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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
-
balanced-lethal
-
beta-aspartyl
- drug development
- medicine
- pharmacology
- biotechnology
- synthesis
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Specify your search results
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
mutant derepressed for aspartate-beta-semialdehyde dehydrogenase biosynthesis
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
malfunction
deletion of the asdA gene precluded the growth of Edwardsiella ictaluri in absence of diaminopimelic acid
malfunction
-
deletion of the asdA gene precluded the growth of Edwardsiella ictaluri in absence of diaminopimelic acid
-
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
-
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
-
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
-
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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 + phosphate + NAD+
L-4-aspartyl phosphate + NADH + H+
-
-
-
-
?
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
-
-
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
-
-
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+
-
-
-
-
?
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+
-
reductive dephosphorylation
-
-
?
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+
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
-
-
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 + 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+
-
-
-
-
?
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+
-
-
-
?
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+
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+
-
-
-
-
?
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
-
-
-
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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+
-
-
-
-
?
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+
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+
-
-
-
-
?
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+
P9WNX5
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+
-
-
-
-
?
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
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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+
additional information
-
NAD+: 0.1% or less the rate of reaction with NADP+
-
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+
NADPH
-
L-aspartate 4-semialdehyde dehydrogenase transfers the pro-S hydrogen from NADPH
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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
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
-
-
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-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
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
tetramer
additional information
dimer
-
crystal structure, subdomain structure of subunits, open and closed enzyme forms
dimer
crystal structure, communication mechanism between the active sites of the subunits, overview
tetramer
-
4 * 39530, nucleotide sequence analysis of the HOM2 region
additional information
-
the asymmetric unit contains three subunits: one complete dimer and a monomer which comes from a dimer lying along the crystallographic 2fold axis
additional information
secondary structure topology, homology modelling and enzyme structure analysis, comparison of the three-dimensional fold and comparative modelling, overview, the fist alphabeta unit contains the highly conserved GxxGxxG NAD-binding motif
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 20% (w/v) PEG 400, 0.1 M HEPES pH 6.5, 0.1 M MgCl2, at 20°C
enzyme in open and closed form, 30 mg/ml purified recombinant enzyme in 10 mM Tris, pH 7.4, 40 mM KCl, with equal volume of reservoir solution, 0.006 ml sitting drops by vapour diffusion utilizing micro-bridges, 20% v/v ethylene glycol, 4°C, X-ray diffraction structure determination and analysis at 1.95 A and 1.6 A resolution, respectively, modeling
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10 mg/ml purified recombinant wild-type and mutant enzymes free or in complex with the substrates, protein in 10 mM HEPES, pH 7.0, 1 mM EDTA, 1 mM DTT, by hanging drop vapour diffusion, 20°C, mixed with equal volume of precipitant solution containing 22-24% PEG 3350, and 0.2 M ammonium acetate, crystals are soaked for 1 h in a solution containing 2 mM aspartate-beta-semialdehyde or 100 mM phosphate, 26% PEG 3350, 0.2 M ammonium acetate, 0.1 M Tris-HCl, pH 8.5, and 20% glycerol, X-ray diffraction structure determination and analysis at about 2.0 A resolution
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15 mg/ml purified recombinant enzyme, in 10 mM HEPES, pH 7.0, 1 mM EDTA, 1 mM DTT, crystallized as apoenzyme, as hemithioacetal, or as hemithioacetal structure with bound phosphate, hanging drop vapour diffusion method, 20°C, 1:1 mixture of protein solution and precipitant solution, the latter containing 24-28% PEG 3350, 0.2 M ammonium acetate, 0.1 M Tris, pH 8.5, overnight, substrate complexing by soaking of crystals in mother liquor with 50 mM potassium phosphate, crystals are frozen in precipitant solution with 20% glycerol added, X-ray diffraction structure determination and analysis at 2.0-2.15 A resolution, modeling
