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

BRENDA support

Literature summary for 5.1.1.18 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

Activating Compound Comment Organism Structure
ATP
-
Mus musculus
DTT
-
Mus musculus

Cloned(Commentary)

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

Inhibitors

Inhibitors Comment Organism Structure
Acetohydroxamic acid i.e. Lithostat Mus musculus
adipodihydroxamic acid
-
Mus musculus
DL-Serine hydroxamate
-
Mus musculus
DL-Threonine hydroxamate
-
Mus musculus
glutarodihydroxamic acid
-
Mus musculus
glycine
-
Mus musculus
Glycine hydroxamate
-
Mus musculus
L-aspartic acid
-
Mus musculus
L-aspartic acid beta-hydroxamate a competitive and selective serine racemase inhibitor Mus musculus
malonodihydroxamic acid
-
Mus musculus
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
oxalodihydroxamic acid
-
Mus musculus
suberodihydroxamic acid
-
Mus musculus
succinodihydroxamic acid
-
Mus musculus
vorinostat i.e. Zolinza Mus musculus

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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)

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

Synonyms

Synonyms Comment Organism
SRR
-
Mus musculus

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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

Ki Value [mM]

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

General Information

General Information Comment Organism
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