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Enzyme Nomenclature
Information on EC 1.2.1.11 - aspartate-semialdehyde dehydrogenase
for references in articles please use BRENDA:EC1.2.1.11
Word Map on EC 1.2.1.11
- 1.2.1.11
-
diaminopimelic
- aspartokinase
- dihydrodipicolinate
-
beta-aspartyl
-
balanced-lethal
- drug development
- medicine
- biotechnology
- pharmacology
- synthesis
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
1.2.1.11
-
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RECOMMENDED NAME
GeneOntology No.
aspartate-semialdehyde dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+
catalytic mechanism, role of substrate binding groups, residues Arg270, Glu243, Arg103, and Lys246 are involved
-
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+
catalytic mechanism, function of the catalytic nucleophile Cys136 and the acid-base catalytic His277, the latter is also stabilizing the hemithioacetal intermediate
-
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+
catalytic mechanism, substrate recognition
-
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+
catalytic Cys135 is essential for activity
-
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+
catalytic mechanism, identification and structural characterization of the tetrahedral reaction intermediate, substrate binding structure
-
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+
catalytic mechanism, active site structure, catalytic nucleophile is Cys134
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
Phosphorylation
-
-
-
-
redox reaction
reduction
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-aspartate-4-semialdehyde:NADP+ oxidoreductase (phosphorylating)
-
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CAS REGISTRY NUMBER
COMMENTARY
9000-98-0
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Homo sapiens
mutant derepressed for aspartate-beta-semialdehyde dehydrogenase biosynthesis
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
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
evolution
-
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
malfunction
deletion of the asdA gene precluded the growth of Edwardsiella ictaluri in absence of diaminopimelic acid
malfunction
-
the aspartate semialdehyde dehydrogenase (asd)-inactivated mutant exhibits significantly reduced growth in calf serum compared with the wild-type. The mutant also exhibits significantly reduced growth in medium, mimicking the concentrations of amino acids and glucose in calf serum, but can be recovered by addition of lysine and threonine
malfunction
-
enzyme deficiency or inhibition of enzyme activity leads to 80% reduced cell wall materials compared to the wild-type, in addition to obvious morphological differences, phenotype, overview
malfunction
-
deletion of the asdA gene precluded the growth of Edwardsiella ictaluri in absence of diaminopimelic acid
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malfunction
-
enzyme deficiency or inhibition of enzyme activity leads to 80% reduced cell wall materials compared to the wild-type, in addition to obvious morphological differences, phenotype, overview
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malfunction
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the aspartate semialdehyde dehydrogenase (asd)-inactivated mutant exhibits significantly reduced growth in calf serum compared with the wild-type. The mutant also exhibits significantly reduced growth in medium, mimicking the concentrations of amino acids and glucose in calf serum, but can be recovered by addition of lysine and threonine
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metabolism
-
the enzyme lies at the first branch point in the biosynthetic pathway of important amino acids including lysine and methionine and the cell-wall component diaminopimelate
metabolism
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aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
-
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
-
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
-
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
-
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
-
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
aspartate-semialdehyde dehydrogenase catalyzes the reductive dephosphorylation of the substrate beta-aspartyl phosphate into aspartate semialdehyde, a key intermediate in the aspartate biosynthetic pathway and functions at a critical junction in the aspartate biosynthetic pathway
metabolism
Q4WWR8;
aspartate-semialdehyde dehydrogenase catalyzes the reductive dephosphorylation of the substrate beta-aspartyl phosphate into aspartate semialdehyde, a key intermediate in the aspartate biosynthetic pathway and functions at a critical junction in the aspartate biosynthetic pathway
metabolism
-
Asd is an essential enzyme for the biosynthesis of lysine, methionine, and threonine from aspartate
metabolism
-
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
metabolism
-
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
metabolism
the enzyme has a rate-limiting key function in the biosynthesis of amino acids L-threonine, L-lysine, and L-isoleucine from L-aspartate via L-homoserine
metabolism
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aspartate-semialdehyde dehydrogenase catalyzes the reductive dephosphorylation of the substrate beta-aspartyl phosphate into aspartate semialdehyde, a key intermediate in the aspartate biosynthetic pathway and functions at a critical junction in the aspartate biosynthetic pathway
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metabolism
-
aspartate-semialdehyde dehydrogenase catalyzes the reductive dephosphorylation of the substrate beta-aspartyl phosphate into aspartate semialdehyde, a key intermediate in the aspartate biosynthetic pathway and functions at a critical junction in the aspartate biosynthetic pathway
