5.1.1.13: aspartate racemase
This is an abbreviated version!
For detailed information about aspartate racemase, go to the full flat file.
Word Map on EC 5.1.1.13
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5.1.1.13
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l-aspartate
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d-amino
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racemization
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asprs
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5'-phosphate-dependent
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horikoshii
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scapharca
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d-serine
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broughtonii
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d-forms
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d-enantiomer
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serrs
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plp-dependent
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d-glutamate
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mirror-symmetric
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food industry
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analysis
- 5.1.1.13
- l-aspartate
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d-amino
-
racemization
- asprs
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5'-phosphate-dependent
- horikoshii
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scapharca
- d-serine
- broughtonii
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d-forms
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d-enantiomer
- serrs
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plp-dependent
- d-glutamate
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mirror-symmetric
- food industry
- analysis
Reaction
Synonyms
Asp racemase, Aspartate racemase, AspR, D-Asp racemase, D-Aspartate racemase, GOT1L1, LsAspR, OCC_11152, P. AspR, PhAspR, PLP-independent AspR, PTO0149, PtoAspR, pyridoxal 5'-phosphate independent aspartate racemase, pyridoxal 5'-phosphate-independent aspartate racemase, Racemase, aspartate, SbAspR, Tl-AspR
ECTree
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General Information
General Information on EC 5.1.1.13 - aspartate racemase
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evolution
malfunction
metabolism
physiological function
additional information
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
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
evolution
JT020910
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
evolution
the essential cysteine residues are conserved as Cys83 and Cys194
evolution
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
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the essential cysteine residues are conserved as Cys83 and Cys194
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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
malfunction
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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
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
malfunction
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knockdown of Got1l1 does not reduce the total D-Asp content of the cells and their culture medium
malfunction
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knockdown of Got1l1 does not reduce the total D-Asp content of the cells and their culture medium
malfunction
substituting the triple serine loop region in AspRs enhances serine racemization
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
malfunction
JT020910
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
because Picrophilus aspartate racemase is highly specific to aspartate, other amino acid racemases might exist in Picrophilus torridus
metabolism
enzyme Got1l1 is not the major aspartate racemase, there might be another D-aspartate-synthesizing enzyme
metabolism
Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
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because Picrophilus aspartate racemase is highly specific to aspartate, other amino acid racemases might exist in Picrophilus torridus
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physiological function
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enzyme GOT1L1 contributes little, if at all, to the biosynthesis of D-Asp in human cells, relationships between the D-Asp content and expression levels of Got1l1 and Ddo mRNAs in cultured human cells
physiological function
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enzyme GOT1L1 contributes little, if at all, to the biosynthesis of D-Asp in rat cells, relationships between the D-Asp content and expression levels of Got1l1 and Ddo mRNAs in cultured rat cells, overview
physiological function
in the hippocampus, D-aspartate strongly enhances N-methyl-D-aspartate receptor-dependent long-term potentiation and is involved in learning and memory
physiological function
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the enzyme from the lactic acid bacterium Lactobacillus sakei NBRC 15893 is considered to be involved in D-aspartate synthesis during the brewing process of Japanese sake at low temperatures
physiological function
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the enzyme is responsible for D-aspartate biosynthesis in vivo. Enzyme SbAspR is a type II PLP-dependent enzyme. D-Aspartate is one of the most abundant free D-amino acids present in the nervous and reproductive systems and plays important physiological roles, including regulating developmental processes, hormone secretion and steroidogenesis
physiological function
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the enzyme from the lactic acid bacterium Lactobacillus sakei NBRC 15893 is considered to be involved in D-aspartate synthesis during the brewing process of Japanese sake at low temperatures
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amino acid analysis of cell-free extract, overview
additional information
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amino acid analysis of cell-free extract, overview
additional information
important role of triple serine loop region for the aspratate racemase activity in several SerRs and AspRs, structure-function analysis, overview
additional information
important role of triple serine loop region for the aspratate racemase activity in several SerRs and AspRs, structure-function analysis, overview
additional information
JT020910
important role of triple serine loop region for the aspratate racemase activity in several SerRs and AspRs, structure-function analysis, overview
additional information
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residue Arg140 recognizes the beta-carboxyl group of the substrate aspartate in SbAspR. The aromatic proline interaction between the domains, which favours the closed form of SbAspR, might influence the arrangement of Arg140 at the active site, active site structure of SbAspR, overview
additional information
Thermococcus litoralis ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
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amino acid analysis of cell-free extract, overview
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