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Literature summary for 5.1.1.13 extracted from

  • Abe, K.; Takahashi, S.; Muroki, Y.; Kera, Y.; Yamada, R.
    Cloning and expression of the pyridoxal 5-phosphate-dependent aspartate racemase gene from the bivalve mollusk Scapharca broughtonii and characterization of the recombinant enzyme (2006), J. Biochem., 139, 235-244.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ADP 10 mM ADP increases the activity to 320% of the control Anadara broughtonii
AMP 10 mM AMP increases the activity to 399% of the control Anadara broughtonii

Cloned(Commentary)

Cloned (Comment) Organism
cloned in Escherichia coli Anadara broughtonii

Protein Variants

Protein Variants Comment Organism
additional information the cDNA included an open reading frame of 1017 bp encoding a protein of 338 amino acids, and the deduced amino acid sequence contains a pyridoxal 5'-phosphate-binding motif Anadara broughtonii

Inhibitors

Inhibitors Comment Organism Structure
ATP 10 mM ATP decreases the activity to 23% Anadara broughtonii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
14.5
-
L-aspartate
-
Anadara broughtonii
17.2
-
D-Aspartate
-
Anadara broughtonii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37100
-
predicted from cDNA Anadara broughtonii

Organism

Organism UniProt Comment Textmining
Anadara broughtonii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
aspartate racemase is purified from the Scapharca broughtonii foot muscle by a procedure that includes sodium sulfate fractionation and blue sepharose column chromatography. The purified enzyme (225 mg) is digested at 25°C for 12 h with 80 mg of lysyl endopeptidase in a reaction mixture comprising 50 mM Tris-HCl, pH 8.0, containing 2 M guanidine hydrochloride, and the resulting peptides is resolved by reverse phase high performance liquid chromatography on a capcell Pac C-8 column (0.2 mm x 15 cm) using an acetonitrile gradient in 0.06% trifluoroacetic acid Anadara broughtonii

Reaction

Reaction Comment Organism Reaction ID
L-aspartate = D-aspartate the enzyme racemizes only aspartate and no other amino acids but the enzyme also shows a dehydratase activity toward L-threo-3-hydroxyaspartate Anadara broughtonii

Source Tissue

Source Tissue Comment Organism Textmining
foot muscle enzyme is purified from foot muscle of Scapharca broughtonii Anadara broughtonii
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate
-
Anadara broughtonii D-aspartate
-
r

Synonyms

Synonyms Comment Organism
Aspartate racemase
-
Anadara broughtonii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Anadara broughtonii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Anadara broughtonii

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate this enzyme is the first aspartate racemase purified from animal tissues and unique in its pyridoxal 5'-phosphate (PLP)–dependence in contrast to microbial aspartate racemases characterized so far Anadara broughtonii