EC Number | Cloned (Comment) | Organism |
---|---|---|
5.1.1.13 | recombinant enzyme expression in Escherichia coli strain BL21(DE3) | Picrophilus torridus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
5.1.1.13 | purified recombinant enzyme, vapour diffusion method, mixing of 8-12 mg/ml protein in 50 mM Tris-HCl, pH 8.0, with reservoir solution containing 20-25% w/v PEG 3400, 200 mM potassium/sodium tartrate, and 1 mM L-aspartate, X-ray diffraction structure determination and analysis at 1.85 A resolution, molecular replacement method using the structure of aspartate racemase from Salmonella typhimurium, PDB ID 3S81, as a probe model | Picrophilus torridus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.1.1.13 | 8.275 | - |
L-aspartate | pH 4.6, 60°C, recombinant enzyme | Picrophilus torridus | |
5.1.1.13 | 11.11 | - |
D-Aspartate | pH 4.6, 60°C, recombinant enzyme | Picrophilus torridus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
5.1.1.13 | cytosol | - |
Picrophilus torridus | 5829 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.1.13 | L-aspartate | Picrophilus torridus | - |
D-aspartate | - |
r | |
5.1.1.13 | L-aspartate | Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 | - |
D-aspartate | - |
r | |
5.1.1.13 | additional information | Picrophilus torridus | Picrophilus torridus aspartate racemase is highly specific to aspartate | ? | - |
? | |
5.1.1.13 | additional information | Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 | Picrophilus torridus aspartate racemase is highly specific to aspartate | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.1.1.13 | Picrophilus torridus | Q6L2R8 | - |
- |
5.1.1.13 | Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 | Q6L2R8 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
5.1.1.13 | recombinant enzyme from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, hydrophobic interaction chromatography, dialysis anion change chromatography, and ultrafiltration | Picrophilus torridus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
5.1.1.13 | additional information | the optimal growth temperature is about 60°C | Picrophilus torridus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.1.13 | D-aspartate | - |
Picrophilus torridus | L-aspartate | - |
r | |
5.1.1.13 | D-aspartate | - |
Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 | L-aspartate | - |
r | |
5.1.1.13 | L-aspartate | - |
Picrophilus torridus | D-aspartate | - |
r | |
5.1.1.13 | L-aspartate | the aspartate racemase exhibits high substrate specificity to aspartate, L- to D-aspartate is the preferred reaction direction | Picrophilus torridus | D-aspartate | - |
r | |
5.1.1.13 | L-aspartate | - |
Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 | D-aspartate | - |
r | |
5.1.1.13 | L-aspartate | the aspartate racemase exhibits high substrate specificity to aspartate, L- to D-aspartate is the preferred reaction direction | Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 | D-aspartate | - |
r | |
5.1.1.13 | additional information | Picrophilus torridus aspartate racemase is highly specific to aspartate | Picrophilus torridus | ? | - |
? | |
5.1.1.13 | additional information | PtoAspR racemizes L- and D-Asp but has no effect on other amino acids tested | Picrophilus torridus | ? | - |
? | |
5.1.1.13 | additional information | Picrophilus torridus aspartate racemase is highly specific to aspartate | Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 | ? | - |
? | |
5.1.1.13 | additional information | PtoAspR racemizes L- and D-Asp but has no effect on other amino acids tested | Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
5.1.1.13 | homodimer | comparisons of Picrophilus torridus enzyme structure with the Pyrococcus aspartate racemase structure. The dimerization interface is composed of three interaction surfaces, including an inter-subunit disulfide bond and contacts through the beta-sheets and alpha-helix. The interface between two molecules (Mol-A and Mol-B) of Picrophilus torridus PtoAspR looks similar to that of Pyrococcus aspartate racemase, except that there is no cysteine disulfide bond between two molecules of PtoAspR. Each subunit is composed of two homologous domains, the N-terminal domain with residues 1-101 and 207-232, and the C-terminal domain with residues 106-206. The putative catalytic residues, Arg49, Cys83, Asn84, Thr85, Lys159, Cys188, Thr189, are located in the pocket between two domains | Picrophilus torridus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
5.1.1.13 | PTO0149 | locus name | Picrophilus torridus |
5.1.1.13 | PtoAspR | - |
Picrophilus torridus |
5.1.1.13 | pyridoxal 5'-phosphate-independent aspartate racemase | - |
Picrophilus torridus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
5.1.1.13 | 60 | - |
- |
Picrophilus torridus |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
5.1.1.13 | 30 | 70 | recombinant enzyme, about 20% of maximal activity at 30°C and 70°C, profile overview | Picrophilus torridus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
5.1.1.13 | 5.5 | - |
- |
Picrophilus torridus |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
5.1.1.13 | 4.6 | 6.5 | recombinant enzyme, the activity at pH 4.6 is approximately 6times lower than that at the optimal pH 5.5. The activity is completely lost at approximately pH 4.0, 50% of maximal actiivty at pH 6.5, profile overview | Picrophilus torridus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
5.1.1.13 | additional information | a pyridoxal 5'-phosphate-independent aspartate racemase. The putative catalytic residues, Arg49, Cys83, Asn84, Thr85, Lys159, Cys188, Thr189, are located in the pocket between two domains | Picrophilus torridus |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
5.1.1.13 | Picrophilus torridus | - |
- |
5.45 |
EC Number | General Information | Comment | Organism |
---|---|---|---|
5.1.1.13 | metabolism | because Picrophilus aspartate racemase is highly specific to aspartate, other amino acid racemases might exist in Picrophilus torridus | Picrophilus torridus |