-
metabolism
-
the enzyme lies at the first branch point in the biosynthetic pathway of important amino acids including lysine and methionine and the cell-wall component diaminopimelate
-
metabolism
-
Asd is an essential enzyme for the biosynthesis of lysine, methionine, and threonine from aspartate
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physiological function
the enzyme catalyzes the NADPH-dependent reductive dephosphorylation of 4-aspartyl phosphate to produce the key intermediate aspartate semialdehyde
physiological function
Q4WWR8;
the enzyme catalyzes the NADPH-dependent reductive dephosphorylation of 4-aspartyl phosphate to produce the key intermediate aspartate semialdehyde
physiological function
-
the enzyme catalyzes the NADPH-dependent reductive dephosphorylation of 4-aspartyl phosphate to produce the key intermediate aspartate semialdehyde
-
physiological function
-
the enzyme catalyzes the NADPH-dependent reductive dephosphorylation of 4-aspartyl phosphate to produce the key intermediate aspartate semialdehyde
-
additional information
The structure of CnASADH belongs to the Rossmann-fold superfamily of pyridine-linked dehydrogenases and shares the same overall monomeric structural features as the other ASADHs for which structures are determined
additional information
-
active site structure analysis and comparison, detailed overview
additional information
Q4WWR8;
active site structure analysis and comparison, detailed overview
additional information
-
active site structure analysis and comparison, detailed overview
-
additional information
-
The structure of CnASADH belongs to the Rossmann-fold superfamily of pyridine-linked dehydrogenases and shares the same overall monomeric structural features as the other ASADHs for which structures are determined
-
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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
beta-3-methylaspartyl phosphate + NADPH
beta-3-methylaspartate 4-semialdehyde + phosphate + NADP+
-
-
-
?
L-aspartate-4-semialdehyde + cacodylate + NADP+
L-4-aspartyl cacodylate + NADPH
10% of the activity with phosphate
-
-
r
aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
second enzyme in the lysine/homoserine biosynthetic pathways
-
-
r
aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
second enzyme in the lysine/homoserine biosynthetic pathways
-
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of threonine
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
enzyme in pathway from L-aspartic acid to L-lysine, L-methionine, L-threonine and L-isoleucine
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-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of threonine
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-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
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synthesis of threonine
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-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
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synthesis of threonine
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-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of methionine
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-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of methionine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
-
part of the biosynthetic aspartate pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
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reductive dephosphorylation
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-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
-
physiological forward reaction, reductive dephosphorylation in the aspartate biosynthetic pathway
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-
r
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
physiological forward reaction direction, key enzyme in diaminopimelic acid biosynthetic pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
physiological forward reaction direction, key enzyme in diaminopimelic acid biosynthetic pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
2nd step in the biosynthetic aspartate pathway, also required for biosynthesis of the beta-lactam caphamycin, overview
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
2nd step in the biosynthetic aspartate pathway, also required for biosynthesis of the beta-lactam caphamycin, overview
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-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
reductive dephosphorylation in the aspartate biosynthetic pathway of plants and microorganisms
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-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
?
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
?
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NAD+
L-4-aspartyl phosphate + NADH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NAD+
L-4-aspartyl phosphate + NADH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
Q4WWR8;
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
Q4WWR8;
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
ASADH is an important enzyme, occupying the first branch position of the biosynthetic pathway of the aspartate family of amino acids, i.e. lysine, methionine, isoleucine and threonine, L-aspartate-beta-semialdehyde is a key intermediate in the biosynthesis of diaminopimelic acid
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
the enzyme takes part in the lysine/homoserine-biosynthetic pathway
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
active site structure, overview
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
the essential ASADH produces the first branch-point metabolite in the biosynthetic pathways that lead to the production of lysine, threonine, methionine and isoleucine as well as the cell-wall precursor diaminopimelate
-
-
?
