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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic analysis | Homo sapiens | |
additional information | - |
additional information | kinetic analysis | Rattus norvegicus |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9GZT4 | - |
- |
Rattus norvegicus | Q76EQ0 | - |
- |
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 | |
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 |
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 | Comment | Organism |
---|---|---|
SerR | - |
Homo sapiens |
SerR | - |
Rattus norvegicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Homo sapiens | |
pyridoxal 5'-phosphate | - |
Rattus norvegicus |
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 |