Cloned (Comment) | Organism |
---|---|
gene sat, sequence comparisons, the sat gene is located in one operon and co-transcribed with the aprMBA genes for membrane-bound APS reductase, recombinant expression of His-tagged enzyme in Escherichia coli | Allochromatium vinosum |
Crystallization (Comment) | Organism |
---|---|
purified native enzyme in open state with a ligand-free active site, vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 8.0, with 0.002 ml of reservoir solution containing 1.5 M potassium sodium tartrate and 100 mM MES, pH 6.5, at 18°C, X-ray diffraction structure determination and analysis at 1.6-1.8 A resolution | Allochromatium vinosum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michealis-Menten kinetics, overview | Allochromatium vinosum | |
0.0095 | - |
adenylyl sulfate | recombinant enzyme, pH 8.0, 30°C | Allochromatium vinosum | |
0.0476 | - |
diphosphate | recombinant enzyme, pH 8.0, 30°C | Allochromatium vinosum |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Allochromatium vinosum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + sulfate | Allochromatium vinosum | - |
diphosphate + adenylyl sulfate | - |
r | |
ATP + sulfate | Allochromatium vinosum DSM 180 | - |
diphosphate + adenylyl sulfate | - |
r | |
diphosphate + adenylyl sulfate | Allochromatium vinosum | - |
ATP + sulfate | - |
r | |
diphosphate + adenylyl sulfate | Allochromatium vinosum DSM 180 | - |
ATP + sulfate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Allochromatium vinosum | O66036 | gene sat | - |
Allochromatium vinosum DSM 180 | O66036 | gene sat | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration, native enzyme by hydrophobic interaction chromatography, ultrafiltration, dialysis, anion exchange chromatography, ultracentrifugation, and gel filtration | Allochromatium vinosum |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
433 | - |
purified recombinant enzyme, ATP synthesis, pH 8.0, 30°C | Allochromatium vinosum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + sulfate | - |
Allochromatium vinosum | diphosphate + adenylyl sulfate | - |
r | |
ATP + sulfate | - |
Allochromatium vinosum DSM 180 | diphosphate + adenylyl sulfate | - |
r | |
diphosphate + adenylyl sulfate | - |
Allochromatium vinosum | ATP + sulfate | - |
r | |
diphosphate + adenylyl sulfate | - |
Allochromatium vinosum DSM 180 | ATP + sulfate | - |
r |
Subunits | Comment | Organism |
---|---|---|
homodimer | each subunit subdivided into three domains, the N-terminal domain I (residues 1-172) is basically built up of a beta-barrel with five antiparallel strands surrounded by alpha-helices, the catalytic domain II (residues 173-331) of a typical Rossmann-like alpha/beta structure and the small C-terminal domain III (residues 332-396) of a small three-strand beta-sheet and two alpha-helices | Allochromatium vinosum |
Synonyms | Comment | Organism |
---|---|---|
adenylsulfurylase | - |
Allochromatium vinosum |
ATP sulfurylase | - |
Allochromatium vinosum |
dissimilatory ATP sulfurylase | - |
Allochromatium vinosum |
SAT | - |
Allochromatium vinosum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Allochromatium vinosum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Allochromatium vinosum |
General Information | Comment | Organism |
---|---|---|
evolution | despite different kinetic properties ATPS involved in sulfur-oxidizing and sulfate-reducing processes are not distinguishable on a structural level presumably due to the interference between functional and evolutionary processes. The sat-aprMBA gene locus in Allochromatium vinosum and other phototrophic members of the family Chromatiaceae, overview | Allochromatium vinosum |
metabolism | sulfate assimilation also proceeds independently of Sat by a separate pathway involving a cysDN-encoded assimilatory ATP sulfurylase | Allochromatium vinosum |
physiological function | the enzyme is dispensible for growth on reduced sulfur compounds due to the presence of an alternate sulfite-oxidizing pathway in Allochromatium vinosum | Allochromatium vinosum |