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1 ilar to that of the alpha-chain of mammalian propionyl-CoA carboxylase.
2 ferase domain of the Streptomyces coelicolor propionyl-CoA carboxylase.
3 dy was the identification of a high level of propionyl-CoA carboxylase activity and a lesser amount o
5 it in the mammalian biotin-dependent enzymes propionyl-CoA carboxylase and 3-methylcrotonyl-CoA carbo
6 nd fatty acid synthase polypeptides, but not propionyl-CoA carboxylase and mitochondrial pyruvate car
7 disease-causing mutations M204K and R374Q of propionyl-CoA carboxylase and R385S of 3-methylcrotonyl-
8 rboxyltransferase subunits of acetyl-CoA and propionyl-CoA carboxylases and of methylmalonyl-CoA deca
9 iotin carboxylase subunits of acetyl-CoA and propionyl-CoA carboxylases and of pyruvate carboxylase.
10 carboxylase (anaplerosis, gluconeogenesis), propionyl-CoA carboxylase, and 3-methylcrotonyl-CoA carb
11 indicate that pccB encodes the beta-chain of propionyl-CoA carboxylases, and suggest that the alpha-c
15 tal structure, provides new insight into the propionyl-CoA carboxylase mechanism, its oligomeric stru
18 MCC has strong sequence conservation with propionyl-CoA carboxylase (PCC), and their holoenzymes a
22 fragments of the mitochondrial carboxylases propionyl-CoA carboxylase, pyruvate carboxylase, and met
23 d that, in intact livers and hearts, (i) the propionyl-CoA carboxylase reaction is slightly reversibl
24 The 12S reaction is similar to that of human propionyl-CoA carboxylase, whose beta-subunit has 50% se
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