EC Number   |
General Information |
Reference |
|---|
    5.1.1.13 | evolution |
the enzyme belongs to the serine/aspartate racemase family, the triple serine loop region regulates the aspartate racemase activity of the serine/aspartate racemase family members. The ancestral gene of the serine/aspartate racemase family is SerR, the evolution of AspR from SerR occured in three steps: first, gene duplication of the original SerR gene. Second, introduction of the two serine residues at position 151 and 152, resulting in a drastic increase of the AspR activity, and third, formation of the complete triple serine loop region by additional introduction of serine residue at position 150, resulting in enhanced the enzyme specificity for aspartate |
746724 |
| 5.1.1.13 | evolution |
the essential cysteine residues are conserved as Cys83 and Cys194 |
-, 747721 |
| 5.1.1.13 | malfunction |
D-aspartate contents of wild-type and Got1l1 knockout mice are not significantly different in the testis and hippocampus. The recombinant Got1l1 expressed in mammalian cells shows L-aspartate aminotransferase activity, but lacks aspartate racemase activity |
746719 |
| 5.1.1.13 | malfunction |
depletion of aspartate racemase by retrovirus-mediated expression of short-hairpin RNA in newborn neurons of the adult hippocampus elicits profound defects in the dendritic development and survival of newborn neurons and survival |
706558 |
| 5.1.1.13 | malfunction |
knockdown of Got1l1 does not reduce the total D-Asp content of the cells and their culture medium |
746721 |
| 5.1.1.13 | malfunction |
retrovirus-mediated expression of short-hairpin RNA complementary to aspartate racemase in newborn neurons of the hippocampus results in a defect in dendritic development and impaired survival of the newborn neurons |
728034 |
| 5.1.1.13 | malfunction |
substituting the triple serine loop region in AspRs enhances serine racemization |
746724 |
| 5.1.1.13 | malfunction |
substituting the triple serine loop region in AspRs enhances serine racemization. Single amino acid substitution mutants, H150S, P151S and N152S, reveal several effects on activity. The Ser150 substitution decreases all enzyme activities, especially the serine dehydrogenase (SDH) activity, while Ser151 dramatically increases the SerR and AspR activities with no change on SDH activity. An increase in the AspR activity is observed after introducing Ser152, while there is little or no change in the other activities |
746724 |
| 5.1.1.13 | metabolism |
because Picrophilus aspartate racemase is highly specific to aspartate, other amino acid racemases might exist in Picrophilus torridus |
-, 747720 |
| 5.1.1.13 | metabolism |
enzyme Got1l1 is not the major aspartate racemase, there might be another D-aspartate-synthesizing enzyme |
746719 |
