Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.2.1.95 - L-2-aminoadipate reductase and Organism(s) Schizosaccharomyces pombe and UniProt Accession P40976

for references in articles please use BRENDA:EC1.2.1.95
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Schizosaccharomyces pombe
UNIPROT: P40976
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Schizosaccharomyces pombe
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
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.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-lysine
enzyme from Schizosaccharomyces pombe is more sensitive to feedback inhibition by lysine in vitro than the enzyme of Saccharomyces cerevisiae
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team