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Literature summary extracted from

  • Hoffman, H.E.; Jiraskova, J.; Cigler, P.; Sanda, M.; Schraml, J.; Konvalinka, J.
    Hydroxamic acids as a novel family of serine racemase inhibitors: mechanistic analysis reveals different modes of interaction with the pyridoxal-5'-phosphate cofactor (2009), J. Med. Chem., 52, 6032-6041.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.1.1.18 ATP
-
 Mus musculus
5.1.1.18 DTT
-
 Mus musculus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.1.18 enzyme expression in Escherichia coli strain MC1061 Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.1.18 Acetohydroxamic acid i.e. Lithostat Mus musculus
5.1.1.18 adipodihydroxamic acid
-
 Mus musculus
5.1.1.18 DL-Serine hydroxamate
-
 Mus musculus
5.1.1.18 DL-Threonine hydroxamate
-
 Mus musculus
5.1.1.18 glutarodihydroxamic acid
-
 Mus musculus
5.1.1.18 glycine
-
 Mus musculus
5.1.1.18 Glycine hydroxamate
-
 Mus musculus
5.1.1.18 L-aspartic acid
-
 Mus musculus
5.1.1.18 L-aspartic acid beta-hydroxamate a competitive and selective serine racemase inhibitor Mus musculus
5.1.1.18 malonodihydroxamic acid
-
 Mus musculus
5.1.1.18 additional information small aliphatic hydroxamic acids as potent serine racemase inhibitors, interaction with the pyridoxal-5'-phosphate cofactor, mechanistic analysis, overview. Some of these hydroxamic acids can act as nonspecific inhibitors of pyridoxal 5'-phosphate-dependent enzymes, the nonspecific effect is likely due to irreversible interaction of the hydroxamic acid moiety with pyridoxal 5'-phosphate to form aldoxime species Mus musculus
5.1.1.18 oxalodihydroxamic acid
-
 Mus musculus
5.1.1.18 suberodihydroxamic acid
-
 Mus musculus
5.1.1.18 succinodihydroxamic acid
-
 Mus musculus
5.1.1.18 vorinostat i.e. Zolinza Mus musculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.1.18 Mg2+ activates, but is not involved in enzyme inhibition by hydroxamic acids Mus musculus

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 Mus musculus
-
 D-serine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.18 Mus musculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.18 recombinant enzyme from Escherichia coli strain MC1061 by hydrophobic interaction and anion exchange chromatography, followed by ATP affinity chromatography and dialysis Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.18 L-serine
-
 Mus musculus D-serine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.1.1.18 SRR
-
 Mus musculus

Temperature Optimum [°C]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.1.18 8
-
 assay at Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
5.1.1.18 pyridoxal 5'-phosphate dependent on Mus musculus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
5.1.1.18 1.3
-
 L-aspartic acid beta-hydroxamate pH 8.0 Mus musculus
5.1.1.18 1.64
-
 glycine pH 8.0 Mus musculus
5.1.1.18 1.9
-
 L-aspartic acid pH 8.0 Mus musculus

General Information

EC Number General Information Comment Organism
5.1.1.18 physiological function the enzyme is responsible for the biosynthesis of the neurotransmitter D-serine, which activates N-methyl-D-aspartate receptors in the central nervous system Mus musculus