Cloned (Comment) | Organism |
---|---|
gene racX, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) pLysS | Bacillus subtilis |
gene ygeA, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) pLysS | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics, Hanes-Woolf plots | Escherichia coli | |
additional information | - |
additional information | kinetics, Hanes-Woolf plots | Bacillus subtilis | |
25.1 | - |
D-homoserine | pH 8.5, 37°C, recombinant enzyme | Escherichia coli | |
27.9 | - |
L-lysine | pH 8.5, 37°C, recombinant enzyme | Bacillus subtilis | |
69.3 | - |
D-Lysine | pH 8.5, 37°C, recombinant enzyme | Bacillus subtilis | |
171 | - |
L-homoserine | pH 8.5, 37°C, recombinant enzyme | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | P32960 | - |
- |
Bacillus subtilis 168 | P32960 | - |
- |
Escherichia coli | P03813 | - |
- |
Escherichia coli K-12 / MG1655 | P03813 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) pLysS by nickel affinity chromatography | Escherichia coli |
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) pLysS by nickel affinity chromatography | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-arginine | 78.1% activity compared to LL-diaminopimelate | Bacillus subtilis | L-arginine | - |
r | |
D-homoserine | high activity with 75% of the activity in the other direction | Escherichia coli | L-homoserine | - |
r | |
D-lysine | 93.5% activity compared to LL-diaminopimelate | Bacillus subtilis | L-lysine | - |
r | |
D-methionine | 4.8% activity compared to L-homoserine | Escherichia coli | L-methionine | - |
r | |
D-ornithine | 46.7% activity compared to LL-diaLinopimelate | Bacillus subtilis | L-ornithine | - |
r | |
L-alanine | 0.9% activity compared to L-homoserine | Escherichia coli | D-alanine | - |
r | |
L-alanine | 25.9% activity compared to LL-diaminopimelate | Bacillus subtilis | D-alanine | - |
r | |
L-aminobutyrate | 4.0% activity compared to LL-diaminopimelate | Bacillus subtilis | D-aminobutyrate | - |
r | |
L-aminobutyrate | 4.6% activity compared to L-homoserine | Escherichia coli | D-aminobutyrate | - |
r | |
L-arginine | 90.5% activity compared to LL-diaminopimelate | Bacillus subtilis | D-arginine | - |
r | |
L-asparagine | 10.3% activity compared to LL-diaminopimelate | Bacillus subtilis | D-asparagine | - |
r | |
L-asparagine | 4.9% activity compared to L-homoserine | Escherichia coli | D-asparagine | - |
r | |
L-glutamine | 0.7% activity compared to L-homoserine | Escherichia coli | D-glutamine | - |
r | |
L-glutamine | 14.4% activity compared to LL-diaminopimelate | Bacillus subtilis | D-glutamine | - |
r | |
L-histidine | 32.1% activity compared to LL-diaminopimelate | Bacillus subtilis | D-histidine | - |
r | |
L-histidine | 7.9% activity compared to L-homoserine | Escherichia coli | D-histidine | - |
r | |
L-homoserine | best substrate | Escherichia coli | D-homoserine | - |
r | |
L-homoserine | 9.3% activity compared to LL-diaminopimelate | Bacillus subtilis | D-homoserine | - |
r | |
L-homoserine | 9.3% activity compared to LL-diaminopimelate | Bacillus subtilis 168 | D-homoserine | - |
r | |
L-homoserine | best substrate | Escherichia coli K-12 / MG1655 | D-homoserine | - |
r | |
L-isoleucine | 3.9% activity compared to L-homoserine | Escherichia coli | D-isoleucine | - |
r | |
L-leucine | 6.6% activity compared to L-homoserine | Escherichia coli | D-leucine | - |
r | |
L-lysine | 81.2% activity compared to LL-diaminopimelate | Bacillus subtilis | D-lysine | - |
r | |
L-Methionine | 13.1% activity compared to LL-diaminopimelate | Bacillus subtilis | D-Methionine | - |
r | |
L-Methionine | 6.0% activity compared to L-homoserine | Escherichia coli | D-Methionine | - |
r | |
L-Methionine | 7.9% activity compared to L-homoserine | Escherichia coli | D-Methionine | - |
r | |
L-Methionine | 6.0% activity compared to L-homoserine | Escherichia coli K-12 / MG1655 | D-Methionine | - |
r | |
L-Norleucine | 1.2% activity compared to L-homoserine | Escherichia coli | D-Norleucine | - |
r | |
L-Norleucine | 5.6% activity compared to LL-diaminopimelate | Bacillus subtilis | D-Norleucine | - |
r | |
L-Norleucine | 5.6% activity compared to LL-diaminopimelate | Bacillus subtilis 168 | D-Norleucine | - |
r | |
L-Norleucine | 1.2% activity compared to L-homoserine | Escherichia coli K-12 / MG1655 | D-Norleucine | - |
r | |
L-Norvaline | 3.6% activity compared to LL-diaminopimelate | Bacillus subtilis | D-Norvaline | - |
