Information on EC 1.2.1.11 - aspartate-semialdehyde dehydrogenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
1.2.1.11
-
RECOMMENDED NAME
GeneOntology No.
aspartate-semialdehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
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+
show the reaction diagram
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+
show the reaction diagram
catalytic mechanism, substrate recognition
-
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
catalytic Cys135 is essential for activity
-
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
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+
show the reaction diagram
catalytic mechanism, active site structure, catalytic nucleophile is Cys134
Q9KQG2, -
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
Lactobacillus plantarum NCIMB 8826
-
-
-
Phosphorylation
-
-
-
-
redox reaction
-
-
-
-
redox reaction
-
-
reduction
-
-
-
-
reduction
Lactobacillus plantarum NCIMB 8826
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Cysteine and methionine metabolism
-
ectoine biosynthesis
-
Glycine, serine and threonine metabolism
-
grixazone biosynthesis
-
homoserine biosynthesis
-
Lysine biosynthesis
-
lysine biosynthesis I
-
lysine biosynthesis II
-
lysine biosynthesis III
-
lysine biosynthesis VI
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
norspermidine biosynthesis
-
spermidine biosynthesis II
-
SYSTEMATIC NAME
IUBMB Comments
L-aspartate-4-semialdehyde:NADP+ oxidoreductase (phosphorylating)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ASA dehydrogenase
-
-
-
-
ASA DH
-
-
-
-
ASADH
-
-
-
-
ASADHD
Lactobacillus plantarum NCIMB 8826
-
-
-
ASD enzyme
Q597F4
-
ASD enzyme
Mycobacterium tuberculosis H37
Q597F4
-
-
aspartate beta-semialdehyde dehydrogenase
-
-
aspartate beta-semialdehyde dehydrogenase
-
-
aspartate semialdehyde dehydrogenase
-
-
-
-
aspartate semialdehyde dehydrogenase
-
-
aspartate semialdehyde dehydrogenase
-
-
aspartate semialdehyde dehydrogenase
-
-
aspartate semialdehyde dehydrogenase
-
-
aspartate semialdehyde dehydrogenase
Lactobacillus plantarum IAM 12477, Lactobacillus plantarum NCIMB 8826
-
-
-
aspartate semialdehyde dehydrogenase
-, P0A542
-
aspartate semialdehyde dehydrogenase
-
-
aspartate semialdehyde dehydrogenase
-
-
aspartate semialdehyde dehydrogenase
Q8KQ27
-
aspartate semialdehyde dehydrogenase
Streptomyces clavuligerus NRRL 3585
Q8KQ27
-
-
aspartate semialdehyde dehydrogenase
Q9KQG2
-
aspartate-beta-semialdehyde dehydrogenase
-
-
aspartate-beta-semialdehyde dehydrogenase
-
-
aspartate-beta-semialdehyde dehydrogenase
-
-
aspartate-beta-semialdehyde dehydrogenase
P44801
-
aspartate-beta-semialdehyde dehydrogenase
-
-
aspartate-beta-semialdehyde dehydrogenase
P0A542
-
aspartate-beta-semialdehyde dehydrogenase
Q597F4
-
aspartate-beta-semialdehyde dehydrogenase
Mycobacterium tuberculosis H37
Q597F4
-
-
aspartate-beta-semialdehyde dehydrogenase
-
-
aspartate-beta-semialdehyde dehydrogenase
Q9KQG2
-
aspartate-semialdehyde dehydrogenase
-
-
aspartate-semialdehyde dehydrogenase
-
-
aspartate-semialdehyde dehydrogenase
-
-
aspartate-semialdehyde dehydrogenase
Lactobacillus plantarum NCIMB 8826
-
-
-
aspartate-semialdehyde dehydrogenase
-
-
aspartate-semialdehyde dehydrogenase
-
-
aspartic beta-semialdehyde dehydrogenase
-
-
-
-
aspartic semialdehyde dehydrogenase
-
-
-
-
aspartyl beta-semialdehyde dehydrogenase
-
-
aspartyl semialdehyde dehydrogenase
-
-
dehydrogenase, aspartate semialdehyde
-
-
-
-
ecASADH
-
-
hiASADH
P44801
-
L-aspartate-beta-semialdehyde dehydrogenase
P44801
-
L-aspartate-beta-semialdehyde:NADP oxidoreductase (phosphorylating)
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9000-98-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
-
Q5ALM0
Uniprot
Manually annotated by BRENDA team
mutant derepressed for aspartate-beta-semialdehyde dehydrogenase biosynthesis
-
-
Manually annotated by BRENDA team
; strain NCIMB 8826
-
-
Manually annotated by BRENDA team
strain IAM 12477
-
-
Manually annotated by BRENDA team
Lactobacillus plantarum IAM 12477
strain IAM 12477
-
-
Manually annotated by BRENDA team
Lactobacillus plantarum NCIMB 8826
strain NCIMB 8826
-
-
Manually annotated by BRENDA team
strain H37 Rv, gene asd
Q597F4
SwissProt
Manually annotated by BRENDA team
Mycobacterium tuberculosis H37
strain H37 Rv, gene asd
Q597F4
SwissProt
Manually annotated by BRENDA team
wild type strain G165-3A and mutant strain G184-1A
-
-
Manually annotated by BRENDA team
no activity in Homo sapiens
-
-
-
Manually annotated by BRENDA team
strain NRRL 3585, gene asd
SwissProt
Manually annotated by BRENDA team
Streptomyces clavuligerus NRRL 3585
strain NRRL 3585, gene asd
SwissProt
Manually annotated by BRENDA team
El Tor N16961, TIGR locus VC2036
SwissProt
Manually annotated by BRENDA team
isozymes ASADH1 and ASADH2
