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Information on EC 1.2.1.95 - L-2-aminoadipate reductase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P07702

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EC Tree
IUBMB 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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Saccharomyces cerevisiae
UNIPROT: P07702
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Word Map
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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(S)-2-amino-6-oxohexanoate
+
NADP+
+
AMP
+
diphosphate
=
L-2-aminoadipate
+
NADPH
+
H+
+
ATP
+
+
+
=
+
+
+
Synonyms
alpha-aminoadipate reductase, lys1+, alpha-aminoadipate delta-semialdehyde synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LYS2
-
-
-
-
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adipate + NADPH + H+ + ATP
adipate semialdehyde + NADP+ + AMP + diphosphate
show the reaction diagram
-
-
-
?
D-2-aminoadipate + NADPH + H+ + ATP
(R)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
show the reaction diagram
-
-
-
?
L-2-aminoadipate + NADPH + H+ + ATP
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
show the reaction diagram
-
-
-
?
S-carboxymethyl-L-cysteine + NADPH + H+ + ATP
S-formylmethyl-L-cysteine + NADP+ + AMP + diphosphate
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
adipate
pH 8.8, 37°C
2.7
D-2-aminoadipate
pH 8.8, 37°C
0.47
L-2-aminoadipate
pH 8.8, 37°C
0.62
NADPH
pH 8.8, 37°C
0.43
S-carboxymethyl-L-cysteine
pH 8.8, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0045
adipate
pH 8.8, 37°C
0.63
D-2-aminoadipate
pH 8.8, 37°C
41.7
L-2-aminoadipate
pH 8.8, 37°C
6
S-carboxymethyl-L-cysteine
pH 8.8, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0005
adipate
pH 8.8, 37°C
0.23
D-2-aminoadipate
pH 8.8, 37°C
88.3
L-2-aminoadipate
pH 8.8, 37°C
14
S-carboxymethyl-L-cysteine
pH 8.8, 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
155000
x * 155000, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 155000, calculated
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
residue Ser880 is modified by phosphopantetheinylate, leading to activiation of the enzyme. Protein Lys5 catalyzes the modification using coenzyme A
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in ERscherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team