Incorporation of pantothenate into citrate lyase by a pantothenateless mutant of Klebsiella pneumoniae.
A pantothenate-requiring mutant of Klebsiella pneumoniae was isolated. The mutant showed an absolute dependence on pantothenate for growth. When grown in the presence of [14C]pantothenate, the mutant incorporated [14C]pantothenate into citrate lyase (3.4 mol/mol of enzyme). Analysis of a double-labeled enzyme ([14C]pantothenate and [3H]acetate) by gel electrophoresis in sodium dodecyl sulfate showed that both 3H and 14C were associated solely with the smallest subunit, the acyl carrier protein of citrate lyase.
D000085:Acetates / Q000378:metabolism; D002250:Carbon Radioisotopes; D002352:Carrier Proteins / Q000378:metabolism; D002951:Citrates; D007711:Klebsiella pneumoniae / Q000201:enzymology / Q000276:immunology / Q000378:metabolism*; D009154:Mutation; D007652:Oxo-Acid-Lyases / Q000096:biosynthesis* / Q000276:immunology; D010205:Pantothenic Acid / Q000378:metabolism*; D014316:Tritium
D000085:Acetates; D002250:Carbon Radioisotopes; D002352:Carrier Proteins; D002951:Citrates; D014316:Tritium; D010205:Pantothenic Acid; D007652:Oxo-Acid-Lyases