Partial purification and characterization of ADP sulfurylase from the purple sulfur bacterium Thiocapsa roseopersicina.
High activities of ADP and ATP sulfurylase were found in the soluble protein fraction of Thiocapsa roseopersicina strain 6311 (DSM 219). ADP sulfurylase was partially purified and characterized. It was a very labile soluble enzyme with a molecular weight of 250,000. The optimum pH was 7.5 and the optimal temperature 35 degrees C. Under test conditions the apparent Km values were determined to be 0.33 mM for adenylylsulfate and 13 mM for phosphate.
Algueró
M
M
Departamento de Microbiología, Facultad de Ciencias, Universidad Autónoma de Barcelona, Bellaterra, España.
Dahl
C
C
Trüper
H G
HG
D002861:Chromobacterium / Q000201:enzymology*; D008970:Molecular Weight; D009713:Nucleotidyltransferases / Q000302:isolation & purification*; D013430:Sulfate Adenylyltransferase / Q000302:isolation & purification
D009713:Nucleotidyltransferases; D013430:Sulfate Adenylyltransferase; C062599:sulfate adenylyltransferase (ADP)