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Literature summary for 5.1.1.18 extracted from

  • Neidle, A.; Dunlop, D.S.
    Allosteric regulation of mouse brain serine racemase (2002), Neurochem. Res., 27, 1719-1724.
    View publication on PubMed
Search for more literature for 5.1.1.18

Activating Compound

Activating Compound Comment Organism Structure
ADP
-
 Mus musculus
ATP 1 mM, decrease of Km-value for racemization by 85%, allosteric mechanism. Inhibitory to L-serine O-sulfate dehydration reaction Mus musculus
GTP
-
 Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8
-
 L-serine racemization reaction, isoform A, pH 8.6, 37°C Mus musculus
13
-
 L-serine racemization reaction, isoform A, presence of ATP, pH 8.6, 37°C Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ may partially replace Mg2+ Mus musculus
Mg2+ required by both isoforms A and B Mus musculus
Mn2+ may partially replace Mg2+ Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
 isoforms A and B, gel filtration Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
 isoforms A and B, bifunctional enzymes, racemization of serine and elimination of L-serine and L-serine-O-sulfate to form pyruvate
-

Purification (Commentary)

Purification (Comment) Organism
both isoforms A and B Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine
-
 Mus musculus pyruvate + NH3
-
 ?
L-serine
-
 Mus musculus D-serine
-
 r
L-serine O-sulfate
-
 Mus musculus O-sulfopyruvate + NH3
-
 ?