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
reverse reaction: reductive dephosphorylation
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
reductive dephosphorylation in the aspartate biosynthetic pathway
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
reductive dephosphorylation in the aspartate biosynthetic pathway, aspartate-beta-semialdehydr is the key intermediate in biosynthesis of diaminopimelic acid
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
formation of an acyl-enzyme intermediate
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
formation of an acyl-enzyme intermediate
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
reverse reaction: reductive dephosphorylation
-
r
additional information
?
-
-
the putative phosphate side contains arginine and a lysine that can provide electrostratic attraction to bind an oxyanion
-
-
-
additional information
?
-
-
maximum velocity with HAsO42- is 0.4 times that with HPO42-
-
-
-
additional information
?
-
-
the kinetic parameters with arsenate are comparable to those of phosphate, vanadate is an excellent substrate for the enzyme
-
-
-
additional information
?
-
-
oxyanion binding sites and structures with arsenate and periodate
-
-
-
additional information
?
-
-
when arsenate is substituted for phosphate the rates are about one-half those with corresponding phosphate concentrations
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
P9WNX5
second enzyme in the lysine/homoserine biosynthetic pathways
-
-
r
aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
P9WNX5
second enzyme in the lysine/homoserine biosynthetic pathways
-
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
Q9FVC4
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
P0A9Q9
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of threonine
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
enzyme in pathway from L-aspartic acid to L-lysine, L-methionine, L-threonine and L-isoleucine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
O25801
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
Q51344
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of threonine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of threonine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of threonine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of methionine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of methionine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
P23247
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
-
part of the biosynthetic aspartate pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
-
physiological forward reaction, reductive dephosphorylation in the aspartate biosynthetic pathway
-
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
P9WNX5
physiological forward reaction direction, key enzyme in diaminopimelic acid biosynthetic pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
P9WNX5
physiological forward reaction direction, key enzyme in diaminopimelic acid biosynthetic pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
Q8KQ27
2nd step in the biosynthetic aspartate pathway, also required for biosynthesis of the beta-lactam caphamycin, overview
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
Q8KQ27
2nd step in the biosynthetic aspartate pathway, also required for biosynthesis of the beta-lactam caphamycin, overview
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
Q9KQG2
reductive dephosphorylation in the aspartate biosynthetic pathway of plants and microorganisms
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
?
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
?
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
Q9KQG2
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
Q4WWR8
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
Q4WWR8
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
Q5ALM0
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
Q5KPK7
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
Q5KPK7
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
C5BB06
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
C5BB06
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
P0A9Q9
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
ASADH is an important enzyme, occupying the first branch position of the biosynthetic pathway of the aspartate family of amino acids, i.e. lysine, methionine, isoleucine and threonine, L-aspartate-beta-semialdehyde is a key intermediate in the biosynthesis of diaminopimelic acid
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
P9WNX5
the enzyme takes part in the lysine/homoserine-biosynthetic pathway
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
the essential ASADH produces the first branch-point metabolite in the biosynthetic pathways that lead to the production of lysine, threonine, methionine and isoleucine as well as the cell-wall precursor diaminopimelate
-
-
?
