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Structure of a fungal form of aspartate semialdehyde dehydrogenase from Cryptococcus neoformans

Dahal, G.; Viola, R.E.; Acta Crystallogr. Sect. F 71, 1365-1371 (2015)

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
Cryptococcus neoformans var. neoformans
Cloned(Commentary)
EC Number
Commentary
Organism
1.2.1.11
gene CNA02450, codon-optimized, recombinant expression of C-terminally His-tagged enzyme ASADH in Escherichia coli strain BL21(DE3)
Cryptococcus neoformans var. neoformans
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 9 mg/ml protein solution with reservoir solution containing 10% PEG 8000, 6% ethylene glycol, 0.1 M HEPES pH 7.5, in a 2:1 ration, at 20°C, crystals are cocrystallized with 4 mM NADP+, X-ray diffraction structure determination and analysis at 2.6 A resolution, modeling by molecular replacement
Cryptococcus neoformans var. neoformans
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.2.1.11
160000
-
recombinant His-tagged enzyme, gel filtration
Cryptococcus neoformans var. neoformans
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+
Cryptococcus neoformans var. neoformans
-
L-4-aspartyl phosphate + NADPH + H+
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
Cryptococcus neoformans var. neoformans ATCC MYA-565
-
L-4-aspartyl phosphate + NADPH + H+
-
-
r
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.1.11
Cryptococcus neoformans var. neoformans
Q5KPK7
serotype D
-
1.2.1.11
Cryptococcus neoformans var. neoformans ATCC MYA-565
Q5KPK7
serotype D
-
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 chromatography, dialysis, and ultrafiltration
Cryptococcus neoformans var. neoformans
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+
-
741535
Cryptococcus neoformans var. neoformans
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
741535
Cryptococcus neoformans var. neoformans ATCC MYA-565
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
Subunits
EC Number
Subunits
Commentary
Organism
1.2.1.11
More
enzyme secondary structure, crystal structure analysis and comparisons, the C-terminal domain consists of six beta-strands, six alpha-helices and a single 310-helix that represent the catalytic site and the dimerization interface, detailed overview
Cryptococcus neoformans var. neoformans
1.2.1.11
tetramer
dimer of dimers, 4 * 40000, about, recombinant His-tagged enzyme, SDS-PAGE
Cryptococcus neoformans var. neoformans
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.2.1.11
8.6
-
assay at
Cryptococcus neoformans var. neoformans
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
the NADP+-binding domain consists of mixed beta-strands flanked on both sides with alpha-helices, with seven beta-strands, five alpha-helices and two 310-helices
Cryptococcus neoformans var. neoformans
1.2.1.11
NADPH
-
Cryptococcus neoformans var. neoformans
Application (protein specific)
EC Number
Application
Commentary
Organism
1.2.1.11
drug development
the enzyme is a validated target for antimicrobial drug design
Cryptococcus neoformans var. neoformans
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.2.1.11
gene CNA02450, codon-optimized, recombinant expression of C-terminally His-tagged enzyme ASADH in Escherichia coli strain BL21(DE3)
Cryptococcus neoformans var. neoformans
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
the NADP+-binding domain consists of mixed beta-strands flanked on both sides with alpha-helices, with seven beta-strands, five alpha-helices and two 310-helices
Cryptococcus neoformans var. neoformans
1.2.1.11
NADPH
-
Cryptococcus neoformans var. neoformans
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 9 mg/ml protein solution with reservoir solution containing 10% PEG 8000, 6% ethylene glycol, 0.1 M HEPES pH 7.5, in a 2:1 ration, at 20°C, crystals are cocrystallized with 4 mM NADP+, X-ray diffraction structure determination and analysis at 2.6 A resolution, modeling by molecular replacement
Cryptococcus neoformans var. neoformans
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.2.1.11
160000
-
recombinant His-tagged enzyme, gel filtration
Cryptococcus neoformans var. neoformans
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+
Cryptococcus neoformans var. neoformans
-
L-4-aspartyl phosphate + NADPH + H+
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
Cryptococcus neoformans var. neoformans ATCC MYA-565
-
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 chromatography, dialysis, and ultrafiltration
Cryptococcus neoformans var. neoformans
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+
-
741535
Cryptococcus neoformans var. neoformans
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
741535
Cryptococcus neoformans var. neoformans ATCC MYA-565
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.2.1.11
More
enzyme secondary structure, crystal structure analysis and comparisons, the C-terminal domain consists of six beta-strands, six alpha-helices and a single 310-helix that represent the catalytic site and the dimerization interface, detailed overview
Cryptococcus neoformans var. neoformans
1.2.1.11
tetramer
dimer of dimers, 4 * 40000, about, recombinant His-tagged enzyme, SDS-PAGE
Cryptococcus neoformans var. neoformans
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.2.1.11
8.6
-
assay at
Cryptococcus neoformans var. neoformans
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
Cryptococcus neoformans var. neoformans
1.2.1.11
additional information
The structure of CnASADH belongs to the Rossmann-fold superfamily of pyridine-linked dehydrogenases and shares the same overall monomeric structural features as the other ASADHs for which structures are determined
Cryptococcus neoformans var. neoformans
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
Cryptococcus neoformans var. neoformans
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
Cryptococcus neoformans var. neoformans
1.2.1.11
additional information
The structure of CnASADH belongs to the Rossmann-fold superfamily of pyridine-linked dehydrogenases and shares the same overall monomeric structural features as the other ASADHs for which structures are determined
Cryptococcus neoformans var. neoformans
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
Cryptococcus neoformans var. neoformans