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
C5BB06, -
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-, P0A542
second enzyme in the lysine/homoserine biosynthetic pathways
-
-
r
beta-3-methylaspartyl phosphate + NADPH
beta-3-methylaspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
P0A9Q9
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-, Q9FVC4
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
Q51344
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-, O25801
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
P23247, -
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
synthesis of threonine
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
synthesis of threonine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
synthesis of threonine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
synthesis of threonine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
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+
show the reaction diagram
-
synthesis of methionine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
synthesis of methionine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
Q8KQ27, -
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
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+
show the reaction diagram
-
part of the biosynthetic aspartate pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
-, Q597F4
physiological forward reaction direction, key enzyme in diaminopimelic acid biosynthetic pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
physiological forward reaction, reductive dephosphorylation in the aspartate biosynthetic pathway
-
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
Q9KQG2, -
reductive dephosphorylation in the aspartate biosynthetic pathway of plants and microorganisms
-
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
reductive dephosphorylation
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
Mycobacterium tuberculosis H37
Q597F4
physiological forward reaction direction, key enzyme in diaminopimelic acid biosynthetic pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
Streptomyces clavuligerus NRRL 3585
Q8KQ27
-, 2nd step in the biosynthetic aspartate pathway, also required for biosynthesis of the beta-lactam caphamycin, overview
-
-
?
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
Q9KQG2
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NAD+
L-4-aspartyl phosphate + NADH + H+
show the reaction diagram
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
P0A9Q9
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-, Q9FVC4
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
Q51344
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-, O25801
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
P23247, -
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
-
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-, P0A542
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
Q5ALM0
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
C5BB06, -
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
P0A542
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+
show the reaction diagram
-, P0A542
the enzyme takes part in the lysine/homoserine-biosynthetic pathway
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
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 + H+
show the reaction diagram
P0A542
active site structure, overview
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
Lactobacillus plantarum NCIMB 8826
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
Lactobacillus plantarum IAM 12477
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
C5BB06
-
-
-
?
L-aspartate-4-semialdehyde + cacodylate + NADP+
L-4-aspartyl cacodylate + NADPH
show the reaction diagram
P44801
10% of the activity with phosphate
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
P44801
-
-
-
?
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-, Q597F4
-
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
reverse reaction: reductive dephosphorylation
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
Q9KQG2, -
-
reverse reaction: reductive dephosphorylation
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
P44801
reductive dephosphorylation in the aspartate biosynthetic pathway
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
reductive dephosphorylation in the aspartate biosynthetic pathway, aspartate-beta-semialdehydr is the key intermediate in biosynthesis of diaminopimelic acid, formation of an acyl-enzyme intermediate
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
formation of an acyl-enzyme intermediate
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
P44801
formation of an acyl-enzyme intermediate
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
Mycobacterium tuberculosis H37
Q597F4
-
-
-
r
additional information
?
