA expression
Manually annotated by BRENDA team
Q4L235
prostatic adenocarcinoma, PC3
Manually annotated by BRENDA team
Q4L235
mRNA expression
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
Q4L235
low mRNA expression
Manually annotated by BRENDA team
Q4L235
; mRNA expression
Manually annotated by BRENDA team
Q4L235
; high mRNA expression
Manually annotated by BRENDA team
Q4L235
; high mRNA expression
Manually annotated by BRENDA team
Q4L235
; mRNA expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
31000
-
-
Lys5 from induced E. coli cells
154900
-
-
analysis of the nucleotide sequence of the 5.1-kb region
155000
-
-
full-length Lys2 from induced E. coli cells
160000
-
-
gel filtration
171000
-
-
gel filtration
180000
-
-
gel filtration
250000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
-
1 * 155000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
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
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
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
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
-70
-
-
unstable
-20
-
-
unstable
4
-
-
1 h, stable
30
-
-
1 h, 20% loss of activity
37
-
-
15 min, 50% loss of activity
additional information
-
-
enzyme activity at 10C is less than 10% of the maximum activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
freezing-thawing, frozen enzyme loses 10-20% of activity during each freeze-thaw cycle
-
lyophilization inactivates
-
addition of 10 mM 2-mercaptoethanol and protease inhibitors e.g.: 5 mM EDTA, 1 mM phenylmethylsulfonyl fluoride to the crude extract improves stability
-
low ionic strength: unstable
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 0.02 mM potassium phosphate buffer, pH 7.0, 5 mM 2-mercaptoethanol, 3 months
-
-20C, 50% v/v glycerol, rapid loss of activity
-
0C, 50% loss of activity, 24 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
using DEAE-cellulose column chromatography
-
using column chromatography on Sephadex G-25 and Sephadex G-200
-
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 ammonium sulfate fractionation and column chromatography on CM-Sephadex
-
partial, using column chromatography on DEAE-cellulose, gel filtration, hydrolxylapatite and Reactive Red-120 agarose
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
heterlogous expressed in Escherichia coli
-
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
-
mutant enzymes expressed in Escherichia coli BL21
Q12572
cDNA is cloned from a human fetal library, library is constructed in a modified pBluescript II SK+ vector, cDNA insert is sequenced
Q4L235
one-step homologous recombination in Saccharomyces cerevisiae, expression of the human gene in the yeast rescues the lys5 knockout phenotype
-
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
-
cloning of the LYS2 gene
-
encoded by two different genes, LYS2 and LYS5
-
LYS2 gene cloned
-
LYS2 gene codes for alpha-aminoadipate reductase, construction and use of LYS2 cartridges
-
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
-
expression of the ORF of the Saccharomycopsis fibuligera alpha-aminoadipate reductase gene (LYS2) in a lys2- strain of Saccharomyces cerevisiae
Q1W284
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
-
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
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
G848K
-
enzyme activity not detectable
G874ade/874R/874K
-
lys arg double mutation in strain G874 isolated after a second induced mutagenesis in ade mutant G846
G905K
-
enzyme activity detectable
G982K
-
enzyme activity detectable
G983ade/983K
-
lys mutation in strain G983 isolated after a second induced mutagenesis in ade mutant G846, enzyme activity detectable
G984K
-
very low activity
G985K
-
enzyme activity not detectable
A459G
Q12572
106% of the alpha-aminoadipate reductase activity of wild-type enzyme
A475G
Q12572
109% of the alpha-aminoadipate reductase activity of wild-type enzyme
A979G
Q12572
94% of the alpha-aminoadipate reductase activity of wild-type enzyme
D461E
Q12572
4% of the alpha-aminoadipate reductase activity of wild-type enzyme
D461N
Q12572
no alpha-aminoadipate reductase activity
D466E
Q12572
15% of the alpha-aminoadipate reductase activity of wild-type enzyme
E420T
Q12572
101% of the alpha-aminoadipate reductase activity of wild-type enzyme
F415Y
Q12572
71% of the alpha-aminoadipate reductase activity of wild-type enzyme
F452L
Q12572
6% of the alpha-aminoadipate reductase activity of wild-type enzyme
F452V
Q12572
45% of the alpha-aminoadipate reductase activity of wild-type enzyme
F468L
Q12572
96% of the alpha-aminoadipate reductase activity of wild-type enzyme
F982L
Q12572
4% of the alpha-aminoadipate reductase activity of wild-type enzyme
F982V
Q12572
no alpha-aminoadipate reductase activity
G418A
Q12572
31% of the alpha-aminoadipate reductase activity of wild-type enzyme
G418V
Q12572
no alpha-aminoadipate reductase activity
