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卤虫5-磷酸核糖焦磷酸酰胺转移酶的存在、初步性质及部分纯化

Presence, preliminary properties and partial purification of 5-phosphoribosylpyrophosphate amidotransferase from Artemia sp.

作者信息

Liras A, Argomaniz L, Llorente P

机构信息

Departmento de Bioquímica, Facultad de Medicina, Universidad Autónoma de Madrid, Spain.

出版信息

Biochim Biophys Acta. 1990 Jan 29;1033(1):114-7. doi: 10.1016/0304-4165(90)90203-9.

DOI:10.1016/0304-4165(90)90203-9
PMID:1689183
Abstract

5'-Phosphoribosylpyrophosphate amidotransferase, which catalyzes the synthesis of phosphoribosylamine in the de novo synthesis of purine nucleotides, has been detected and partially purified approx. 800-fold from Artemia sp. nauplii. The apparent Km values for 5'-phosphoribosyl 1-pyrophosphate as substrate were 0.7 mM and 0.4 mM in the presence of glutamine and ammonia as nitrogenous sources, respectively, and the enzymatic activity was inhibited by purine 5'-ribonucleotide compounds and 5', 5'''-p1, p4-diguanosine tetraphosphate.

摘要

5'-磷酸核糖焦磷酸酰胺转移酶催化嘌呤核苷酸从头合成中磷酸核糖胺的合成,已从卤虫无节幼体中检测到并部分纯化了约800倍。以5'-磷酸核糖1-焦磷酸为底物时,在谷氨酰胺和氨作为氮源存在下,其表观Km值分别为0.7 mM和0.4 mM,并且该酶活性受到嘌呤5'-核糖核苷酸化合物和5', 5'''-p1, p4-二鸟苷四磷酸的抑制。

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Biochim Biophys Acta. 1990 Jan 29;1033(1):114-7. doi: 10.1016/0304-4165(90)90203-9.
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De novo purine biosynthesis in the crustacean Artemia: influence of salinity and geographical origin.卤虫中嘌呤的从头合成:盐度和地理起源的影响。
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