-
-
the putative phosphate side contains arginine and a lysine that can provide electrostratic attraction to bind an oxyanion
-
-
-
additional information
?
-
-
when arsenate is substituted for phosphate the rates are about one-half those with corresponding phosphate concentrations
-
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-, P0A542
second enzyme in the lysine/homoserine biosynthetic pathways
-
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
P0A9Q9
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-, Q9FVC4
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
Q51344
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-, O25801
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
P23247, -
-
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
synthesis of threonine
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
synthesis of threonine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
synthesis of threonine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
synthesis of threonine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
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+
show the reaction diagram
-
synthesis of methionine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
synthesis of methionine
-
-
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
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+
show the reaction diagram
-
part of the biosynthetic aspartate pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
-, Q597F4
physiological forward reaction direction, key enzyme in diaminopimelic acid biosynthetic pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
physiological forward reaction, reductive dephosphorylation in the aspartate biosynthetic pathway
-
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
Q9KQG2, -
reductive dephosphorylation in the aspartate biosynthetic pathway of plants and microorganisms
-
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
Mycobacterium tuberculosis H37
Q597F4
physiological forward reaction direction, key enzyme in diaminopimelic acid biosynthetic pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
Streptomyces clavuligerus NRRL 3585
Q8KQ27
2nd step in the biosynthetic aspartate pathway, also required for biosynthesis of the beta-lactam caphamycin, overview
-
-
?
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
Q9KQG2
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
Q5ALM0
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
C5BB06, -
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
P0A542
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+
show the reaction diagram
-, P0A542
the enzyme takes part in the lysine/homoserine-biosynthetic pathway
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
-
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 + H+
show the reaction diagram
Lactobacillus plantarum NCIMB 8826
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
Lactobacillus plantarum IAM 12477
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
C5BB06
-
-
-
?
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
P44801
reductive dephosphorylation in the aspartate biosynthetic pathway
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
reductive dephosphorylation in the aspartate biosynthetic pathway, aspartate-beta-semialdehydr is the key intermediate in biosynthesis of diaminopimelic acid
-
-
r
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
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+
NADP+
-
dependent on
NADP+
Q9KQG2, -
binding mechanism and structure
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+
P0A542
binding domain structure, overview
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+
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(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,5R)-2,3,4,5-tetrahydropyridine-2,5-dicarboxylate
-
-
(2R,5R)-5-nitro-2,3,4,5-tetrahydropyridine-2-carboxylate
-
-
(2R,7aR)-2,3,7,7a-tetrahydro-1H-indole-2,6-dicarboxylate
-
-
(2R,7aR)-6-hydroxy-2,3,7,7a-tetrahydro-1H-indole-2-carboxylate
-
-
(2R,7aR)-6-nitro-2,3,7,7a-tetrahydro-1H-indole-2-carboxylate
-
-
(2R,8aR)-2,7-dinitro-1,2,8,8a-tetrahydronaphthalene
-
-
(3aR)-2-oxo-2,3,3a,4-tetrahydro-1H-benzimidazole-5-carboxylic acid
