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(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
L-2-aminoadipate + NADPH + H+ + ATP
Substrates: presence of ATP and Mg2+ required
Products: -
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adipate + NADPH + H+ + ATP
adipate semialdehyde + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
D-2-aminoadipate + NADPH + H+ + ATP
(R)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
L-2-aminoadipate + NADPH + H+ + ATP
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
S-carboxymethyl-L-cysteine + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
-
Substrates: 20fold lower activity than with L-2-aminoadipate
Products: -
?
S-carboxymethyl-L-cysteine + NADPH + H+ + ATP
S-formylmethyl-L-cysteine + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
additional information
?
-
L-2-aminoadipate + NADPH + H+ + ATP
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
L-2-aminoadipate + NADPH + H+ + ATP
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
L-2-aminoadipate + NADPH + H+ + ATP
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
L-2-aminoadipate + NADPH + H+ + ATP
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
Substrates: -
Products: -
?
L-2-aminoadipate + NADPH + H+ + ATP
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: in strains Q176, D6/1014/A, and P2, the enzyme exhibits decreasing affinity for alpha-aminoadipate with increasing capacity of the respective strain to produce penicillin
Products: -
?
additional information
?
-
-
Substrates: no substrates: adipic acid, DL-diaminopimelic acid, L-glutamate
Products: -
?
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metabolism
the enzyme is involved in the fungal de novo L-lysine biosynthesis via ATP- and NADPH-dependent reduction of the intermediate L-alpha-aminoadipic acid into L-alpha-aminoadipate 6-semialdehyde as a multifunctional aminoacyl-adenylate-forming reductase, pathway overview
physiological function
L-alpha-aminoadipic acid reductases catalyze the ATP- and NADPH-dependent reduction of L-alpha-aminoadipic acid to the corresponding 6-semialdehyde during fungal L-lysine biosynthesis
additional information
the enzyme has a multidomain composition but features a unique domain of elusive function, termed the adenylation activating (ADA) domain, that extends the reductase N-terminally. The activity of alpha-aminoadipate reductase and A domain depends on the N-terminally extending domain. ADA domain sequence comparison and protein interaction analysis, homology modeling, overview
malfunction
enzyme-deficient mutants are defective in the biosynthesis of all known polyketides and nonribosomal peptides and hypersensitive to both iron depletion and oxidative stress. Enzyme disruption reduces germination speed on insect cuticles and results in significant loss of virulence. Enzyme inactivation slightly reduces mycelium hydrophobicity and has no significant effect on conidium hydrophobicity
malfunction
-
enzyme-deficient mutants are defective in the biosynthesis of all known polyketides and nonribosomal peptides and hypersensitive to both iron depletion and oxidative stress. Enzyme disruption reduces germination speed on insect cuticles and results in significant loss of virulence. Enzyme inactivation slightly reduces mycelium hydrophobicity and has no significant effect on conidium hydrophobicity
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A459G
106% of the alpha-aminoadipate reductase activity of wild-type enzyme
A475G
109% of the alpha-aminoadipate reductase activity of wild-type enzyme
A979G
94% of the alpha-aminoadipate reductase activity of wild-type enzyme
D461E
4% of the alpha-aminoadipate reductase activity of wild-type enzyme
D461N
no alpha-aminoadipate reductase activity
D466E
15% of the alpha-aminoadipate reductase activity of wild-type enzyme
E420T
101% of the alpha-aminoadipate reductase activity of wild-type enzyme