G421A
Q12572
75% of the alpha-aminoadipate reductase activity of wild-type enzyme
G425A
Q12572
99% of the alpha-aminoadipate reductase activity of wild-type enzyme
G474A
Q12572
41% of the alpha-aminoadipate reductase activity of wild-type enzyme
G978A
Q12572
2% of the alpha-aminoadipate reductase activity of wild-type enzyme
G978S
Q12572
no alpha-aminoadipate reductase activity
G981A
Q12572
no alpha-aminoadipate reductase activity
G981V
Q12572
no alpha-aminoadipate reductase activity
G984A
Q12572
3% of the alpha-aminoadipate reductase activity of wild-type enzyme
G984S
Q12572
no alpha-aminoadipate reductase activity
H460R
Q12572
no alpha-aminoadipate reductase activity
I422V
Q12572
92% of the alpha-aminoadipate reductase activity of wild-type enzyme
I463L
Q12572
no alpha-aminoadipate reductase activity
I987V
Q12572
92% of the alpha-aminoadipate reductase activity of wild-type enzyme
K424R
Q12572
26% of the alpha-aminoadipate reductase activity of wild-type enzyme
K424T
Q12572
3% of the alpha-aminoadipate reductase activity of wild-type enzyme
K451Q
Q12572
58% of the alpha-aminoadipate reductase activity of wild-type enzyme
K451R
Q12572
no alpha-aminoadipate reductase activity
K535Q
Q12572
94% of the alpha-aminoadipate reductase activity of wild-type enzyme
L446I
Q12572
71% of the alpha-aminoadipate reductase activity of wild-type enzyme
L471V
Q12572
89% of the alpha-aminoadipate reductase activity of wild-type enzyme
L983V
Q12572
31% of the alpha-aminoadipate reductase activity of wild-type enzyme
M440L
Q12572
99% of the alpha-aminoadipate reductase activity of wild-type enzyme
P423V
Q12572
51% of the alpha-aminoadipate reductase activity of wild-type enzyme
P462A
Q12572
2% of the alpha-aminoadipate reductase activity of wild-type enzyme
P462S
Q12572
no alpha-aminoadipate reductase activity
Q464E
Q12572
17% of the alpha-aminoadipate reductase activity of wild-type enzyme
Q511E
Q12572
31% of the alpha-aminoadipate reductase activity of wild-type enzyme
Q511L
Q12572
129% of the alpha-aminoadipate reductase activity of wild-type enzyme
R465K
Q12572
2% of the alpha-aminoadipate reductase activity of wild-type enzyme
R465S
Q12572
no alpha-aminoadipate reductase activity
S417A
Q12572
10% of the alpha-aminoadipate reductase activity of wild-type enzyme
S417T
Q12572
82% of the alpha-aminoadipate reductase activity of wild-type enzyme
S419A
Q12572
16% of the alpha-aminoadipate reductase activity of wild-type enzyme
S419T
Q12572
no alpha-aminoadipate reductase activity
S456T
Q12572
59% of the alpha-aminoadipate reductase activity of wild-type enzyme
S985A
Q12572
85% of the alpha-aminoadipate reductase activity of wild-type enzyme
T416A
Q12572
no alpha-aminoadipate reductase activity
T416S
Q12572
35% of the alpha-aminoadipate reductase activity of wild-type enzyme
T469S
Q12572
80% of the alpha-aminoadipate reductase activity of wild-type enzyme
T506A
Q12572
49% of the alpha-aminoadipate reductase activity of wild-type enzyme
T506S
Q12572
no alpha-aminoadipate reductase activity
T534A
Q12572
103% of the alpha-aminoadipate reductase activity of wild-type enzyme
T977S
Q12572
70% of the alpha-aminoadipate reductase activity of wild-type enzyme
T980S
Q12572
28% of the alpha-aminoadipate reductase activity of wild-type enzyme
V426L
Q12572
64% of the alpha-aminoadipate reductase activity of wild-type enzyme
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
V529I
Q12572
117% of the alpha-aminoadipate reductase activity of wild-type enzyme
additional information
-
alpha-AASA dehydrogenase deficiency is characterised by increases of alpha-aminoadipic semialdehyde in urine, plasma and cerebrospinal fluid
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
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
additional information
Q1W284
the sequence of the Saccharomycopsis fibuligera alpha-aminoadipate reductase gene Lys2p has the highest identity of 53% with the AAR of Candida albicans SC5314 and an identity of 51% with that of Saccharomyces cerevisiae. Expression of the ORF of SfLYS2 in a lys2- strain of Saccharomyces cerevisiae can functionally complement the lysine mutant of the Saccharomyces cerevisiae strain. Cloning of SfLYS2 may provide a general tool in developing genetics-based studies not only with Saccharomycopsis fibuligera but also with Saccharomyces cerevisiae
additional information
Saccharomycopsis fibuligera PD70
-
the sequence of the Saccharomycopsis fibuligera alpha-aminoadipate reductase gene Lys2p has the highest identity of 53% with the AAR of Candida albicans SC5314 and an identity of 51% with that of Saccharomyces cerevisiae. Expression of the ORF of SfLYS2 in a lys2- strain of Saccharomyces cerevisiae can functionally complement the lysine mutant of the Saccharomyces cerevisiae strain. Cloning of SfLYS2 may provide a general tool in developing genetics-based studies not only with Saccharomycopsis fibuligera but also with Saccharomyces cerevisiae
-