-
-
(3aR)-5-nitro-1,3,3a,4-tetrahydro-2H-benzimidazol-2-one
-
-
(3aR)-5-nitro-3a,4-dihydro-1H-indene-1,3(2H)-dione
-
-
(3aR)-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
-
-
(3aR)-6-chloro-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
-
-
(7aR)-2-oxo-2,3,7,7a-tetrahydro-1H-indole-6-carboxylate
-
-
(7aR)-3-(carboxylatomethyl)-6-nitro-7,7a-dihydro-1H-indole-2-carboxylate
-
-
(S)-2-amino-5-fluoro-4-oxo-5-phosphono-pentanoic acid
-
irreversible inhibition
(S)-2-amino-5-phosphono-pent-4-ynoic acid
-
-
2'-phosphoribose AMP
-
-
3-Chloroacetylpyridine-adenine dinucleotide phosphate
-
NADP+ and NADPH protect
3-hydroxyaspartic acid
-
-
4-nitro-N,N-diethylbenzimidazolinone
-
-
-
4-nitro-N,N-dimethylbenzimidazolinone
-
-
-
4-nitro-N-ethylphthalimide
-
-
-
4-nitro-N-methylphthalimide
-
-
-
5-(carboxylatocarbonyl)-1H-pyrrole-2-carboxylate
-
-
5-nitropyridine-2-methylcarboxylate
-
-
-
5-[[(4-nitrophenyl)amino]carbonyl]-1,3-benzenedimethylcarboxylate
-
-
-
acetylenic and z-olefinic analogues
-
competitive inhibition
-
Adenosine 5'-triphosphate
-
causes a time-dependent inactivation at a concentration of 3.5 mM, 0C, pH 6.5 and 2 mM dithiothreitol, inactivation can be completely reversed by warming the reaction mixture to 25C, 50% inactivation occurs at a concentration of 2.5 mM, NADH protects
Aromatic aldehydes
-
e.g.: benzaldehyde, weak
-
cis-5-phosphonic acid pipecolic acid
-
-
-
cysteine
-
in the reverse reaction
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
formaldehyde
-
-
Glutaraldehyde
-
-
GSSG
-
oxidized glutathione
homocysteine
-
in the reverse reaction
iodoacetamide
-
at 0.1 mM: 45.4% inactivation in the absence of NADP+, 22% inactivation in the presence of 1 mM NADP+
iodoacetate
-
-
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
Q9KQG2, -
inactivation, reversible by addition of DTT or 2-mercaptoethanol
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-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-isoleucine
-
at 1 mM: 18% repression of enzyme synthesis, at 5 mM: 62% repression of enzyme synthesis
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
L-lysine
-
enzyme assayed in the reverse reaction at pH 10
L-lysine
-
slightly represses the enzyme
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
-
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-methionine
-
at 1 mM: 40% repression of the enzyme synthesis, at 5 mM: 62% repression of the enzyme synthesis
L-threonine
-
enzyme assayed in the reverse reaction at pH 10
L-threonine
-
represses the enzyme considerably
N-ethylmaleimide
-
-
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+
NADPH-Tris-chloride buffer
-
promotes a weak inactivation at 0C, NADH protects
p-hydroxymercuribenzoate
-
-
perrhenate
-
very weak inhibitor
-
petrosamine B
-
50% inhibition at 0.306 mM. Petrosamine B is a pyridoacridine alkaloid isolated from the sponge Oceanapia sp.
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.
phosphonate
-
weak inhibitor
pipecolic acid-5-(R)-phosphate hydrochloric acid
-
-
-
pipecolic acid-5-(S)-phosphate hydrochloric acid
-
-
-
potassium phosphate
-
at a concentration of 10 mM promotes 60% inactivation at 0C 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
pyridine-2,5-dimethylcarboxylate
-
-
-
S-methyl cysteine sulfoxide
-
inhibitor binding structure deduced from crystal structure
S-methyl-L-cysteine sulfoxide
Q9KQG2, -
covalently binding inhibitor via Cys134 at the active site, inactivation, inhibition and binding mechanism, reversible by addition of DTT or 2-mercaptoethanol
thieno[2,3-b]thiophene-2,5-dicarboxylate
-
-
trans-5-phosphonic acid pipecolic acid
-
-
-
Tris salts
-
100 mM promotes 60.5% inactivation in the presence of 10 mM ATP and 17% inactivation in the absence of ATP
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
additional information
-
not: chelating agents
-
additional information
-
no feed-back inhibition by threonine or methionine
-
additional information
-
-
-
additional information
-
-
-
additional information
-
inhibitor binding structure and mechanism
-
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
Q8KQ27, -
no inhibition by pathway endproducts amino acids threonine, methionine, lysine, and isoleucine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
