Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.1.1.18 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

Inhibitors

Inhibitors Comment Organism Structure
Dihydroxyfumarate
-
Mus musculus
glycine competitive Mus musculus
L-asparagine
-
Mus musculus
L-cysteine-S-sulfate
-
Mus musculus
L-erythro-3-hydroxyaspartate
-
Mus musculus
Maleate
-
Mus musculus
malonate
-
Mus musculus
meso-tartrate
-
Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.49
-
L-serine O-sulfate pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction Mus musculus
3.2
-
D-serine pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction Mus musculus
3.8
-
L-serine pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction Mus musculus
4
-
L-serine pH 8.0, 37°C, presence of 1 mM ATP, elimination 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 Q9QZX7 bifunctional enzyme, racemization of serine and elimination of L-serine and L-serine-O-sulfate to form pyruvate
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-serine
-
Mus musculus pyruvate + NH3
-
?
D-serine
-
Mus musculus L-serine
-
r
L-serine
-
Mus musculus pyruvate + NH3
-
?
L-serine
-
Mus musculus D-serine
-
r
L-serine O-sulfate
-
Mus musculus O-sulfopyruvate + NH3
-
?
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
0.49
-
L-serine O-sulfate pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction Mus musculus
3.2
-
D-serine pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction Mus musculus
3.8
-
L-serine pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction Mus musculus
4
-
L-serine pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction Mus musculus
14.5
-
D-serine pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction Mus musculus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.043
-
L-erythro-3-hydroxyaspartate pH 8.0, 37°C Mus musculus
0.071
-
malonate pH 8.0, 37°C Mus musculus
0.55
-
Maleate pH 8.0, 37°C Mus musculus
0.64
-
L-cysteine-S-sulfate pH 8.0, 37°C Mus musculus
0.66
-
meso-tartrate pH 8.0, 37°C Mus musculus
0.69
-
Dihydroxyfumarate pH 8.0, 37°C Mus musculus
1.13
-
L-asparagine pH 8.0, 37°C Mus musculus
1.64
-
glycine pH 8.0, 37°C Mus musculus