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
P44801
reductive dephosphorylation in the aspartate biosynthetic pathway
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
reductive dephosphorylation in the aspartate biosynthetic pathway, aspartate-beta-semialdehydr is the key intermediate in biosynthesis of diaminopimelic acid
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
in contrast to Gram-negative bacterial aspartate-beta-semialdehyde dehydrogenases which are specific for NADP+ the enzyme of Gram-positive showed a dual specificity for NAD+ and NADP+
NAD+
very low activity with the wild-type enzyme, but 44fold and 66fold higher activity with enzyme mutants Q350N and Q350N/H171A, respectively, compared to the wild-type
NADP+
-
; in contrast to Gram-negative bacterial aspartate-beta-semialdehyde dehydrogenases which are specific for NADP+ the enzyme of Gram-positive showed a dual specificity for NAD+ and NADP+
NADP+
the NADP+-binding domain consists of mixed beta-strands flanked on both sides with alpha-helices, with seven beta-strands, five alpha-helices and two 310-helices
NADPH
-
L-aspartate 4-semialdehyde dehydrogenase transfers the pro-S hydrogen from NADPH
additional information
-
NAD+: 0.1% or less the rate of reaction with NADP+
-
additional information
cofactor modes of wild-type and mutant enzymes determined by molecular modeling
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-2-amino-5-fluoro-4-oxo-5-phosphono-pentanoic acid
-
irreversible inhibition
3-Chloroacetylpyridine-adenine dinucleotide phosphate
-
NADP+ and NADPH protect
Adenosine 5'-triphosphate
-
causes a time-dependent inactivation at a concentration of 3.5 mM, 0°C, pH 6.5 and 2 mM dithiothreitol, inactivation can be completely reversed by warming the reaction mixture to 25°C, 50% inactivation occurs at a concentration of 2.5 mM, NADH protects
caulerpin
-
molecular docking and dynamics simulation of Vibrio anguillarum aspartate semialdehyde dehydrogenase with natural product caulerpin, which binds with high energy. Caulerpin can be used as antibiotic against Vibrio anguillarum in fish aquaculture industry
-
D-Cystine
-
70% inhibition at 0.01 mM, binds via the cysteine moiety covalently to the catalytic Cys135 of the enzyme, pH-dependent proces, optimal at pH 7.0-7.5, inhibition is reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione, no protection by aspartate-beta-semialdehyde, NADP+ or NADPH, inhibition mechanism and kinetics
DTNB
-
reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione
iodoacetamide
-
at 0.1 mM: 45.4% inactivation in the absence of NADP+, 22% inactivation in the presence of 1 mM NADP+
L-cystine diethyl ester
-
68% inhibition at 0.01 mM, reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione
L-cystine dimethyl ester
-
67% inhibition at 0.01 mM, reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione
L-cystine hydroxamate
-
20% inhibition at 0.01 mM, reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione
L-leucine
-
inhibits, when added to a final concentration of 10 mM in the assay system produces a decrease of 0.004 units in specific activity
NADPH-Tris-chloride buffer
-
promotes a weak inactivation at 0°C, NADH protects
potassium phosphate
-
at a concentration of 10 mM promotes 60% inactivation at 0°C in the presence of 10 mM ATP, at a concentration of 100 mM promotes 61% inactivation in the presence of 10 mM ATP and 32% inactivation in the absence of ATP, NADH protects
S-methyl cysteine sulfoxide
-
inhibitor binding structure deduced from crystal structure
S-methyl-L-cysteine sulfoxide
covalently binding inhibitor via Cys134 at the active site, inactivation, inhibition and binding mechanism, reversible by addition of DTT or 2-mercaptoethanol