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15 mg/ml purified recombinant wild-type enzyme in 10 mM HEPES, pH 7.0, 1 mM EDTA, and 1 mM DTT, enzyme is free or complexed with substrates phosphate and/or asparate-beta-semialdehyde, hanging drop vapour diffusion method, 20°C, against an equal volume of precipitant solution containing 24-28% PEG 3350, 0.2 M ammonium acetate, and 0.1 M Tris-HCl, pH 8.5, soaking of crystals before harvest in 100 mM phosphate and 2 mM aspartate-beta-semialdehyde, crystallization of mutant H277N in 10 mM HEPES, pH 7.0, 1 mM EDTA, and 1 mM DTT, by addition of precipitant solution containing 5 mM NADP+ and 5 mM inhibitor S-methyl-L-cysteine sulfoxide, 22% PEG 3350, 0.2 M ammonium acetate and 0.1 M sodium cacodylate, pH 6.5, X-ray diffraction structure determination and analysis at about 2.0 A resolution
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about 10 mg/ml pure recombinant wild-type enzyme in 10 mM HEPES, pH 7.0, 1 mM EDTA, and 1 mM DTT, complexed with oxyanions arsenate or periodate, hanging drop vapour diffusion method, 20°C, against an equal volume of precipitant solution containing 22-24% PEG 4000, 0.2 M ammonium acetate, and Tris-HCl, pH 8.5, soaking of crystals before harvest in a solution containing 26% PEG3350, 0.2 M ammonium acetate, 100 mM periodate or arsenate,0.1 M Tris-HCl, pH 8.5, and 20% glycerol, X-ray diffraction structure determination and analysis at 2.3 A resolution
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2.3 A resolution; the structure of aspartate-beta-semialdehyde dehydrogenase has been determined to 2.3 A resolution using multiwavelength anomalous diffraction phasing of a seleno-methionine-substituted derivative
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by using the hanging-drop vapour-diffusion method, crystallization in 2 different crystal forms, diffraction data analysis suggests the presence of up to four monomers in the asymmetric unit of the orthorhombic crystal form and of one or 2 monomers in the cubic crystal form; purified recombinant His-tagged enzyme, 9 mg/ml protein in 10 mM potassium phosphate buffer, pH 8.0, and 10 mM DTT, sitting drop vapour diffusion method, mixing of 500 nl of protein and of reservoir solution, the latter containing 1.6 M ammonium sulfate and 100 mM citric acid, pH 5.0, 2 days at 18°C, two different crystal forms, X-ray diffraction structure determination and analysis at 2.18-2.75 A resolution
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in complex with S-methyl-l-cysteine sulfoxide and sulfate, sitting drop vapor diffusion method, using 1.6 M ammonium sulfate and 100 mM citric acid pH 5.0
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; crystallization of the apo-enzyme, in complex with NADP+, in complex with L-aspartate-beta-semialdehyde, in complex with NADP+ and L-aspartate-beta-semialdehyde
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12 mg/ml purified recombinant enzyme free or in ternary complex with NADP+ and covalently bound inhibitor S-methyl-L-cysteine sulfoxide, protein in 10 mM HEPES, pH 7.0, 1 mM EDTA, and 1 mM DTT, hanging drop vapour diffusion method, 20°C, with or without 5 mM NADP+ and 5 mM inhibitor, against an equal volume of precipitant solution: containing 18% PEG 3350, 0.2 M sodium acetate, and 0.1 M Tris, pH 8.5 for the free enzyme, or containing 22% PEG 3350, 0.2 M sodium acetate, and 0.1 M sodium citrate, pH 5.6 for the ternary complex, addition of 20% glycerol for crystal freezing, X-ray diffraction structure determination and analysis at 2.8 A and 1.84 A resolution, respectively
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
additional information
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stability of recombinant wild-type and mutant enzymes, oveview
50
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3 min, 50% loss of activity, mutant, 5 min, no loss of activity, wild type
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilization of purified or partially purified enzyme, slight loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM potassium phosphate, pH 7.2, 0.1 mM EDTA, 1 mM dithioerythritol, 50% glycerol, 2 months
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4°C, 10 mM potassium phosphate, pH 7.2, 0.1 mM EDTA, 1 mM dithioerythritol, several days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
anion exchange chromatography and gel-filtration; using anion-exchange chromatography, Source 15Q, followed by gel filtration
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by using affinity chromatography and gel filtration; recombinant His-tagged enzyme from Escherichia coli strain M15 by nickel affinity chromatography and gel filtration
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cobalt immobilized metal-affinity column chromatography and Source 30Q column chromatography
K-12, using ammonium sulfate precipitation and column chromatography on Sephadex G-200 and DEAE-Sephadex A-50
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Ni-affinity chromatography and anion exchange chromatography; using a Co2+ affinity matrix and anion exchange chromatography
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recombinant enzyme from Escherichia coli to over 95% purity by anion exchange chromatography and gel filtration
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recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography to 96% purity
using ammonium sulfate precipitation and column chromatography on Q Sepharose XL and Procion Red-A
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using ammonium sulfate precipitation and column chromatography on Sephadex G-200, DEAE-cellulose and hydroxylapatite
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using anionic exchange chromatography on DEAE EMD 650 column and Q-Sepharose column
using column chromatography on DEAE-cellulose, DEAE-Sephadex A-50, hydroxylapatite, ultrogel ACA-44 and Sepharose C3
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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
using column chromatography on Q Sepharose XL and phenyl-Sepharose