F415Y
71% of the alpha-aminoadipate reductase activity of wild-type enzyme
F452L
6% of the alpha-aminoadipate reductase activity of wild-type enzyme
F452V
45% of the alpha-aminoadipate reductase activity of wild-type enzyme
F468L
96% of the alpha-aminoadipate reductase activity of wild-type enzyme
F982L
4% of the alpha-aminoadipate reductase activity of wild-type enzyme
F982V
no alpha-aminoadipate reductase activity
G418A
31% of the alpha-aminoadipate reductase activity of wild-type enzyme
G418V
no alpha-aminoadipate reductase activity
G421A
75% of the alpha-aminoadipate reductase activity of wild-type enzyme
G425A
99% of the alpha-aminoadipate reductase activity of wild-type enzyme
G474A
41% of the alpha-aminoadipate reductase activity of wild-type enzyme
G881E
conserved residue in the posttranslational activation domain LGGHSI, less than 50% of wild-type activity
G882R
conserved residue in the posttranslational activation domain LGGHSI, loss of activity
G882S
conserved residue in the posttranslational activation domain LGGHSI, loss of activity
G978A
2% of the alpha-aminoadipate reductase activity of wild-type enzyme
G978S
no alpha-aminoadipate reductase activity
G981A
no alpha-aminoadipate reductase activity
G981V
no alpha-aminoadipate reductase activity
G984A
3% of the alpha-aminoadipate reductase activity of wild-type enzyme
G984S
no alpha-aminoadipate reductase activity
H460R
no alpha-aminoadipate reductase activity
H883R
conserved residue in the posttranslational activation domain LGGHSI, strong reduction of activity
I422V
92% of the alpha-aminoadipate reductase activity of wild-type enzyme
I463L
no alpha-aminoadipate reductase activity
I885L G881E
conserved residue in the posttranslational activation domain LGGHSI, less than 50% of wild-type activity
I987V
92% of the alpha-aminoadipate reductase activity of wild-type enzyme
K424R
26% of the alpha-aminoadipate reductase activity of wild-type enzyme
K424T
3% of the alpha-aminoadipate reductase activity of wild-type enzyme
K451Q
58% of the alpha-aminoadipate reductase activity of wild-type enzyme
K451R
no alpha-aminoadipate reductase activity
K535Q
94% of the alpha-aminoadipate reductase activity of wild-type enzyme
L446I
71% of the alpha-aminoadipate reductase activity of wild-type enzyme
L471V
89% of the alpha-aminoadipate reductase activity of wild-type enzyme
L983V
31% of the alpha-aminoadipate reductase activity of wild-type enzyme
M440L
99% of the alpha-aminoadipate reductase activity of wild-type enzyme
P423V
51% of the alpha-aminoadipate reductase activity of wild-type enzyme
P462A
2% of the alpha-aminoadipate reductase activity of wild-type enzyme
P462S
no alpha-aminoadipate reductase activity
Q464E
17% of the alpha-aminoadipate reductase activity of wild-type enzyme
Q511E
31% of the alpha-aminoadipate reductase activity of wild-type enzyme
Q511L
129% of the alpha-aminoadipate reductase activity of wild-type enzyme
R465K
2% of the alpha-aminoadipate reductase activity of wild-type enzyme
R465S
no alpha-aminoadipate reductase activity
S417A
10% of the alpha-aminoadipate reductase activity of wild-type enzyme
S417T
82% of the alpha-aminoadipate reductase activity of wild-type enzyme
S419A
16% of the alpha-aminoadipate reductase activity of wild-type enzyme
S419T
no alpha-aminoadipate reductase activity
S456T
59% of the alpha-aminoadipate reductase activity of wild-type enzyme
S884A
conserved residue in the posttranslational activation domain LGGHSI, loss of activity
S884F
conserved residue in the posttranslational activation domain LGGHSI, loss of activity
S985A
85% of the alpha-aminoadipate reductase activity of wild-type enzyme
T416A
no alpha-aminoadipate reductase activity
T416S
35% of the alpha-aminoadipate reductase activity of wild-type enzyme
T469S
80% of the alpha-aminoadipate reductase activity of wild-type enzyme
T506A
49% of the alpha-aminoadipate reductase activity of wild-type enzyme