(1R)-5-[(2-carboxyphenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
-
-
(1R)-5-[(3-nitrophenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
-
-
(1R)-5-[(4-nitrophenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
-
-
(2R,3aR)-5-[(methylsulfonyl)methyl]-2,3,3a,4-tetrahydro-1H-indole-2-carboxylate
-
-
(2R,3aR)-5-[(methylsulfonyl)methyl]-2,3,3a,4-tetrahydro-1H-indole-2-carboxylate
-
-
(3aR)-2-oxo-2,3,3a,4-tetrahydro-1H-benzimidazole-5-carboxylic acid
-
-
(7aR)-3-(carboxylatomethyl)-6-nitro-7,7a-dihydro-1H-indole-2-carboxylate
-
-
4-([[(1S)-1-carboxy-2-hydroxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
-
-
4-([[(1S)-1-carboxy-2-hydroxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
-
-
4-([[(1S)-1-carboxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
-
-
5-[[(4-nitrophenyl)amino]carbonyl]-1,3-benzenedimethylcarboxylate
-
-
iodoacetate
-
inhibition of arsenolysis, inhibition of the reduction of beta-aspartyl phosphate
iodoacetate
-
at 1 mM: completely inhibits in the absence or presence of NADP+, at 0.1 mM: 3% inactivation in the absence of NADP+, 50% inactivation in the presence of 1 mM NADP+
L-2-Amino-4-oxo-5-chloropentanoic acid
-
L-aspartate 4-semialdehyde protects the enzyme against inactivation, both NADP+ and NADPH decrease the rate of inactivation
L-2-Amino-4-oxo-5-chloropentanoic acid
-
substrate analogue, irreversible inactivation, pseudo-first-order kinetics
L-cystine
-
complete inhibition at 0.01 mM, binds via the cysteine moiety covalently to the catalytic Cys135 of the enzyme, pH-dependent process, optimal at pH 7.0-7.5, inhibition is reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione, no protection by aspartate-beta-semialdehyde, NADP+ or NADPH, inhibition mechanism and kinetics
L-cystine
inactivation, reversible by addition of DTT or 2-mercaptoethanol
L-isoleucine
-
at 1 mM: 18% repression of enzyme synthesis, at 5 mM: 62% repression of enzyme synthesis
L-isoleucine
-
inhibits, when added to a final concentration of 10 mM in the assay system produces a decrease of 0.003 units in specific activity
L-lysine
-
at 1 mM: 22% repression of the enzyme synthesis, at 5 mM: 44% repression of the enzyme synthesis, at 10 mM: 28% inhibition of the enzyme activity assayed in the reverse reaction
L-methionine
-
at 1 mM: 40% repression of the enzyme synthesis, at 5 mM: 62% repression of the enzyme synthesis
L-methionine
-
inhibits, when added to a final concentration of 10 mM in the assay system produces a decrease of 0.004 units in specific activity
L-threonine
-
at 1 mM: 25% repression of the enzyme synthesis, at 5 mM: 43% repression of the enzyme synthesis, at 10 mM: 37% inhibition of the enzyme activity assayed in the reverse reaction
N-((4-(2-benzyl)vinyl)benzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(2-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(2-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(3-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(3-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-(2-perfluoropropyl))-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-carboxamidebenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-difluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-ethylmaleimide
-
only 1 mol per subunit causes complete inactivation, at 0.1 mM: 91% inactivation in the absence of NADP+, 12% inactivation in the presence of 1 mM NADP+
petrosamine B
-
50% inhibition at 0.306 mM. Petrosamine B is a pyridoacridine alkaloid isolated from the sponge Oceanapia sp.; isolated from the methanol extract of the saustralian sponge Oceanapia sp.
petrosamine B
-
50% inhibition at 0.306 mM. Petrosamine B is a pyridoacridine alkaloid isolated from the sponge Oceanapia sp.
