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Literature summary for 1.2.1.11 extracted from

  • Mank, N.; Pote, S.; Majorek, K.; Arnette, A.; Klapper, V.; Hurlburt, B.; Chruszcz, M.
    Structure of aspartate beta-semialdehyde dehydrogenase from Francisella tularensis (2018), Acta Crystallogr. Sect. F, 74, 14-22 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.1.11

Cloned(Commentary)

Cloned (Comment) Organism
gene asd, sequence comparisons, recombinant expression of N-terminal His6-tagged enzyme in Escherichia coli strain BL21(DE3) Francisella tularensis subsp. tularensis

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme, X-ray diffractions structure determination and analysis at 2.45 A resolution Francisella tularensis subsp. tularensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate 4-semialdehyde + phosphate + NADP+ Francisella tularensis subsp. tularensis
-
 L-4-aspartyl phosphate + NADPH + H+
-
 r
L-aspartate 4-semialdehyde + phosphate + NADP+ Francisella tularensis subsp. tularensis Schu 4
-
 L-4-aspartyl phosphate + NADPH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Francisella tularensis subsp. tularensis Q5NHM4
-
-
Francisella tularensis subsp. tularensis Schu 4 Q5NHM4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate 4-semialdehyde + phosphate + NADP+
-
 Francisella tularensis subsp. tularensis L-4-aspartyl phosphate + NADPH + H+
-
 r
L-aspartate 4-semialdehyde + phosphate + NADP+
-
 Francisella tularensis subsp. tularensis Schu 4 L-4-aspartyl phosphate + NADPH + H+
-
 r

Subunits

Subunits Comment Organism
dimer the central part of the dimerization domain is a sixstranded beta-sheet consisting of two pairs of parallel beta-strands flanking two central antiparallel strands. The sheets are oriented parallel to the sheet of the second subunit so that many interactions can occur between the side chains of nearby residues. Hydrogen bonds are formed between Thr257 and Asn157, between the two Ser159 residues, and between Tyr161 and the carbonyl O atom of Thr160. A buried hydrophobic patch is also formed by Ile260, Phe341 and Ala273. There are two highly charged regions at opposite ends of the beta-sheet. The subunit assembly aligns these highly charged regions in the dimer. These patches are formed by residues 327-336 of a loop in the beta-sheet and residues 214-236 of the arm. A series of salt bridges are formed in this region by Arg327, Glu238, Lys329, Asp258 and His339 Francisella tularensis subsp. tularensis

Synonyms

Synonyms Comment Organism
ASADH
-
 Francisella tularensis subsp. tularensis
aspartate beta-semialdehyde dehydrogenase
-
 Francisella tularensis subsp. tularensis
FtASADH
-
 Francisella tularensis subsp. tularensis

Cofactor

Cofactor Comment Organism Structure
NADP+ binding structure at the active site, structure analysis, overview Francisella tularensis subsp. tularensis
NADPH
-
 Francisella tularensis subsp. tularensis

General Information

General Information Comment Organism
additional information active site of FtASADH and NADP+ binding, structure analysis, overview Francisella tularensis subsp. tularensis
physiological function aspartate beta-semialdehyde dehydrogenase (ASADH) catalyzes the conversion of phosphoaspartate to aspartate beta-semialdehyde (L-ASA) via reductive dephosphorylation using NADPH as a cofactor Francisella tularensis subsp. tularensis