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Literature summary for 5.1.1.10 extracted from

  • Strisovsky, K.; Jiraskova, J.; Mikulova, A.; Rulisek, L.; Konvalinka, J.
    Dual substrate and reaction specificity in mouse serine racemase: identification of high-affinity dicarboxylate substrate and inhibitors and analysis of the beta-eliminase activity (2005), Biochemistry, 44, 13091-13100.
    View publication on PubMed
Search for more literature for 5.1.1.10

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.8
-
 L-serine pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction Mus musculus
14.5
-
 D-serine pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36121
-
 x * 36121, MALDI-MS, x * 36123, calculated Mus musculus
36123
-
 x * 36121, MALDI-MS, x * 36123, calculated Mus musculus

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-serine
-
 Mus musculus L-serine
-
 r
L-serine
-
 Mus musculus D-serine
-
 r
additional information racemization and elimination activities reside at the same active site of enzyme. Racemization activity is specific to serine, elimination activity has a broader specificity for L-amino acids with a suitable leaving group at the beta-carbon Mus musculus ?
-
 ?

Subunits

Subunits Comment Organism
? x * 36121, MALDI-MS, x * 36123, calculated Mus musculus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.8
-
 L-serine pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction Mus musculus
14.5
-
 D-serine pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction Mus musculus