Tris salts
-
100 mM promotes 60.5% inactivation in the presence of 10 mM ATP and 17% inactivation in the absence of ATP
additional information
-
no inhibition by N,N'-diacetyl-L-cystine, L-cystine di-beta-naphthylamide, disulfiram, N-acetyl-L-cystine, 2,2-dithiodipyridine, 4,4-dithiodipyridine, L- and D-cysteine, and oxidized and reduced coenzyme A
-
additional information
-
no feed-back inhibition by threonine or methionine
-
additional information
-
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
-
additional information
no inhibition by pathway endproducts amino acids threonine, methionine, lysine, and isoleucine
-
additional information
-
no inhibition by pathway endproducts amino acids threonine, methionine, lysine, and isoleucine
-
additional information
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.17
L-aspartate 4-semialdehyde
-
in 0.2 M bicine buffer, pH 8.6, at 25°C
0.1
L-aspartate-4-semialdehyde
-
recombinant mutant R103K and mutant K246L
0.2
L-aspartate-4-semialdehyde
-
recombinant wild-type enzyme and mutant E243D
0.2
L-aspartate-4-semialdehyde
-
recombinant wild-type enzyme, pH 9.0, 30°C
0.5
L-aspartate-4-semialdehyde
-
recombinant mutant H277N, pH 9.0, 30°C
0.955
L-aspartate-4-semialdehyde
recombinant enzyme, pH 9.0, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.12
L-aspartate 4-semialdehyde
pH and temperature not specified in the publication
3.2
L-aspartate-4-semialdehyde
-
recombinant mutant H277N, pH 9.0, 30°C
330
L-aspartate-4-semialdehyde
-
recombinant wild-type enzyme, pH 9.0, 30°C
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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
1.2
(S)-2-amino-5-fluoro-4-oxo-5-phosphono-pentanoic acid
-
0.2 M Tris, 1 mM EDTA, pH 8.6, 15 mM phosphate, 0.15 mM NADP+, 37°C
3.9
(S)-2-amino-5-phosphono-pent-4-ynoic acid
-
0.2 M Tris, 1 mM EDTA, pH 8.6, 15 mM phosphate, 0.15 mM NADP+, 37°C
0.04
3-Chloroacetylpyridine-adenine dinucleotide phosphate
-
competitive inhibitor with respect to NADP+
0.324 - 0.654
4-([[(1S)-1-carboxy-2-hydroxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
3.6
N-(4-bromobenzyl)-N-(2-carboxy)ethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
additional information
additional information
-
inhibition kinetics at 21°C and pH 7.5
-
0.11
(1R)-5-[(4-nitrophenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.18
(1R)-5-[(4-nitrophenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.69
(2R,5R)-2,3,4,5-tetrahydropyridine-2,5-dicarboxylate
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
1.2
(2R,5R)-2,3,4,5-tetrahydropyridine-2,5-dicarboxylate
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
1.2
(2R,5R)-5-nitro-2,3,4,5-tetrahydropyridine-2-carboxylate
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
2.1
(2R,5R)-5-nitro-2,3,4,5-tetrahydropyridine-2-carboxylate
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.4
(3aR)-5-nitro-1,3,3a,4-tetrahydro-2H-benzimidazol-2-one
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
1.1
(3aR)-5-nitro-1,3,3a,4-tetrahydro-2H-benzimidazol-2-one
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
2.6
(3aR)-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
3.3
(3aR)-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.15
(3aR)-6-chloro-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.18
(3aR)-6-chloro-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.324
4-([[(1S)-1-carboxy-2-hydroxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
-
pH 8.6, 22°C
0.654
4-([[(1S)-1-carboxy-2-hydroxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
-
pH 8.6, 22°C
0.296
4-([[(1S)-1-carboxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
-
pH 8.6, 22°C
0.609
4-([[(1S)-1-carboxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
-
pH 8.6, 22°C
4
4-nitro-N,N-diethylbenzimidazolinone
-
Ki above 4 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
4
4-nitro-N,N-diethylbenzimidazolinone
-
Ki above 4 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.086
4-nitro-N,N-dimethylbenzimidazolinone
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.086
4-nitro-N,N-dimethylbenzimidazolinone
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
4
4-nitro-N-ethylphthalimide
-
Ki above 4 mM in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
4
4-nitro-N-ethylphthalimide
-
Ki above 4 mM in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.89
4-nitro-N-methylphthalimide
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
1.1
4-nitro-N-methylphthalimide
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
20
5-[[(4-nitrophenyl)amino]carbonyl]-1,3-benzenedimethylcarboxylate
-
Ki above 20 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
20
5-[[(4-nitrophenyl)amino]carbonyl]-1,3-benzenedimethylcarboxylate
-
Ki above 20 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
20
dimethyl pyridine-2,5-dicarboxylate
-
Ki above 20 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
20
dimethyl pyridine-2,5-dicarboxylate
-
Ki above 20 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
20
methyl 5-nitropyridine-2-carboxylate
-
Ki above 20 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
20
methyl 5-nitropyridine-2-carboxylate
-
Ki above 20 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.476
N-((4-(2-benzyl)vinyl)benzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
1.1
N-((4-(2-benzyl)vinyl)benzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.396
N-(1-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.529
N-(2-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.737
N-(2-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.524
N-(2-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.721
N-(2-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.329
N-(2-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.54
N-(2-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.708
N-(2-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.509
N-(2-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.727
N-(2-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.442
N-(3-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.665
N-(3-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.43
N-(3-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.69
N-(3-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.427
N-(3-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.684
