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Information on EC 1.2.1.95 - L-2-aminoadipate reductase
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EC Tree
1.2.1.95 L-2-aminoadipate reductaseIUBMB Comments
This enzyme, characterized from the yeast Saccharomyces cerevisiae, catalyses the reduction of L-2-aminoadipate to (S)-2-amino-6-oxohexanoate during L-lysine biosynthesis. An adenylation domain activates the substrate at the expense of ATP hydrolysis, and forms L-2-aminoadipate adenylate, which is attached to a peptidyl-carrier protein (PCP) domain. Binding of NADPH results in reductive cleavage of the acyl-S-enzyme intermediate, releasing (S)-2-amino-6-oxohexanoate. Different from EC 1.2.1.31, L-aminoadipate-semialdehyde dehydrogenase, which catalyses a similar transformation in the opposite direction without ATP hydrolysis.
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Word Map
- 1.2.1.95
- albicans
-
schizosaccharomyces
- saccharopine
- pombe
- chrysogenum
-
phosphopantetheinylate
- l-lysine
- homoisocitrate
- homocitrate
-
isofunctional
-
lysine-supplemented
- pptases
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
alpha-aminoadipate reductase, lys1+, alpha-aminoadipate delta-semialdehyde synthase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAR
AarA
alpha-aminoadipate reductase
Lys1+
LYS2
LYS2
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-2-amino-6-oxohexanoate + holo-[LYS2 peptidyl-carrier-protein] + NADP+ = L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein] + NADPH + H+
(1b)
-
-
-
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate = L-2-aminoadipate + NADPH + H+ + ATP
overall reaction
-
-
-
L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein] + AMP + diphosphate = L-2-aminoadipate + holo-[LYS2 peptidyl-carrier-protein] + ATP
(1a)
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(S)-2-amino-6-oxohexanoate:NADP+ oxidoreductase (ATP-forming)
This enzyme, characterized from the yeast Saccharomyces cerevisiae, catalyses the reduction of L-2-aminoadipate to (S)-2-amino-6-oxohexanoate during L-lysine biosynthesis. An adenylation domain activates the substrate at the expense of ATP hydrolysis, and forms L-2-aminoadipate adenylate, which is attached to a peptidyl-carrier protein (PCP) domain. Binding of NADPH results in reductive cleavage of the acyl-S-enzyme intermediate, releasing (S)-2-amino-6-oxohexanoate. Different from EC 1.2.1.31, L-aminoadipate-semialdehyde dehydrogenase, which catalyses a similar transformation in the opposite direction without ATP hydrolysis.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
L-2-aminoadipate + NADPH + H+ + ATP
presence of ATP and Mg2+ required
-
-
?
adipate + NADPH + H+ + ATP
adipate semialdehyde + NADP+ + AMP + diphosphate
-
-
-
?
D-2-aminoadipate + NADPH + H+ + ATP
(R)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
-
-
?
L-2-aminoadipate + NADPH + H+ + ATP
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
S-carboxymethyl-L-cysteine + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
-
20fold lower activity than with L-2-aminoadipate
-
-
?
S-carboxymethyl-L-cysteine + NADPH + H+ + ATP
S-formylmethyl-L-cysteine + NADP+ + AMP + diphosphate
-
-
-
?
L-2-aminoadipate + NADPH + H+ + ATP
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
-
-
?
L-2-aminoadipate + NADPH + H+ + ATP
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
-
-
?
L-2-aminoadipate + NADPH + H+ + ATP
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
-
-
?
L-2-aminoadipate + NADPH + H+ + ATP
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
-
-
-
?
L-2-aminoadipate + NADPH + H+ + ATP
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
no substrates: adipic acid, DL-diaminopimelic acid, L-glutamate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-2-aminoadipate + NADPH + H+ + ATP
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
-
can partly replace Mg2+, leading to 60% of maximum activity with Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-aminoadipate
inhibitory effect can be reversed by adding methionine
L-lysine
-
in strains Q176, D6/1014/A, and P2, in vivo activity of alpha-aminoadipate reductase from superior penicillin producer strains is more strongly inhibited by lysine, and this is related to their ability to accumulate increased amounts of alpha-aminoadipate, and hence penicillin
L-lysine
-
competitive with respect to alpha-aminoadipate. Presence of Lysine inhibits incorporation of alpha-aminoadipate into protein-bound lysine
L-lysine
enzyme from Schizosaccharomyces pombe is more sensitive to feedback inhibition by lysine in vitro than the enzyme of Saccharomyces cerevisiae
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
growth on medium containing lysine as the sole nitrogen source
-
additional information
-
growth on medium containing lysine as the sole nitrogen source
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.65
ATP
-
pH not specified in the publication, temperature not specified in the publication
0.3
L-2-aminoadipate
-
pH not specified in the publication, temperature not specified in the publication
0.06
NADPH
-
pH not specified in the publication, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.26
L-lysine
-
pH not specified in the publication, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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
-
Show AA Sequence and Transmembrane Helices (1274 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
132600
about, recombinant truncated enzyme, sequence calculation
155000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 depends on the N-terminally extending domain
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
side-chain modification
alpha-aminoadipate reductase Lys2 is posttranslationally activated by phosphopantetheinyl transferase Lys5 which transfers a phosphopantetheinyl group from coenzyme A to Lys2. Activation is required for catalytic activity
side-chain modification
residue Ser880 is modified by phosphopantetheinylate, leading to activiation of the enzyme. Protein Lys5 catalyzes the modification using coenzyme A
side-chain modification
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
G418A
31% of the alpha-aminoadipate reductase activity of wild-type enzyme
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
G984A
3% of the alpha-aminoadipate reductase activity of wild-type enzyme
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
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
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
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
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
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
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
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
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged truncated enzyme mutants from Escherichia coli strain KRX by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of the ORF of the Saccharomycopsis fibuligera alpha-aminoadipate reductase gene (LYS2) in a lys2- strain of Saccharomyces cerevisiae
recombinant expression of N-terminally His6-tagged truncated NPS3 enzyme mutant lacking the 247 amino acids of the N-terminal ADA domain from pET21a-based expression plasmid pMR1, recombinant expression of N-terminally His6-tagged truncated NPS3 enzyme mutant lacking the 152 amino acids of the N-terminal ADA domain from expression plasmid pDK22, and recombinant expression of the 102.8 kDa ADA-A didomain (lacking the C-terminal 515 amino acids) and the 75.7 kDa standalone NPS3A domain, respectively, in which the first 247 and terminal 515 amino acids are absent, from plasmids pDK24 and pDK25, both based on expression vector pET28a, all in Escherichia coli strain KRX
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activity from cells grown in lysine-supplemented minimal or YEPD media is less than the activity of cells grown in minimal medium
liver enzyme mRNA abundance is reduced 60% in pigs consuming the low lysine diet compared with the high protein diet and 68% in pigs consuming the low lysine diet compared with pigs consuming the high lysine diet
-
activity from cells grown in lysine-supplemented minimal or YEPD media is less than the activity of cells grown in minimal medium
activity from cells grown in lysine-supplemented minimal or YEPD media is less than the activity of cells grown in minimal medium
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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
-
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
-
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
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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