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Literature summary for 5.1.1.18 extracted from

  • Nitoker, N.; Major, D.T.
    Understanding the reaction mechanism and intermediate stabilization in mammalian serine racemase using multiscale quantum-classical simulations (2015), Biochemistry, 54, 516-527 .
    View publication on PubMed
Search for more literature for 5.1.1.18

Application

Application Comment Organism
drug development the enzyme and enzyme mutants may serve as targets for future docking studies and drug design Homo sapiens
drug development the enzyme and enzyme mutants may serve as targets for future docking studies and drug design Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic analysis Homo sapiens
additional information
-
 additional information kinetic analysis Rattus norvegicus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9GZT4
-
-
Rattus norvegicus Q76EQ0
-
-

Reaction

Reaction Comment Organism Reaction ID
L-serine = D-serine analysis of the catalytic reaction mechanism and intermediate stabilization in mammalian serine racemase using multiscale quantum-classical simulations, hybrid quantum mechanics/molecular mechanics molecular dynamics simulations in conjunction with umbrella sampling are performed, overview. The unprotonated pyridoxal 5'-phosphate-substrate intermediate is stabilized mostly due to solvation effects contributed by water molecules and active-site residues, as well as long-range electrostatic interactions with the enzyme environment Homo sapiens
a
L-serine = D-serine analysis of the catalytic reaction mechanism and intermediate stabilization in mammalian serine racemase using multiscale quantum-classical simulations, hybrid quantum mechanics/molecular mechanics molecular dynamics simulations in conjunction with umbrella sampling are performed, overview. The unprotonated pyridoxal 5'-phosphate-substrate intermediate is stabilized mostly due to solvation effects contributed by water molecules and active-site residues, as well as long-range electrostatic interactions with the enzyme environment Rattus norvegicus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine
-
 Homo sapiens D-serine
-
 r
L-serine
-
 Rattus norvegicus D-serine
-
 r
additional information analysis of enzyme-substrate-cofactor interactions in the active site, overview Homo sapiens ?
-
 ?
additional information analysis of enzyme-substrate-cofactor interactions in the active site, overview Rattus norvegicus ?
-
 ?

Synonyms

Synonyms Comment Organism
SerR
-
 Homo sapiens
SerR
-
 Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Homo sapiens
pyridoxal 5'-phosphate
-
 Rattus norvegicus

General Information

General Information Comment Organism
additional information enzyme activity site structure, docking and modeling, overview Homo sapiens
additional information enzyme activity site structure, docking and modeling, overview Rattus norvegicus
physiological function serine racemase (SerR) is a pyridoxal 5'-phosphate-dependent enzyme catalyzing the racemization of L-Ser to D-Ser. In mammals, D-Ser is an endogenous coagonist required for the activation of N-methyl-D-aspartate receptors (NMDARs) Homo sapiens
physiological function serine racemase (SerR) is a pyridoxal 5'-phosphate-dependent enzyme catalyzing the racemization of L-Ser to D-Ser. In mammals, D-Ser is an endogenous coagonist required for the activation of N-methyl-D-aspartate receptors (NMDARs) Rattus norvegicus