N-(3-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.441
N-(3-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.678
N-(3-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.009
N-(4-(2-perfluoropropyl))-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.639
N-(4-(2-perfluoropropyl))-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.012
N-(4-biphenyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.057
N-(4-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.629
N-(4-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.229
N-(4-carboxamidebenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.649
N-(4-carboxamidebenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.072
N-(4-carboxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.635
N-(4-carboxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.054
N-(4-difluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.698
N-(4-difluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.063
N-(4-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.608
N-(4-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.016
N-(4-t-butylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.648
N-(4-t-butylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.036
N-(4-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.663
N-(4-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.024
N-(4-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.628
N-(4-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
3.8
N-(4-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.176
N-(ethylmorpholino)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.692
N-(ethylmorpholino)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.276
N-acetal-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.22
N-acetonitrile, N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.498
N-acetonitrile, N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.303
N-allyl, N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.297
N-benzyl, N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.296
N-methyl, N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0029
-
of the recombinant in the crude extracts of Escherichia coli
0.01
-
grown in minimal medium or in minimal medium plus lysine, methionine and threonine
0.013
-
grown in minimal medium plus lysine or in minimal medium plus threonine
0.015
-
grown in minimal medium plus leucine or in minimal medium plus methionine
0.04
-
assay system plus lysine or assays system plus lysine, threonine and methionine
0.043
-
no addition to the assay system or assay system plus methionine
26
additional information
26
-
K12 23631/pOP12 strain, minimal media plus N-formyllysine and tetracycline
additional information
-
lysine production activity in recombinant strains, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
8.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
-
pH 6.5: about 45% of activity maximum, mutant, about 8% of activity maximum, wild type, pH 9.0: about 55% of activity maximum, mutant, about 30% of activity maximum, wild type
8.4 - 9.5
-
at pH 8.4 and pH 9.5: 50% of maximal activity, L-aspartate 4-semialdehyde + phosphate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
30
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Q2T7H5
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264);
Q5ALM0
Candida albicans (strain SC5314 / ATCC MYA-2876);
Q5KPK7
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565);
Escherichia coli (strain K12);
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
Q57658
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440);
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh);
Q5F5D2
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090);
Q4WWR8
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100);
Q51344
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1);
Streptococcus pneumoniae (strain ATCC BAA-255 / R6);
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4);
Q971Y6
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7);
Q5SKU8
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579);
Trichophyton rubrum BMU01672;
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961);
P44801
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
P44801
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
P44801
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
P44801
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
P44801
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
P44801
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
P44801
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
P44801
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
P44801
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
P44801
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
P44801
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
P44801
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
P9WNX4
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh);
P9WNX4
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh);
Q8DQ00
Streptococcus pneumoniae (strain ATCC BAA-255 / R6);
Q8DQ00
Streptococcus pneumoniae (strain ATCC BAA-255 / R6);
A0A0H2UPS5
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4);
A0A0H2UPS5
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4);
A0A0H2UPS5
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4);
A0A0H2UPS5
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4);
Q9KQG2
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961);
Q9KQG2
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961);
P23247
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961);
P23247
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961);
Q9KQG2
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961);
Q9KQG2
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961);
Q9KQG2
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37000
38070
-
the expressed and purified monomer protein construct includes the 17-amino-acid sequence RGSHHHHHHGSACELGT between the N-terminal Met and the second amino acid Gly of the native Asd sequence, the total length of this protein is 362 amino acids
75000
-
homodimer in solution, determined by gel filtration; recombinant His-tagged enzyme, gel filtration
160000
recombinant His-tagged enzyme, gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
tetramer
additional information