H2CO3
-
enhances activity 4 or 5 times in both directions
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.6
-
arsenate
-
-
140
-
Cacodylate
-
recombinant wild-type enzyme, pH 9.0, 30C
6
-
HAsO42-
-
-
0.16
-
L-4-aspartyl phosphate
-
-
0.16
-
L-4-aspartyl phosphate
-
in 0.2 M bicine buffer, pH 8.6, at 25C
0.12
-
L-aspartate 4-semialdehyde
Q51344
-
0.16
-
L-aspartate 4-semialdehyde
P23247
gene II
0.17
-
L-aspartate 4-semialdehyde
-
in 0.2 M bicine buffer, pH 8.6, at 25C
0.19
-
L-aspartate 4-semialdehyde
P23247
gene I
0.2
-
L-aspartate 4-semialdehyde
-
-
0.24
-
L-aspartate 4-semialdehyde
-
-
1.25
-
L-aspartate 4-semialdehyde
-
-
2.6
-
L-aspartate 4-semialdehyde
-
-
0.03
-
L-aspartate-4-semialdehyde
-
recombinant mutant R103L
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, 30C
0.4
-
L-aspartate-4-semialdehyde
-
recombinant mutant R270K
0.5
-
L-aspartate-4-semialdehyde
-
recombinant mutant H277N, pH 9.0, 30C
0.955
-
L-aspartate-4-semialdehyde
Q597F4
recombinant enzyme, pH 9.0, 30C
0.065
-
NADP+
Q597F4
recombinant enzyme, pH 9.0, 30C
0.09
-
NADP+
-
-
0.11
-
NADP+
-
recombinant mutant R103L
0.13
-
NADP+
Q51344
-
0.17
-
NADP+
-
recombinant mutant R270K
0.2
-
NADP+
-
recombinant wild-type enzyme
0.2
-
NADP+
-
recombinant wild-type enzyme, pH 9.0, 30C
0.32
-
NADP+
P23247
gene I
0.36
-
NADP+
P23247
gene II
0.6
-
NADP+
-
recombinant mutant K246L
0.7
-
NADP+
-
recombinant mutant R103K
1.1
-
NADP+
-
recombinant mutant H277N, pH 9.0, 30C
1.6
-
NADP+
-
recombinant mutant E243D
0.02
-
NADPH
-
mutant
0.025
-
NADPH
-
wild type
0.0929
-
NADPH
-, Q9FVC4
at 0.15 mM aspartyl phosphate
0.032
-
phosphate
-
in 0.2 M bicine buffer, pH 8.6, at 25C
1
-
phosphate
-
recombinant mutant K246L
1.1
-
phosphate
P23247
gene I
1.5
-
phosphate
Q51344
-
1.5
-
phosphate
-
recombinant mutant E243D
1.6
-
phosphate
-
-
1.6
-
phosphate
-
recombinant wild-type enzyme
1.6
-
phosphate
-
recombinant wild-type enzyme, pH 9.0, 30C
1.9
-
phosphate
-
recombinant mutant R270K
2.7
-
phosphate
-
recombinant mutant H277N, pH 9.0, 30C
2.9
-
phosphate
-
-
9
-
phosphate
-
-
11.39
-
phosphate
Q597F4
recombinant enzyme, pH 9.0, 30C
22
-
phosphate
P23247
gene II
36.6
-
phosphate
-
recombinant mutant R103K
240
-
phosphate
-
recombinant mutant R103L
0.14
-
vanadate
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
15.6
-
aspartyl phosphate
-, Q9FVC4
-
0.12
-
L-aspartate 4-semialdehyde
Q5ALM0
pH and temperature not specified in the publication
58
-
L-aspartate 4-semialdehyde
P23247
gene II
120
-
L-aspartate 4-semialdehyde
P23247
gene I
160
-
L-aspartate 4-semialdehyde
Q51344
-
330
-
L-aspartate 4-semialdehyde
-
-
0.24
-
L-aspartate-4-semialdehyde
-
recombinant mutant R103L
0.4
-
L-aspartate-4-semialdehyde
-
recombinant mutant R270K
1.2
-
L-aspartate-4-semialdehyde
-
recombinant mutant R103K
3.2
-
L-aspartate-4-semialdehyde
-
recombinant mutant H277N, pH 9.0, 30C
4
-
L-aspartate-4-semialdehyde
-
recombinant mutant E243D
11
-
L-aspartate-4-semialdehyde
-
recombinant mutant K246L
330
-
L-aspartate-4-semialdehyde
-
recombinant wild-type enzyme
330
-
L-aspartate-4-semialdehyde
-
recombinant wild-type enzyme, pH 9.0, 30C
2
-
L-aspartate-semialdehyde
-
-
3.2
-
NADP+
-
recombinant mutant H277N, pH 9.0, 30C
8.49
-
NADP+
Q597F4
recombinant enzyme, pH 9.0, 30C
330
-
NADP+
-
recombinant wild-type enzyme, pH 9.0, 30C
3.2
-
phosphate
-
recombinant mutant H277N, pH 9.0, 30C
330
-
phosphate
-
recombinant wild-type enzyme, pH 9.0, 30C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
236
-
L-aspartate 4-semialdehyde
-
in 0.2 M bicine buffer, pH 8.6, at 25C
222982
265
-
phosphate
-
in 0.2 M bicine buffer, pH 8.6, at 25C
27500
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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 22C
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 22C
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 22C
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 22C
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 22C
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 22C
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 22C
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 22C
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 22C