r | |
L-Norvaline | 5.8% activity compared to L-homoserine | Escherichia coli | D-Norvaline | - |
r | |
L-Norvaline | 3.6% activity compared to LL-diaminopimelate | Bacillus subtilis 168 | D-Norvaline | - |
r | |
L-Norvaline | 5.8% activity compared to L-homoserine | Escherichia coli K-12 / MG1655 | D-Norvaline | - |
r | |
L-Ornithine | 86.2% activity compared to LL-diaminopimelate | Bacillus subtilis | D-Ornithine | - |
r | |
L-Ornithine | 86.2% activity compared to LL-diaminopimelate | Bacillus subtilis 168 | D-Ornithine | - |
r | |
L-phenylalanine | 0.6% activity compared to L-homoserine | Escherichia coli | D-phenylalanine | - |
r | |
L-phenylalanine | 21.9% activity compared to LL-diaminopimelate | Bacillus subtilis | D-phenylalanine | - |
r | |
L-serine | 1.5% activity compared to L-homoserine | Escherichia coli | D-serine | - |
r | |
L-serine | 19.1% activity compared to LL-diaminopimelate | Bacillus subtilis | D-serine | - |
r | |
L-tyrosine | 22.8% activity compared to LL-diaminopimelate | Bacillus subtilis | D-tyrosine | - |
r | |
L-valine | 6.2% activity compared to L-homoserine | Escherichia coli | D-valine | - |
r | |
LL-diaminopimelate | best substrate | Bacillus subtilis | meso-diaminopimelate | - |
r | |
LL-diaminopimelate | 0.7% activity compared to L-homoserine | Escherichia coli | meso-diaminopimelate | - |
r | |
additional information | 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 | Bacillus subtilis | ? | - |
? | |
additional information | enzyme YgeA displays broad substrate specificity but low catalytic activity. YgeA preferentially catalyzes the racemization of homoserine. Histochemic product analysis and quantification by HPLC and spectroscopy | Escherichia coli | ? | - |
? | |
additional information | 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 | Bacillus subtilis 168 | ? | - |
? | |
additional information | enzyme YgeA displays broad substrate specificity but low catalytic activity. YgeA preferentially catalyzes the racemization of homoserine. Histochemic product analysis and quantification by HPLC and spectroscopy | Escherichia coli K-12 / MG1655 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | quaternary structure analysis of the enzyme using BN-PAGE, overview | Escherichia coli |
More | quaternary structure analysis of the enzyme using BN-PAGE, overview | Bacillus subtilis |
Synonyms | Comment | Organism |
---|---|---|
broad-spectrum amino acid racemase | - |
Escherichia coli |
broad-spectrum amino acid racemase | - |
Bacillus subtilis |
PLP-independent amino acid racemase | - |
Escherichia coli |
PLP-independent amino acid racemase | - |
Bacillus subtilis |
RacX | - |
Bacillus subtilis |
YgeA | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
- |
Escherichia coli |
37 | - |
- |
Bacillus subtilis |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | 45 | activity range, RacX shows less than half of the activity at 37°C, almost inactive at 50°C, profile overview | Bacillus subtilis |
25 | 50 | activity range, activity increases from 25°C to 37°C and is highest at 37°C. Activity decreases from 40°C to 50°C, and is almost absent at 55°C, profile overview | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0013 | - |
L-lysine | pH 8.5, 37°C, recombinant enzyme | Bacillus subtilis | |
0.0037 | - |
D-Lysine | pH 8.5, 37°C, recombinant enzyme | Bacillus subtilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
- |
Escherichia coli |
8.5 | - |
assay at | Bacillus subtilis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
7 | 10 | activity range, over 50% of maximal activity at pH 8.0-9.5, profile overview | Escherichia coli |
7.5 | 9.5 | activity range, profile overview | Bacillus subtilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | pyridoxal 5'-phosphate is not required by the enzyme | Escherichia coli | |
additional information | pyridoxal 5'-phosphate is not required by the enzyme | Bacillus subtilis |
General Information | Comment | Organism |
---|---|---|
additional information | conformational structure modeling of RacX based on the structure of Asp racemase from Pyrococcus horikoshi, PDB ID 1JFL | Bacillus subtilis |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.000047 | - |
L-lysine | pH 8.5, 37°C, recombinant enzyme | Bacillus subtilis | |
0.000054 | - |
D-Lysine | pH 8.5, 37°C, recombinant enzyme | Bacillus subtilis |