On the purification and mechanism of action of 5-aminoimidazole-4-carboxamide-ribonucleotide transformylase from chicken liver.
On the purification and mechanism of action of 5-aminoimidazole-4-carboxamide-ribonucleotide transformylase from chicken liver.
复制标题
鸡肝中5-氨基咪唑-4-甲酰胺-核糖核苷酸转化酶的纯化及作用机制研究
DOI:
10.1021/bi00505a017
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发表时间:
1981
期刊:
影响因子:
2.9
通讯作者:
Benkovic,SJ
中科院分区:
文献类型:
--
作者:
Mueller,WT;Benkovic,SJ
5-Amino-4-imidazolecarboxamide-ribonucleotide transformylase (EC 2.1. 2.3, AICAR TFase), 1 one of two reduced folate-requiring transformylases involved in purinebiosynthesis, catalyzes the formylation of AICAR with 10-formyl-H4folate to produce FAICAR and H4folate. The enzyme has been partially purified from chicken liver by Flaks et al.(1957), by Baggott & Krumdieck (1979a)(41-to 158-fold, respec-tively), and 63-foldfrom Ehrlich Ascites tumor cells by Geiger & Guglielini (1975). Inosinicase (EC 3.5. 4.10, IMP cyclohydrolase) immediately follows AICAR TFase in the purine biosynethic pathway, cyclizing FAICAR to IMP. In all of the above purifications this enzyme was reported to copurify with the transformylase (Baggott & Krumdieck, 1979b), which gave rise to speculation that the two activities were either tightly associated or were on the same protein.