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Information on EC 1.2.1.11 - aspartate-semialdehyde dehydrogenase and Organism(s) Vibrio cholerae serotype O1 and UniProt Accession Q9KQG2

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Vibrio cholerae serotype O1
UNIPROT: Q9KQG2 not found.
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The enzyme appears in selected viruses and cellular organisms
Synonyms
asadh, aspartate semialdehyde dehydrogenase, aspartate-beta-semialdehyde dehydrogenase, aspartate-semialdehyde dehydrogenase, aspartate beta-semialdehyde dehydrogenase, asa dh, aspartic semialdehyde dehydrogenase, l-aspartate-beta-semialdehyde dehydrogenase, asd enzyme, ecasadh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ASA dehydrogenase
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ASA DH
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ASADH
aspartate beta-semialdehyde dehydrogenase
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aspartate semialdehyde dehydrogenase
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aspartate-beta-semialdehyde dehydrogenase
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aspartic beta-semialdehyde dehydrogenase
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aspartic semialdehyde dehydrogenase
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dehydrogenase, aspartate semialdehyde
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L-aspartate-beta-semialdehyde:NADP oxidoreductase (phosphorylating)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Phosphorylation
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redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
L-aspartate-4-semialdehyde:NADP+ oxidoreductase (phosphorylating)
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CAS REGISTRY NUMBER
COMMENTARY hide
9000-98-0
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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-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
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?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
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r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
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-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
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?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-([[(1S)-1-carboxy-2-hydroxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
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4-([[(1S)-1-carboxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
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N-((4-(2-benzyl)vinyl)benzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(1-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(2-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(2-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(2-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(2-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(2-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(3-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(3-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(3-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(3-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(4-(2-perfluoropropyl))-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(4-biphenyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(4-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(4-carboxamidebenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(4-carboxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(4-difluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(4-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(4-t-butylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(4-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(4-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-(ethylmorpholino)-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-acetal-N-carboxymethyl-3,4-dicarboxybenzylamine
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N-acetonitrile, N-carboxymethyl-3,4-dicarboxybenzylamine
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N-allyl, N-carboxymethyl-3,4-dicarboxybenzylamine
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N-benzyl, N-carboxymethyl-3,4-dicarboxybenzylamine
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N-carboxyethyl-3,4-dicarboxybenzylamine
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N-carboxymethyl-3,4-dicarboxybenzylamine
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N-methyl, N-carboxymethyl-3,4-dicarboxybenzylamine
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additional information
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the ASADH enzyme family shares the same substrate binding and active site catalytic groups, but the enzymes from representative bacterial and fungal species show different inhibition patterns when previously screened against low molecular weight inhibitors identified from fragment library screening. ASADH inhibitor development, overview. No inhibition by 4-([[(1S)-1-carboxy-2-hydroxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid, N-(4-bromobenzyl)-N-carboxyethyl-3,4-dicarboxybenzylamine , and N-(4-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16 - 0.19
L-aspartate 4-semialdehyde
0.32 - 0.36
NADP+
1.1 - 22
phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
58 - 120
L-aspartate 4-semialdehyde
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.654
4-([[(1S)-1-carboxy-2-hydroxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
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pH 8.6, 22°C
0.609
4-([[(1S)-1-carboxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
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pH 8.6, 22°C
1.1
N-((4-(2-benzyl)vinyl)benzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.749
N-(1-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.737
N-(2-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.721
N-(2-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.724
N-(2-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.708
N-(2-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.727
N-(2-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.665
N-(3-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.69
N-(3-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.684
N-(3-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.678
N-(3-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.639
N-(4-(2-perfluoropropyl))-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.634
N-(4-biphenyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.629
N-(4-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.649
N-(4-carboxamidebenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.635
N-(4-carboxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.698
N-(4-difluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.608
N-(4-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.648
N-(4-t-butylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.663
N-(4-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.628
N-(4-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.692
N-(ethylmorpholino)-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.655
N-acetal-N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.498
N-acetonitrile, N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.663
N-allyl, N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.696
N-benzyl, N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.528
N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
0.675
N-methyl, N-carboxymethyl-3,4-dicarboxybenzylamine
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pH 8.6, 22°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the ASADH enzyme family shares the same substrate binding and active site catalytic groups, but the enzymes from representative bacterial and fungal species show different inhibition patterns when previously screened against low molecular weight inhibitors identified from fragment library screening
metabolism
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aspartate-beta-semialdehyde dehydrogenase lies at the first branch point in the aspartate metabolic pathway which leads to the biosynthesis of several essential amino acids and some important metabolites. This pathway is crucial for many metabolic processes in plants and microbes like bacteria and fungi, but is absent in mammals
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme and enzyme in complex with substrate L-aspartate semialdehyde, method optimization, purified protein in 50 mM sodium citrate, pH 5.6, with 0.2 M ammonium acetate and 2 mM DTT via dialysis overnight, hanging drop vapour diffusion method, 4°C, diluted back into 100 mM Tris, pH 8.5, with 200 mM ammonium acetate and 5 mM DTT with 12 mg/ml protein, 0.001 ml protein solution is mixed with 0.001 ml of precipitant containing 0.1 M sodium citrate, pH 5.5-6.5, 5 mM DTT, 0.1-0.4 M ammonium acetate, and 24-27% PEG 8000, method optimization, overview, X-ray diffraction structure determination and analysis at 2.0-2.2 A resolution, molecular replacement method
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli to over 95% purity by anion exchange chromatography and gel filtration
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using column chromatography on Q Sepharose XL and omega-aminohexyl-agarose for the purification of V. cholerae I and column chromatography on Q Sepharose XL for the purification of V. cholerae II
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, the genome contains two genes for the enzyme
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expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Viola, R.E.; Liu, X.; Ohren, J.F.; Faehnle, C.R.
The structure of a redundant enzyme: a second isoform of aspartate beta-semialdehyde dehydrogenase in Vibrio cholerae
Acta Crystallogr. Sect. D
D64
321-330
2008
Vibrio cholerae serotype O1
Manually annotated by BRENDA team
Thangavelu, B.; Bhansali, P.; Viola, R.E.
Elaboration of a fragment library hit produces potent and selective aspartate semialdehyde dehydrogenase inhibitors
Bioorg. Med. Chem.
23
6622-6631
2015
Streptococcus pneumoniae, Vibrio cholerae serotype O1
Manually annotated by BRENDA team