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Literature summary for 2.7.7.4 extracted from

  • Prioretti, L.; Lebrun, R.; Gontero, B.; Giordano, M.
    Redox regulation of ATP sulfurylase in microalgae (2016), Biochem. Biophys. Res. Commun., 478, 1555-1562.
    View publication on PubMed
Search for more literature for 2.7.7.4

Inhibitors

Inhibitors Comment Organism Structure
iodoacetic acid
-
 Synechocystis sp.
iodoacetic acid
-
 Thalassiosira pseudonana
N-ethylmaleimide
-
 Synechocystis sp.
N-ethylmaleimide
-
 Thalassiosira pseudonana

Organism

Organism UniProt Comment Textmining
Synechocystis sp. P74241 gene sat
-
Thalassiosira pseudonana B8CBW8 gene THAPSDRAFT_269714
-
Thalassiosira pseudonana PLY-693 B8CBW8 gene THAPSDRAFT_269714
-

Synonyms

Synonyms Comment Organism
ATP sulfurylase
-
 Thalassiosira pseudonana
ATP sulfurylase
-
 Synechocystis sp.
ATPS-A
-
 Synechocystis sp.
ATPS-B
-
 Thalassiosira pseudonana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Thalassiosira pseudonana
25
-
 assay at Synechocystis sp.

General Information

General Information Comment Organism
evolution an ATPS type A is mostly present in freshwater cyanobacteria, with four conserved cysteine residues. Oceanic cyanobacteria and most eukaryotic algae instead, possess an ATPS-B containing seven to ten cysteines, five of them are conserved, but only one in the same position as ATPS-A. Oceanic cyanobacteria have ATPS-B structurally and functionally closer to that from most of eukaryotic algae than to the ATPS-A from other cyanobacteria suggests that life in the sea or freshwater may have driven the evolution of ATPS. ATPS-B belongs to the oceanic cyanobacteria of the genera Synechococcus and Prochlorococcus and to all eukaryotic algae except dinoflagellates, sequence alignment of ATPS from the algal species, overview Thalassiosira pseudonana
evolution an ATPS type A is mostly present in freshwater cyanobacteria, with four conserved cysteine residues. Oceanic cyanobacteria and most eukaryotic algae instead, possess an ATPS-B containing seven to ten cysteines, five of them are conserved, but only one in the same position as ATPS-A. The absence of this residue in the ATPS-A of the freshwater cyanobacterium Synechocystis sp. is consistent with its lack of regulation. Oceanic cyanobacteria have ATPS-B structurally and functionally closer to that from most of eukaryotic algae than to the ATPS-A from other cyanobacteria suggests that life in the sea or freshwater may have driven the evolution of ATPS. ATPS-A is typical of all freshwater cyanobacteria and marine-coastal cyanobacteria that do not belong to the genera Synechococcus and Prochlorococcus, sequence alignment of ATPS from the algal species, overview Synechocystis sp.
additional information three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview Thalassiosira pseudonana
additional information three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview Synechocystis sp.
physiological function ATP sulfurylase (ATPS) catalyzes the first step of sulfur assimilation in photosynthetic organisms, role of cysteines on the regulation of the different algal enzymes ATPS-A and ATPS-B. The LC-MS/MS analysis of ATPS-A of the freshwater cyanobacterium Synechocystis sp. shows that the lack of residue Cys247 causes a lack of regulation Synechocystis sp.
physiological function ATP sulfurylase (ATPS) catalyzes the first step of sulfur assimilation in photosynthetic organisms, role of cysteines on the regulation of the different algal enzymes ATPS-A and ATPS-B. The LC-MS/MS analysis of ATPS-B from the marine diatom Thalassiosira pseudonana shows that the residue Cys247 is presumably involved in the redox regulation Thalassiosira pseudonana