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Information on EC 1.2.1.31 - L-aminoadipate-semialdehyde dehydrogenase and Organism(s) Candida albicans and UniProt Accession Q12572

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EC Tree
IUBMB Comments
(S)-2-amino-6-oxohexanoate undergoes a spontaneous dehydration forming the cyclic (S)-2,3,4,5-tetrahydropyridine-2-carboxylate, which serves as a substrate for the hydrogenation reaction.
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This record set is specific for:
Candida albicans
UNIPROT: Q12572
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Word Map
The taxonomic range for the selected organisms is: Candida albicans
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
aldh7a1, antiquitin, alpha-ar, aasadh, aldehyde dehydrogenase 7a1, alpha-aar, lys1p, alpha-aasa dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, alpha-aminoadipate semialdehyde dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-aminoadipate semialdehyde dehydrogenase
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2-aminoadipic semialdehyde dehydrogenase
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alpha-aminoadipate-semialdehyde dehydrogenase
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Alpha-AR
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dehydrogenase, aminoadipate semialdehyde
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L-alpha-aminoadipate delta-semialdehyde oxidoreductase
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L-alpha-aminoadipate delta-semialdehyde:NAD oxidoreductase
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L-alpha-aminoadipate delta-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
L-2-aminoadipate-6-semialdehyde:NAD(P)+ 6-oxidoreductase
(S)-2-amino-6-oxohexanoate undergoes a spontaneous dehydration forming the cyclic (S)-2,3,4,5-tetrahydropyridine-2-carboxylate, which serves as a substrate for the hydrogenation reaction.
CAS REGISTRY NUMBER
COMMENTARY hide
9067-87-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-alpha-aminoadipate + NAD(P)H
L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
show the reaction diagram
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-lysine
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70% inhibition at 50 mM
S-(beta-aminoethyl)-L-cysteine
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92% inhibition at 1 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LYS2_CANAX
1391
0
154741
Swiss-Prot
other Location (Reliability: 3)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
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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
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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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterlogous expressed in Escherichia coli
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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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Suvarna, K.; Seah, L.; Bhattacherjee, V.; Bhattacharjee, J.K.
Molecular analysis of the LYS2 gene of Candida albicans: homology to peptide antibiotic synthetases and the regulation of the.alpha-aminoadipate reductase
Curr. Genet.
33
268-275
1998
Candida albicans, Saccharomyces cerevisiae
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team