using heat treatment, acid precipitation, protamine sulfate treatment and ammonium sulfate precipitation
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using heat treatment, column chromatography on DEAE-cellulose, ammonium sulfate precipitation and column chromatography on Sephadex G-200
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using protamine sulfate treatment, ammonium sulfate precipitation, chromatography on DEAE-Sephadex A-50 column, Bio-Gel hydroxylapatite phosphate column, Bio-Gel hydroxylapatite sulfate column, acid treatment and column chromatography on Sephadex G-200
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning and recombinant protein overproduction with Escherichia coli
co-expression with L-lysine-insensitive aspartokinase, dihydrodipicolinate synthase, and dihydrodipicolinate reductase in the parent strain and in an AEC-resistant mutant strain of Lactobacillus plantarum from a shuttle vector, leading to increased L-lysine production, but absolutely requiring overexpression of aspartokinase or dihydrodipicolinate synthase, overview
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expressed as inclusion bodies with an N-terminal hexahistidine tag in pET28b vector or subcloned into pET41 vector with NdeI/SalI
expressed in Escherichia coli
expressed in Escherichia coli, the genome contains two genes for the enzyme
expression as His-tag fusion protein in Escherichia coli BL21 (DE3); into a pET28a vector for expression in Escherichia coli BL21DE3
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expression in Escherichia coli
expression in Escherichia coli Hfr3000; genes are amplified from chromosomal DNA of Lactobacillus plantarum and cloned into the pCR2.1-TOPO vector for sequencing, and subcloned into the pUC18 vector for heterologous expression in Escherichia coli
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expression in Escherichia coli; into the pET41-41a vector for transformation into Rosetta-competent Escherichia coli cells
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expression of His-tagged enzyme in Escherichia coli strain M15; heterologous expression in Escherichia coli
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gene asd, cloning from genomic DNA library, DNA sequence determination and analysis, expression in enzyme-deficient auxotrophic Escherichia coli strain CGSC5080
gene asd, subcloning in Escherichia coli strain JM109, DNA sequence determination and analysis, optimization of functional overexpression in Escherichia coli strain M15 as His-tagged protein
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C136S
E243D
H277N
K246R
R103K
R103L
R267L
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the mutant shows 9.5% activity compared to the wild type enzyme
R270K
C136S
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site-directed mutagenesis, active site mutant is nearly inactive due to decrease in nuleophilicity, and also by a change in the orientation of the histidine imidazole ring
E243D
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site-directed mutagenesis, unaltered Km for the substrates but 8fold increased Km for cofactor NADP+, active site structural alterations
E243D
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the mutant shows 1.2% activity compared to the wild type enzyme
H277N
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site-directed mutagenesis, active site mutant shows 100fold decreased catalytic efficiency compared to the wild-type enzyme, shift in the position of the bound reaction intermediate
K246R
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site-directed mutagenesis, mutation of a putative phosphate binding residue, unaltered substrate Km, active site structural alterations
K246R
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the mutant shows 3.3% activity compared to the wild type enzyme
R103K
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site-directed mutagenesis, adversely affected interaction between enzyme and phosphate, active site structural alterations
R103K
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the mutant shows 0.4% activity compared to the wild type enzyme
R103L
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site-directed mutagenesis, altered interaction between enzyme and phosphate, active site structural alterations
R103L
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the mutant shows 0.07% activity compared to the wild type enzyme
R270K
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site-directed mutagenesis, active site mutant, unaltered substrate Km, active site structural alterations
R270K
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the mutant shows 0.1% activity compared to the wild type enzyme
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
drug development
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ASADH is a target for the development of novel antibiotics, especially for Gram-negative bacteria that require diaminopimelate for cell-wall biosynthesis
medicine
pharmacology
additional information
pharmacology
inhibitor design from enzyme three-dimensional structure
pharmacology
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inhibitor design from enzyme three-dimensional structure
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additional information
enzyme is an attractive target for development of antibacterial, fungicidal, or herbicidal compounds
additional information
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enzyme is an attractive target for development of antibacterial, fungicidal, or herbicidal compounds
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.11)
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