Activities | Families | Sequences | Fold types | References | Help
B6db references: 86304372

type Journal Article
authors Fubara, B.; Eckenrode, F.; Tressel, T.; Davis, L.
title Purification and properties of aminoacetone synthetase from beef liver mitochondria
journal J Biol Chem
ui 86304372
year (1986)
volume 261
number 26
pages 12189-96.
keywords Acetyl Coenzyme A/metabolism
abstract Aminoacetone synthetase from beef liver mitochondria was purified to homogeneity and shown to be a member of the pyridoxal 5'-phosphate- dependent family of enzymes. This enzyme catalyzes the condensation of glycine and acetyl-CoA to produce CO2, CoA, and the stable product aminoacetone. Bovine aminoacetone synthetase is a dimer (Mr 56,000) of identical subunits and contains 2 mol of pyridoxal phosphate/mol of dimer. The holoenzyme was resolved by dialysis against cysteine and has a pI of 5.2. The holoenzyme shows an absorption maximum at 428 nm which undergoes a shift to 335 nm when reduced with sodium borohydride. The Km values of glycine and acetyl-CoA were 22 mM and 53 microM, respectively. Initial velocity studies indicate that the condensation reaction proceeds by an ordered mechanism. With the exception of aminomalonate, bovine aminoacetone synthetase acts specifically on glycine and acetyl-CoA. Coupled reactions of purified bovine aminoacetone synthetase and porcine L-threonine dehydrogenase demonstrated the interconversion of threonine and glycine.
last changed 2002/11/04 17:41

B6db references