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Literature summary for 5.1.1.18 extracted from

  • Hoffman, H.; Jiraskova¡, J.; Zvelebil, M.; Konvalinka, J.
    Random mutagenesis of human serine racemase reveals residues important for the enzymatic activity (2010), Collect. Czech. Chem. Commun., 75, 59-79.
No PubMed abstract available
Search for more literature for 5.1.1.18

Application

Application Comment Organism
drug development serine racemase inhibitors might be useful in treatment of neurodegenrative diseases Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information generation of enzyme mutants by random mutagenesis for determination of structurally and functionally important residues in the enzyme, e.g. S84 and P111, that are crucial for enzyme activity, and C217 and K221 that are important for Mg2+ binding and enzyme stability Homo sapiens

General Stability

General Stability Organism
enzyme residues C217 and K221 are important for Mg2+ binding and enzyme stability Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Homo sapiens 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ enzyme residues C217 and K221 are important for Mg2+ binding and enzyme stability Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-serine Homo sapiens
-
 D-serine
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine
-
 Homo sapiens D-serine
-
 ?
L-serine enzyme residues S84 and P111 are crucial for enzyme activity Homo sapiens D-serine
-
 ?

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on Homo sapiens

General Information

General Information Comment Organism
malfunction increased levels of enzyme-mediated D-serine production are associated with amyotrophic lateral sclerosis and Alzheimer's disease Homo sapiens
physiological function the enzyme is responsible for D-serine production in the central nervous system, where D-serine acts as a co-agonist of the N-methyl-D-aspartate receptor ion channels Homo sapiens