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Literature summary for 2.7.7.4 extracted from

  • Parey, K.; Demmer, U.; Warkentin, E.; Wynen, A.; Ermler, U.; Dahl, C.
    Structural, biochemical and genetic characterization of dissimilatory ATP sulfurylase from Allochromatium vinosum (2013), PLoS ONE, 8, e74707.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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 (Commentary)

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 [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

Metals/Ions Comment Organism Structure
Mg2+ required Allochromatium vinosum

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Allochromatium vinosum O66036 gene sat
-
Allochromatium vinosum DSM 180 O66036 gene sat
-

Purification (Commentary)

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 [micromol/min/mg]

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 and Products (Substrate)

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

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

Synonyms Comment Organism
adenylsulfurylase
-
Allochromatium vinosum
ATP sulfurylase
-
Allochromatium vinosum
dissimilatory ATP sulfurylase
-
Allochromatium vinosum
SAT
-
Allochromatium vinosum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Allochromatium vinosum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Allochromatium vinosum

General Information

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