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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
amino acid racemase, acl racemase, broad-spectrum amino acid racemase, broad specificity amino acid racemase, amino-acid racemase, broad substrate specificity amino acid racemase, gknsaar, n-succinylamino acid racemase, broad-specificity amino acid racemase,
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broad-spectrum amino acid racemase
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PLP-independent amino acid racemase
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L-Amino acid racemase
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Racemase, amino acid
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-, -, -, -, -, -, -, -, -, -
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amino-acid racemase
A pyridoxal-phosphate protein.
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D-arginine
L-arginine
78.1% activity compared to LL-diaminopimelate
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r
D-lysine
L-lysine
93.5% activity compared to LL-diaminopimelate
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r
D-ornithine
L-ornithine
46.7% activity compared to LL-diaLinopimelate
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r
L-alanine
D-alanine
25.9% activity compared to LL-diaminopimelate
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r
L-aminobutyrate
D-aminobutyrate
4.0% activity compared to LL-diaminopimelate
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r
L-arginine
D-arginine
90.5% activity compared to LL-diaminopimelate
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r
L-asparagine
D-asparagine
10.3% activity compared to LL-diaminopimelate
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r
L-glutamine
D-glutamine
14.4% activity compared to LL-diaminopimelate
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r
L-histidine
D-histidine
32.1% activity compared to LL-diaminopimelate
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r
L-homoserine
D-homoserine
9.3% activity compared to LL-diaminopimelate
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r
L-lysine
D-lysine
81.2% activity compared to LL-diaminopimelate
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r
L-Methionine
D-Methionine
13.1% activity compared to LL-diaminopimelate
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r
L-Norleucine
D-Norleucine
5.6% activity compared to LL-diaminopimelate
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r
L-Norvaline
D-Norvaline
3.6% activity compared to LL-diaminopimelate
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r
L-Ornithine
D-Ornithine
86.2% activity compared to LL-diaminopimelate
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r
L-phenylalanine
D-phenylalanine
21.9% activity compared to LL-diaminopimelate
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r
L-serine
D-serine
19.1% activity compared to LL-diaminopimelate
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r
L-tyrosine
D-tyrosine
22.8% activity compared to LL-diaminopimelate
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r
LL-diaminopimelate
meso-diaminopimelate
best substrate
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r
additional information
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enzyme RacX displays broad substrate specificity but low catalytic activity. RacX preferentially racemizes arginine, lysine, and ornithine. Histochemic product analysis and quantification by HPLC and spectroscopy
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additional information
pyridoxal 5'-phosphate is not required by the enzyme
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69.3
D-Lysine
pH 8.5, 37°C, recombinant enzyme
27.9
L-lysine
pH 8.5, 37°C, recombinant enzyme
additional information
additional information
kinetics, Hanes-Woolf plots
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0.0037
D-Lysine
pH 8.5, 37°C, recombinant enzyme
0.0013
L-lysine
pH 8.5, 37°C, recombinant enzyme
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0.000054
D-Lysine
pH 8.5, 37°C, recombinant enzyme
0.000047
L-lysine
pH 8.5, 37°C, recombinant enzyme
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7.5 - 9.5
activity range, profile overview
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25 - 45
activity range, RacX shows less than half of the activity at 37°C, almost inactive at 50°C, profile overview
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UniProt
brenda
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additional information
conformational structure modeling of RacX based on the structure of Asp racemase from Pyrococcus horikoshi, PDB ID 1JFL
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additional information
quaternary structure analysis of the enzyme using BN-PAGE, overview
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recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) pLysS by nickel affinity chromatography
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gene racX, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) pLysS
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Miyamoto, T.; Katane, M.; Saitoh, Y.; Sekine, M.; Homma, H.
Identification and characterization of novel broad-spectrum amino acid racemases from Escherichia coli and Bacillus subtilis
Amino Acids
49
1885-1894
2017
Escherichia coli (P03813), Bacillus subtilis (P32960), Bacillus subtilis 168 (P32960), Escherichia coli K-12 / MG1655 (P03813)
brenda
5.1.1.10 amino-acid racemase
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