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Literature summary for 5.1.1.18 extracted from

  • Ito, T.; Maekawa, M.; Hayashi, S.; Goto, M.; Hemmi, H.; Yoshimura, T.
    Catalytic mechanism of serine racemase from Dictyostelium discoideum (2013), Amino Acids, 44, 1073-1084.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression oof wild-type and mutant enzyme in Escherichia coli strain Rosetta 2 (DE3) Dictyostelium discoideum

Protein Variants

Protein Variants Comment Organism
H84A site-directed mutagenesis, the mutant shows reduced racemase and dehydrase activities compared to the wild-type enzyme Dictyostelium discoideum
K111A site-directed mutagenesis, the mutant shows reduced racemase and dehydrase activities compared to the wild-type enzyme Dictyostelium discoideum
K56A site-directed mutagenesis, catalytically inactive mutant Dictyostelium discoideum
additional information circular dichroism spectral analysis of wild-type and mutant enzymes, overview Dictyostelium discoideum
P150S site-directed mutagenesis, the mutant shows reduced racemase and dehydrase activities compared to the wild-type enzyme Dictyostelium discoideum
R132A site-directed mutagenesis, the mutant shows reduced racemase and dehydrase activities compared to the wild-type enzyme Dictyostelium discoideum
S80A site-directed mutagenesis, catalytically inactive mutant Dictyostelium discoideum
S80C site-directed mutagenesis, the mutant shows reduced racemase and dehydrase activities compared to the wild-type enzyme Dictyostelium discoideum
S81A site-directed mutagenesis, Ser81 is located on the opposite side of K56, the mutation converts the enzyme from serine racemase to L-serine dehydrase, the mutant shows no racemase activity and has significantly reduced D-serine dehydrase activity, but it completely retains its L-serine dehydrase activity Dictyostelium discoideum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-serine Dictyostelium discoideum
-
D-serine
-
r

Organism

Organism UniProt Comment Textmining
Dictyostelium discoideum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-serine = D-serine the abstraction and addition of alpha-hydrogen to L- and D-serine are conducted by residues K56 and S81 at the si- and re-sides, respectively, of pyridoxal 5'-phosphate, K56 functions as a residue that abstracts the alpha-hydrogen from the Schiff base intermediate, two-base catalytic mechanism, overview Dictyostelium discoideum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine
-
Dictyostelium discoideum D-serine
-
r
additional information the enzyme catalyzes racemization and dehydration of both isomers of serine Dictyostelium discoideum ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Dictyostelium discoideum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Dictyostelium discoideum

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on, binding residue is Lys56 Dictyostelium discoideum

General Information

General Information Comment Organism
evolution the eukaryotic serine racemase from Dictyostelium discoideum is a fold-type II pyridoxal 5'-phosphate-dependent enzyme Dictyostelium discoideum
additional information circular dichroism spectral analysis of wild-type and mutant enzymes, overview Dictyostelium discoideum