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Literature summary extracted from

  • Dahal, G.; Viola, R.E.
    Structure of a fungal form of aspartate semialdehyde dehydrogenase from Cryptococcus neoformans (2015), Acta Crystallogr. Sect. F, 71, 1365-1371 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment 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 Cloned (Comment) 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 (Comment) 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] Comment 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment 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 Purification (Comment) 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Subunits

EC Number Subunits Comment 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

Synonyms

EC Number Synonyms Comment Organism
1.2.1.11 ASADH
-
 Cryptococcus neoformans var. neoformans
1.2.1.11 CNA02450
-
 Cryptococcus neoformans var. neoformans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.11 8.6
-
 assay at Cryptococcus neoformans var. neoformans

Cofactor

EC Number Cofactor Comment 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

General Information

EC Number General Information Comment 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