| Literature DB >> 8566777 |
F Montamat1, M Guilloton, F Karst, S Delrot.
Abstract
An 1.7-kb Arabidopsis thaliana (At) cDNA was isolated by complementation of a bap1 mutation affecting the transport of branched-chain amino acids (aa) in the yeast Saccharomyces cerevisiae. The determination of the nucleotide (nt) sequence revealed an open reading frame of 1383 nt which may encode a protein of 461 aa with a predicted molecular mass of 51,038 Da. The deduced aa sequence exhibited strong similarities with mammalian 3-hydroxy-3-methylglutaryl-coenzyme A synthase (HMGS) sequences. Although former biochemical studies have suggested that acetoacetyl-coenzyme A thiolase (AACT) and HMGS activities were carried by a single protein in plants, complementation studies and measurements of enzymatic activities clearly showed that the At HMGS is devoid of AACT activity.Entities:
Mesh：
Substances：
Year: 1995 PMID： 8566777 DOI： 10.1016/0378-1119(95)00642-7
Source DB: PubMed Journal: Gene ISSN： 0378-1119 Impact factor: 3.688