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Literature summary extracted from

  • Mizobuchi, T.; Nonaka, R.; Yoshimura, M.; Abe, K.; Takahashi, S.; Kera, Y.; Goto, M.
    Crystal structure of a pyridoxal 5'-phosphate-dependent aspartate racemase derived from the bivalve mollusc Scapharca broughtonii (2017), Acta Crystallogr. Sect. F, 73, 651-656 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.1.13 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Anadara broughtonii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.1.1.13 purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, mixing of 0.006 ml of 2.5 mg/ml protein in 10 mM Tris-HCl, 20 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, pH 8.8, with 0.003 ml of reservoir solution containing 27% w/v PEG 4000, 50 mM sodium acetate, pH 5.0, 200 mM ammonium acetate, and 15% v/v glycerol, and equilibration against 0.1 ml of reservoir solution, 14°C, X-ray diffraction structure determination and analysis at 1.90 A resolution Anadara broughtonii

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.1.13 malonate
-
 Anadara broughtonii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.1.13 L-aspartate Anadara broughtonii
-
 D-aspartate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.13 Anadara broughtonii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.13 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Anadara broughtonii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.13 L-aspartate
-
 Anadara broughtonii D-aspartate
-
 r
5.1.1.13 additional information SbAspR catalyzes both racemization and dehydration. Residue Arg140 recognizes the beta-carboxyl group of the substrate aspartate in SbAspR Anadara broughtonii ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.1.1.13 AspR
-
 Anadara broughtonii
5.1.1.13 SbAspR
-
 Anadara broughtonii

Cofactor

EC Number Cofactor Comment Organism Structure
5.1.1.13 pyridoxal 5'-phosphate dependent on Anadara broughtonii

General Information

EC Number General Information Comment Organism
5.1.1.13 additional information residue Arg140 recognizes the beta-carboxyl group of the substrate aspartate in SbAspR. The aromatic proline interaction between the domains, which favours the closed form of SbAspR, might influence the arrangement of Arg140 at the active site, active site structure of SbAspR, overview Anadara broughtonii
5.1.1.13 physiological function the enzyme is responsible for D-aspartate biosynthesis in vivo. Enzyme SbAspR is a type II PLP-dependent enzyme. D-Aspartate is one of the most abundant free D-amino acids present in the nervous and reproductive systems and plays important physiological roles, including regulating developmental processes, hormone secretion and steroidogenesis Anadara broughtonii