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Literature summary extracted from

  • Marchesani, F.; Bruno, S.; Paredi, G.; Raboni, S.; Campanini, B.; Mozzarelli, A.
    Human serine racemase is nitrosylated at multiple sites (2018), Biochim. Biophys. Acta, 1866, 813-821 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.1.1.18 ATP activates Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.1.18 sequence comparisons, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 CodonPlus (DE3)-RIL Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
5.1.1.18 C113S site-directed mutagenesis, the C113S mutant exhibits a KM for L-serine which is 3.5fold higher than for the wild-type enzyme and a 3.3fold lower specific activity. ATP binding to the mutant in the presence of L-serine occurs with a 5fold higher EC50 compared to wild-type, with conserved binding cooperativity. Phenotype, overview Homo sapiens
5.1.1.18 D318N site-directed mutagenesis Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.1.18 S-nitrosoglutathione GSNO, inhibition of human serine racemase by S-nitrosylation at Cys133, Cys128,and Cys269. The time-course is markedly biphasic, with a fast phase associated with the reaction of Cys113. The inhibition results from a conformational change rather than the direct displacement of ATP. Effect of nitrosylation on the cross-talk between ATP binding site and active site, both ATP and glycine bind to their respective sites with the same affinity regardless of the nitrosylation state Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.1.18 additional information
-
additional information kinetics of wild-type and mutant enzymes Homo sapiens
5.1.1.18 16
-
L-serine pH 8.0, 37°C, recombinant wild-type enzyme Homo sapiens
5.1.1.18 50
-
L-serine pH 8.0, 37°C, recombinant mutant D318N Homo sapiens
5.1.1.18 54
-
L-serine pH 8.0, 37°C, recombinant mutant C113S Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.1.18 Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.1.18 L-serine Homo sapiens
-
D-serine
-
r

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.18 Homo sapiens Q9GZT4
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
5.1.1.18 S-nitrosylation human serine racemase is nitrosylated at multiple sites, which inhibits the enzyme activity. Besides Cys113, two additional cysteine residues, Cys269, unique to the human orthologue, and Cys128, are recognized as S-nitrosylation sites through mass spectrometry and site-directed mutagenesis. S-nitrosylation produces a partial interruption of the cross-talk between the ATP binding site and the active site. The inhibition results from a conformational change rather than the direct displacement of ATP Homo sapiens

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.18 recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 CodonPlus (DE3)-RIL Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.18 L-serine
-
Homo sapiens D-serine
-
r

Subunits

EC Number Subunits Comment Organism
5.1.1.18 monomer crystal structure analysis, PDB ID 3L6B Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
5.1.1.18 hSR
-
Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.1.18 37
-
assay at Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.1.18 0.85
-
L-serine pH 8.0, 37°C, recombinant mutant C113S Homo sapiens
5.1.1.18 1.92
-
L-serine pH 8.0, 37°C, recombinant mutant D318N Homo sapiens
5.1.1.18 2.77
-
L-serine pH 8.0, 37°C, recombinant wild-type enzyme Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.1.18 8
-
assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
5.1.1.18 pyridoxal 5'-phosphate
-
Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
5.1.1.18 additional information
-
additional information biphasic inhibition kinetics via S-nitrosylation Homo sapiens

General Information

EC Number General Information Comment Organism
5.1.1.18 physiological function serine racemase is a pyridoxal 5'-phosphate dependent enzyme responsible for the synthesis of D-serine, a neuromodulator of the NMDA receptors. Its activity is modulated by several ligands, including ATP, divalent cations and protein interactors. The enzyme is negatively regulated by reversible S-nitrosylation of cysteine residues, C113, C128, and C269, overview Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.1.1.18 0.016
-
L-serine pH 8.0, 37°C, recombinant mutant C113S Homo sapiens
5.1.1.18 0.038
-
L-serine pH 8.0, 37°C, recombinant mutant D318N Homo sapiens
5.1.1.18 0.17
-
L-serine pH 8.0, 37°C, recombinant wild-type enzyme Homo sapiens