EC Number | Cloned (Comment) | Organism |
---|---|---|
6.3.2.36 | gene TK1686, DNA and amino acid sequence determination and analysis, sequence comparisons | Thermococcus kodakarensis |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
6.3.2.36 | purified free enzyme, and enzyme in complexes with ATP, and ATP and 4-phosphopantoate, sitting drop vapor diffusion method, for the free enzyme: mixing of 0.001 ml of 20 mg/ml of protein in 50 mM Tris-HC, pH 8.0, and 150 mM NaCl, with 0.001 ml of reservoir solution containing 18-20% PEG 3350, 200 mM ammonium acetate, and 100 mM Bis-Tris, pH 6.5, 20°C, 1 week, method optimization, for the enzyme-ATP-Mg2+ complex: 20 mg/ml protein is incubated for several hours at 4°C in the presence of 10 mM ATP and 10 mM MgCl2, mixing of 0.001 ml protein solution with 0.001 ml of reservoir solution containing 17% PEG 10000, 100 mM ammonium acetate, and 100 mM Bis-Tris, pH 5.5, equilibration with reservoir solution, 20°C, 2 weeks, for the enzyme-ATP-Mg2+-4-phosphopantoate complex, mixing of 0.001 ml of 20 mg/ml of protein in 50 mM Tris-HC, pH 8.0, 150 mM NaCl, mM ATP, 5 mM MgCl2, and 5 mM PPo, with 0.001 ml of reservoir solution containing 50% tacsimate, pH 4.0, 1% PEG 3350, and 100 mM sodium acetate trihydrate, pH 4.5, 4°C, 3 days, X-ray diffraction structure determination and analysis at 2.0-2.4 A resolution | Thermococcus kodakarensis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.3.2.36 | Mg2+ | required | Thermococcus kodakarensis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
6.3.2.36 | 60000 | - |
about, gel filtration | Thermococcus kodakarensis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.2.36 | ATP + (R)-4-phosphopantoate + beta-alanine | Thermococcus kodakarensis | - |
AMP + diphosphate + (R)-4'-phosphopantothenate | - |
? | |
6.3.2.36 | ATP + (R)-4-phosphopantoate + beta-alanine | Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1 | - |
AMP + diphosphate + (R)-4'-phosphopantothenate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.3.2.36 | Thermococcus kodakarensis | Q5JIZ8 | - |
- |
6.3.2.36 | Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1 | Q5JIZ8 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.2.36 | ATP + (R)-4-phosphopantoate + beta-alanine | - |
Thermococcus kodakarensis | AMP + diphosphate + (R)-4'-phosphopantothenate | - |
? | |
6.3.2.36 | ATP + (R)-4-phosphopantoate + beta-alanine | - |
Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1 | AMP + diphosphate + (R)-4'-phosphopantothenate | - |
? | |
6.3.2.36 | additional information | substrate binding structures, overview | Thermococcus kodakarensis | ? | - |
? | |
6.3.2.36 | additional information | substrate binding structures, overview | Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
6.3.2.36 | homodimer | 2 x 30000, about, sequence calculation | Thermococcus kodakarensis |
6.3.2.36 | More | PPS forms an asymmetric homodimer, in which two monomers composing a dimer, deviated from the exact twofold symmetry, displaying 4°13° distortion | Thermococcus kodakarensis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.3.2.36 | phosphopantothenate synthetase | - |
Thermococcus kodakarensis |
6.3.2.36 | Pps | - |
Thermococcus kodakarensis |
6.3.2.36 | TK1686 | - |
Thermococcus kodakarensis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.3.2.36 | ATP | nuleotide binding structure analysis, modeling, overview | Thermococcus kodakarensis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
6.3.2.36 | metabolism | the common pathway for coenzyme A biosynthesis which involves two enzymes to convert pantoate to 4'-phosphopantothenate involves two enzymes, pantoate kinase, and phosphopantothenate synthetase (PPS), they are responsible for this conversion in archaea. In archea, In these archaea, pantoate is phosphorylated by PoK to produce 4-phosphopantoate (PPo), and then condensation of PPo and beta-alanine is catalyzed by PPS, generating 4'-phosphopantothenate | Thermococcus kodakarensis |
6.3.2.36 | additional information | enzyme structure and substrate binding analysis, structure comparisons, structure-function analysis, overview | Thermococcus kodakarensis |
6.3.2.36 | physiological function | enzyme PPS catalyzes the ATP-dependent condensation of 4-phosphopantoate and beta-alanine generating 4'-phosphopantothenate | Thermococcus kodakarensis |