Transcarboxylase. 8. Isolation and properties of a biotin-carboxyl carrier protein.
Methylmalonyl CoA-oxalacetate transcarboxylase (EC 2. 1. 3. 1) from Propionibacterium shermanii is a biotin enzyme of 670,000 molecular weight containing 6 moles of biotin per mole of enzyme. The active enzyme dissociates spontaneously at low ionic strength and alkaline pH to a mixture of inactive subunits. One type of subunit contains all the biotin of the original molecule. The biotin unit has an S(20,w) = 1.3S and a molecular weight of approximately 12,000. It contains 1 mole of biotin and 1 half-cystine per mole. Qualitative dansyl techniques indicate that alanine is the amino terminal residue of the biotin subunit.
D000409:Alanine / Q000032:analysis; D001426:Bacterial Proteins / Q000032:analysis / Q000302:isolation & purification*; D001710:Biotin; D002852:Chromatography, Ion Exchange; D003553:Cystine / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D008314:Malonates; D008970:Molecular Weight; D009994:Osmolar Concentration; D010071:Oxaloacetates; D011424:Propionibacterium / Q000201:enzymology; D014166:Transferases; D014461:Ultracentrifugation
D001426:Bacterial Proteins; D008314:Malonates; D010071:Oxaloacetates; D003553:Cystine; D001710:Biotin; D014166:Transferases; D000409:Alanine