Isolation and characterization of a cDNA encoding Arabidopsis thaliana 3-hydroxy-3-methylglutaryl-coenzyme A synthase.
[No authors listed]
摘要
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.
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基因功能
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原始数据
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文献解读
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