Purification and characterization of two proteins with inorganic pyrophosphatase activity from Desulfovibrio vulgaris: rubrerythrin and a new, highly active, enzyme.
The inorganic pyrophosphatase activity of a soluble extract from the strict anaerobe, sulfate-reducing, Desulfovibrio vulgaris, is readily resolved into two peaks. After purification, two active proteins with very dissimilar properties are obtained. One is the non-heme iron-containing rubrerythrin, with a specific activity of 350 pyrophosphate hydrolyzed, min-1, mg protein-1. The other, a protein of Mr = 39,000, with a specific activity of 12,000.
Liu
M Y
MY
Department of Biochemistry, School of Chemical Sciences, University of Georgia, Athens 30602.
Le Gall
J
J
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002845:Chromatography; D003901:Desulfovibrio / Q000201:enzymology*; D005288:Ferredoxins / Q000302:isolation & purification* / Q000378:metabolism; D006422:Hemerythrin; D008969:Molecular Sequence Data; D011755:Pyrophosphatases / Q000302:isolation & purification*; D012416:Rubredoxins; D012995:Solubility; D013056:Spectrophotometry, Ultraviolet
D000596:Amino Acids; D001426:Bacterial Proteins; D005288:Ferredoxins; D006422:Hemerythrin; D012416:Rubredoxins; C055857:rubrerythrins; D011755:Pyrophosphatases