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 22C
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 22C
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 22C
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+, 37C
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+, 37C
0.05
-
2'-phosphoribose AMP
-
-
0.04
-
3-Chloroacetylpyridine-adenine dinucleotide phosphate
-
competitive inhibitor with respect to NADP+
4
-
4-nitro-N,N-diethylbenzimidazolinone
-
Ki above 4 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22C
-
0.086
-
4-nitro-N,N-dimethylbenzimidazolinone
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22C
-
4
-
4-nitro-N-ethylphthalimide
-
Ki above 4 mM in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22C
-
0.89
-
4-nitro-N-methylphthalimide
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22C
-
1.1
-
4-nitro-N-methylphthalimide
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22C
-
20
-
5-nitropyridine-2-methylcarboxylate
-
Ki above 20 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22C
-
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 22C
-
0.22
-
Periodate
-
-
140
-
perrhenate
-
-
-
17
-
phosphonate
-
-
20
-
pyridine-2,5-dimethylcarboxylate
-
Ki above 20 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22C
-
11
-
tellurate
-
-
26
-
tungstate
-
-
20
-
z-olefin
-
-
-
10
-
homocysteine
-
-
additional information
-
additional information
-
inhibition kinetics at 21C and pH 7.5
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.306
-
petrosamine B
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.002
-
-
K12 6201 strain, enriched media plus diaminopimelic acid
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
0.012
-
-
grown in minimal medium plus isoleucine
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
0.02
-
-
grown in complex medium
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
0.048
-
-
assay system plus threonine
0.12
-
-
B AC70R1 strain, enriched media
0.215
-
-
gene asd1
0.373
-
Q8KQ27, -
partially purified recombinant enzyme
0.4
-
-
K12 23631 strain, minimal media plus N-formyllysine
0.94
-
-
B AC70R1 strain, minimal media
1.8
-
-
K12 6201/PoP126 strain, enriched media plus ampicillin
2.149
-
-
gene asd2; when expressed in Escherichia coli
2.7
-
-
B AC70R1/PoP12 strain, enriched media plus tetracycline
5.3
-
-
B AC70R1/PoP12 strain, minimal media plus tetracycline
26
-
-
K12 23631/pOP12 strain, minimal media plus N-formyllysine and tetracycline
26
-
-, Q9FVC4
-
145
-
-
K12 23631/pOP12, after three times purification of the enzyme
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
Q51344
-
additional information
-
P23247
-
additional information
-
Q597F4
purified recombinant enzyme
additional information
-
-
lysine production activity in recombinant strains, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
7.8
-
mutant
7.5
-
-
assay at
8
9
-
L-aspartate 4-semialdehyde + arsenate
8
-
-
wild type
8
-
-
L-aspartyl phosphate + NADPH
8
-
-
activity assay
8.5
-
-
in both directions
9
-
-
L-aspartate 4-semialdehyde + PO43-
9
-
Q597F4
assay at
9
-
-
activity assay
9
-
-
activity assay
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
19
-
-
mutant
22
-
-
activity assay performed at room temperature
23
-
-
activity assay
25
-
-
assay at
28
-
-
above 28C, wild type
30
-
-
assay at
30
-
-
assay at
30
-
Q597F4
assay at
30
-
-
activity assay
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
highly expressed; weakly expressed
Manually annotated by BRENDA team
Lactobacillus plantarum NCIMB 8826
-
highly expressed; weakly expressed
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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)
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
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)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
70000
-
-
gel filtration
75000
-
-
homodimer in solution, determined by gel filtration; recombinant His-tagged enzyme, gel filtration
77000
-
-
sucrose density gradient centrifugation
77500
-
-
ultracentrifugation
140000
-
-
gel filtration
156000
-
-
sedimentation equilibrium, meniscus depletion technique
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 45000, SDS-PAGE
?