T506S
no alpha-aminoadipate reductase activity
T534A
103% of the alpha-aminoadipate reductase activity of wild-type enzyme
T977S
70% of the alpha-aminoadipate reductase activity of wild-type enzyme
T980S
28% of the alpha-aminoadipate reductase activity of wild-type enzyme
V426L
64% of the alpha-aminoadipate reductase activity of wild-type enzyme
V529I
117% of the alpha-aminoadipate reductase activity of wild-type enzyme
G910A
mutation in the activation domain (IGGHSI), no activity
S913A
mutation in the activation domain (IGGHSI), no activity
S913T
mutation in the activation domain (IGGHSI), no activity
additional information
truncated enzymes based on NPS3, the L-alpha-aminoadipic acid reductase of the basidiomycete Ceriporiopsis subvermispora, lacking the ADA domain either partially or entirely are tested for activity in vitro, together with an ADA-adenylation didomain and the ADA domain-less adenylation domain
additional information
enzyme Lys1 is active when expressed in Escherichia coli and exhibits significant alpha-aminoadipate reductase activity without the addition of CoA or Schizosaccharomyces pombe phosphopantetheinyl transferase
additional information
-
enzyme Lys1 is active when expressed in Escherichia coli and exhibits significant alpha-aminoadipate reductase activity without the addition of CoA or Schizosaccharomyces pombe phosphopantetheinyl transferase
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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
Schizosaccharomyces pombe (P40976), Schizosaccharomyces pombe, Schizosaccharomyces pombe 972 (P40976)
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 (P07702), Saccharomyces cerevisiae
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 (Q9HDP9), Acremonium chrysogenum, Acremonium chrysogenum ATCC 48272 (Q9HDP9)
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 (Q12572), Candida albicans
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
Guo, S.; Bhattacharjee, J.K.
Site-directed mutational analysis of the novel catalytic domains of alpha-aminoadipate reductase (Lys2p) from Candida albicans
Mol. Genet. Genomics
269
271-279
2003
Candida albicans (Q12572), Candida albicans
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 (P40976), Schizosaccharomyces pombe
brenda
Yan, H.; He, P.; Cheng, H.R.; Shen, A.; Jiang, N.
Cloning, sequencing and characterization of the alpha-aminoadipate reductase gene (LYS2) from Saccharomycopsis fibuligera
Yeast
24
189-199
2007
Saccharomycopsis fibuligera (Q1W284), Saccharomycopsis fibuligera, Saccharomycopsis fibuligera PD70 (Q1W284), Saccharomycopsis fibuligera PD70
brenda
Lu, Y.; Mach, R.; Affenzeller, K.; Kubicek, C.
Regulation of alpha-aminoadipate reductase from Penicillium chrysogenum in relation to the flux from alpha-aminoadipate into penicillin biosynthesis
Can. J. Microbiol.
38
758-763
1992
Penicillium chrysogenum
brenda
Affenzeller, K.; Jaklitsch, W.; Hnlinger, C.; Kubicek, C.
Lysine biosynthesis in Penicillium chrysogenum is regulated by feedback inhibition of alpha-aminoadipate reductase
FEMS Microbiol. Lett.
58
293-297
1989
Penicillium chrysogenum
-
brenda
Kalb, D.; Lackner, G.; Rappe, M.; Hoffmeister, D.
Activity of alpha-aminoadipate reductase depends on the N-terminally extending domain
ChemBioChem
16
1426-1430
2015
Gelatoporia subvermispora (A0A0S2LUS1)
brenda
Gatrell, S.; Berg, L.; Grimmett, J.; Moritz, J.; Blemings, K.
Effect of moderate alterations of dietary protein or lysine on indices of lysine metabolism in liver, kidney, and heart of growing pigs1
Can. J. Anim. Sci.
98
9-17
2017
Sus scrofa
-
brenda
Donzelli, B.; Turgeon, B.; Gibson, D.; Krasnoff, S.
Disruptions of the genes involved in lysine biosynthesis, iron acquisition, and secondary metabolisms affect virulence and fitness in Metarhizium robertsii
Fungal Genet. Biol.
98
23-34
2017
Metarhizium robertsii (A0A0A1V264), Metarhizium robertsii ARSEF 2575 (A0A0A1V264)
brenda