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Structure of a fungal form of aspartate-semialdehyde dehydrogenase from Aspergillus fumigatus

Dahal, G.P.; Viola, R.E.; Acta Crystallogr. Sect. F 73, 36-44 (2017)

Data extracted from this reference:

Application
EC Number
Application
Commentary
Organism
1.2.1.11
drug development
the enzyme is a validated target for antimicrobial drug design
Aspergillus fumigatus
Cloned(Commentary)
EC Number
Commentary
Organism
1.2.1.11
gene AFUA_3G06830, codon-optimized, recombinant expression of C-terminally His-tagged enzyme ASADH in Escherichia coli strain BL21(DE3)
Aspergillus fumigatus
Crystallization (Commentary)
EC Number
Crystallization
Organism
1.2.1.11
purified recombinant C-terminally His-tagged enzyme, hanging drop vapour diffusion method, crystallization screening, mixing of 0.001 ml protein solution plus 0.001 ml reservoir solution containing 1.9 M ammonium sulfate, 100 mM Bis-Tris, pH 6.5, at 20°C, crystals are either soaked or cocrystallized with 5 mM NADP+ and with several moderate inhibitors that are identified from fragment library screening, crystal cryoprotection with reservoir solution containing 20% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 2.8-3.2 A resolution, modeling by molecular replacement using CaASADH, PDB ID 3hsk, as the search model
Aspergillus fumigatus
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
Aspergillus fumigatus
-
L-4-aspartyl phosphate + NADPH + H+
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
Aspergillus fumigatus ATCC MYA-4609
-
L-4-aspartyl phosphate + NADPH + H+
-
-
r
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.1.11
Aspergillus fumigatus
Q4WWR8
-
-
1.2.1.11
Aspergillus fumigatus ATCC MYA-4609
Q4WWR8
-
-
1.2.1.11
no activity in Homo sapiens
-
and other mammals
-
Purification (Commentary)
EC Number
Commentary
Organism
1.2.1.11
recombinant C-terminally His-tagged enzyme ASADH from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, and dialysis
Aspergillus fumigatus
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
741540
Aspergillus fumigatus
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
741540
Aspergillus fumigatus ATCC MYA-4609
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
Subunits
EC Number
Subunits
Commentary
Organism
1.2.1.11
dimer
enzyme AfASADH displays a crystallographic dimer
Aspergillus fumigatus
1.2.1.11
More
enzyme secondary structure, crystal structure analysis, detailed overview
Aspergillus fumigatus
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
-
Aspergillus fumigatus
1.2.1.11
NADPH
-
Aspergillus fumigatus
Application (protein specific)
EC Number
Application
Commentary
Organism
1.2.1.11
drug development
the enzyme is a validated target for antimicrobial drug design
Aspergillus fumigatus
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.2.1.11
gene AFUA_3G06830, codon-optimized, recombinant expression of C-terminally His-tagged enzyme ASADH in Escherichia coli strain BL21(DE3)
Aspergillus fumigatus
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
-
Aspergillus fumigatus
1.2.1.11
NADPH
-
Aspergillus fumigatus
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.2.1.11
purified recombinant C-terminally His-tagged enzyme, hanging drop vapour diffusion method, crystallization screening, mixing of 0.001 ml protein solution plus 0.001 ml reservoir solution containing 1.9 M ammonium sulfate, 100 mM Bis-Tris, pH 6.5, at 20°C, crystals are either soaked or cocrystallized with 5 mM NADP+ and with several moderate inhibitors that are identified from fragment library screening, crystal cryoprotection with reservoir solution containing 20% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 2.8-3.2 A resolution, modeling by molecular replacement using CaASADH, PDB ID 3hsk, as the search model
Aspergillus fumigatus
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
Aspergillus fumigatus
-
L-4-aspartyl phosphate + NADPH + H+
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
Aspergillus fumigatus ATCC MYA-4609
-
L-4-aspartyl phosphate + NADPH + H+
-
-
r
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.2.1.11
recombinant C-terminally His-tagged enzyme ASADH from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, and dialysis
Aspergillus fumigatus
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
741540
Aspergillus fumigatus
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
741540
Aspergillus fumigatus ATCC MYA-4609
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.2.1.11
dimer
enzyme AfASADH displays a crystallographic dimer
Aspergillus fumigatus
1.2.1.11
More
enzyme secondary structure, crystal structure analysis, detailed overview
Aspergillus fumigatus
General Information
EC Number
General Information
Commentary
Organism
1.2.1.11
metabolism
aspartate-semialdehyde dehydrogenase catalyzes the reductive dephosphorylation of the substrate beta-aspartyl phosphate into aspartate semialdehyde, a key intermediate in the aspartate biosynthetic pathway and functions at a critical junction in the aspartate biosynthetic pathway
Aspergillus fumigatus
1.2.1.11
additional information
active site structure analysis and comparison, detailed overview
Aspergillus fumigatus
1.2.1.11
physiological function
the enzyme catalyzes the NADPH-dependent reductive dephosphorylation of 4-aspartyl phosphate to produce the key intermediate aspartate semialdehyde
Aspergillus fumigatus
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.2.1.11
metabolism
aspartate-semialdehyde dehydrogenase catalyzes the reductive dephosphorylation of the substrate beta-aspartyl phosphate into aspartate semialdehyde, a key intermediate in the aspartate biosynthetic pathway and functions at a critical junction in the aspartate biosynthetic pathway
Aspergillus fumigatus
1.2.1.11
additional information
active site structure analysis and comparison, detailed overview
Aspergillus fumigatus
1.2.1.11
physiological function
the enzyme catalyzes the NADPH-dependent reductive dephosphorylation of 4-aspartyl phosphate to produce the key intermediate aspartate semialdehyde
Aspergillus fumigatus