-
x * 37000, SDS-PAGE
?
Q597F4
x * 37000, about, recombinant enzyme, SDS-PAGE
?
Mycobacterium tuberculosis H37
-
x * 37000, about, recombinant enzyme, SDS-PAGE
-
dimer
-
2 * 38000, SDS-PAGE
dimer
-
2 * 44000, SDS-PAGE
dimer
-
2 * 40000
dimer
-, Q9FVC4
2 * 36000, SDS-PAGE
dimer
-
crystal structure, subdomain structure of subunits, open and closed enzyme forms
dimer
Q9KQG2, -
crystal structure, communication mechanism between the active sites of the subunits, overview
dimer
-
2 * 37000, about, recombinant His-tagged nezyme, SDS-PAGE
dimer
P0A542
dimerization domain structure, overview
homodimer
-
crystallization
homodimer
-
crystallization
homodimer
-
recombinant enzyme
homodimer
Q5ALM0
x-ray crystallography
tetramer
-
4 * 41000, SDS-PAGE
tetramer
-
4 * 39530, nucleotide sequence analysis of the HOM2 region
homodimer
-
2 * 39000, SDS-PAGE
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
P0A542
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion method, using 20% (w/v) PEG 400, 0.1 M HEPES pH 6.5, 0.1 M MgCl2, at 20C
Q5ALM0
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, 4C, X-ray diffraction structure determination and analysis at 1.95 A and 1.6 A resolution, respectively, modeling
-
using the hanging drop method
-
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, 20C, 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
-
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, 20C, 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
-
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, 20C, 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
-
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, 20C, 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
-
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
-
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 18C, two different crystal forms, X-ray diffraction structure determination and analysis at 2.18-2.75 A resolution
-
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
-
; 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
-
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, 20C, 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
Q9KQG2, -
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, 4C, 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
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
-
-
20 min, crude extract, 20% loss of activity
50
-
-
3 min, 50% loss of activity, mutant, 5 min, no loss of activity, wild type
65
-
-
30 min, wild type, stable
additional information
-
-
stability of recombinant wild-type and mutant enzymes, oveview
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
lyophilization of purified or partially purified enzyme, slight loss of activity
-
adenosine 5'-triphosphate, time dependent inactivation at 0C
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, no noticeable loss of activity
-, Q9FVC4
-20C, 10 mM potassium phosphate, pH 7.2, 0.1 mM EDTA, 1 mM dithioerythritol, 50% glycerol, 2 months
-
4C, 10 mM potassium phosphate, pH 7.2, 0.1 mM EDTA, 1 mM dithioerythritol, several days
-
frozen or on ice, after dialysis, 1 month stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
using anionic exchange chromatography on DEAE EMD 650 column and Q-Sepharose column
-, Q9FVC4
cobalt immobilized metal-affinity column chromatography and Source 30Q column chromatography
Q5ALM0
K-12, using ammonium sulfate precipitation and column chromatography on Sephadex G-200 and DEAE-Sephadex A-50
-
recombinant enzyme from strain BL21(DE3) in several steps
-
to homogeneity
-
using column chromatography on DEAE-cellulose, DEAE-Sephadex A-50, hydroxylapatite, ultrogel ACA-44 and Sepharose C3
-
using heat treatment, column chromatography on DEAE-cellulose, ammonium sulfate precipitation and column chromatography on Sephadex G-200
-
using ammonium sulfate precipitation and column chromatography on Q Sepharose XL and Procion Red-A
-
Ni-affinity chromatography
-
anion exchange chromatography and gel-filtration; using anion-exchange chromatography, Source 15Q, followed by gel filtration
-
by using affinity chromatography and gel filtration; recombinant His-tagged enzyme from Escherichia coli strain M15 by nickel affinity chromatography and gel filtration
-
Ni-NTA column chromatography and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography to 96% purity
Q597F4
using column chromatography on Q Sepharose XL and phenyl-Sepharose
Q51344
using ammonium sulfate precipitation and column chromatography on Sephadex G-200, DEAE-cellulose and hydroxylapatite
-
using heat treatment, acid precipitation, protamine sulfate treatment and ammonium sulfate precipitation
-
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
-
Ni-affinity chromatography and anion exchange chromatography; using a Co2+ affinity matrix and anion exchange chromatography
-
partially, recombinant enzyme from Escherichia coli, 37fold
Q8KQ27, -
recombinant enzyme from Escherichia coli to over 95% purity by anion exchange chromatography and gel filtration
-
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
P23247
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
cloning and recombinant protein overproduction with Escherichia coli
-, Q9FVC4
expressed in Escherichia coli BL21 cells
Q5ALM0
expression Escherichia coli
-
recombinant large scale expression in strain BL21(DE3)
-
expressed in Escherichia coli
-
expression of wild-type and mutant enzymes
-
expressed as inclusion bodies with an N-terminal hexahistidine tag in pET28b vector or subcloned into pET41 vector with NdeI/SalI
-, O25801
expression in 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
-
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
-
expression in Escherichia coli; into the pET41-41a vector for transformation into Rosetta-competent Escherichia coli cells
-
expressed in Escherichia coli M15 cells
-
expression of His-tagged enzyme in Escherichia coli strain M15; heterologous expression in Escherichia coli
-
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
Q597F4
expressed in Escherichia coli
-
expressed in Escherichia coli
Q51344
HOM2 gene encodes aspartic semialdehyde dehydrogenase
-
expressed in Escherichia coli
-
expressed in Escherichia coli
-
expression as His-tag fusion protein in Escherichia coli BL21 (DE3); into a pET28a vector for expression in Escherichia coli BL21DE3
-
gene asd, cloning from genomic DNA library, DNA sequence determination and analysis, expression in enzyme-deficient auxotrophic Escherichia coli strain CGSC5080
Q8KQ27, -
expressed in Escherichia coli, the genome contains two genes for the enzyme
P23247
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C136S
-
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
C136S
-
the mutation virtually eliminates catalysis
E243D
-
site-directed mutagenesis, unaltered Km for the substrates but 8fold increased Km for cofactor NADP+, active site structural alterations
E243D
-
the mutant shows 1.2% activity compared to the wild type enzyme
H277N
-
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
H277N
-
the mutant shows 1% activity compared to the wild type enzyme
K246R
-
site-directed mutagenesis, mutation of a putative phosphate binding residue, unaltered substrate Km, active site structural alterations
K246R
-
the mutant shows 3.3% activity compared to the wild type enzyme
R103K
-
site-directed mutagenesis, adversely affected interaction between enzyme and phosphate, active site structural alterations
R103K
-
the mutant shows 0.4% activity compared to the wild type enzyme
R103L
-
site-directed mutagenesis, altered interaction between enzyme and phosphate, active site structural alterations
R103L
-
the mutant shows 0.07% activity compared to the wild type enzyme
R267L
-
the mutant shows 9.5% activity compared to the wild type enzyme
R270K
-
site-directed mutagenesis, active site mutant, unaltered substrate Km, active site structural alterations
R270K
-
the mutant shows 0.1% activity compared to the wild type enzyme
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
enzyme is potential target for antimicrobial drugs
pharmacology
-
enzyme is a target for development of antibiotics
medicine
-
target for antibiotic development
biotechnology
-
development of lysine-overproducing strains
biotechnology
Lactobacillus plantarum NCIMB 8826
-
development of lysine-overproducing strains
-
medicine
Q597F4
enzyme is a validated drug target
pharmacology
Q597F4
inhibitor design from enzyme three-dimensional structure
medicine
Mycobacterium tuberculosis H37
-
enzyme is a validated drug target
-
pharmacology
Mycobacterium tuberculosis H37
-
inhibitor design from enzyme three-dimensional structure
-
medicine
-
target for antibiotic development
drug development
-
ASADH is a target for the development of novel antibiotics, especially for Gram-negative bacteria that require diaminopimelate for cell-wall biosynthesis
additional information
Q9KQG2, -
enzyme is an attractive target for development of antibacterial, fungicidal, or herbicidal compounds