人精氨酸琥珀酸合成酶Mg-ATP结合必需精氨酸残基的鉴定。

Protein sequences & data analysis Pub Date : 1989-07-01
Y Isashiki, T Noda, K Kobayashi, M Sase, T Saheki, K Titani
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引用次数: 0

摘要

人精氨酸琥珀酸合成酶(ASS)的活性被1,2-环己二酮和苯乙二醛等α -二羰基按准一级动力学灭活。Mg-ATP几乎完全保护了该酶,并部分保护了其类似物。Mg-ATP对细胞失活的保护作用最强,其次是Mg-ADP、AMP、腺苷和mg -无机焦磷酸。这些结果表明精氨酸残基对Mg-ATP结合的重要性。经[14C]苯乙二醛标记后经溴化氰处理后,测定了其比放射性最高的肽的氨基酸序列。获得的序列PEFYNRFKGRNDLM与Bock等人[核酸Res 11:6505-6512, 1983]从cDNA核苷酸序列中推断出的氨基酸序列的148-161残基相对应,并且与几种atp需要酶的atp结合位点序列具有高度的同源性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Identification of essential arginine residue(s) for Mg-ATP binding of human argininosuccinate synthetase.

Human argininosuccinate synthetase (ASS) activity was found to be inactivated by alpha-dicarbonyls such as 1,2-cyclohexanedione and phenylglyoxal in accordance with pseudo first-order kinetics. The enzyme was almost completely protected from this inactivation by Mg-ATP and partially by its analogues. The strongest protective effect against inactivation was found with Mg-ATP, followed by Mg-ADP, AMP, adenosine and Mg-inorganic pyrophosphate. These results suggest the importance of arginine residue(s) for Mg-ATP binding. We determined the amino acid sequence of the peptide with the highest specific radioactivity derived from ASS which had been labeled with [14C]phenylglyoxal and then cleaved by cyanogen bromide treatment. The sequence obtained, PEFYNRFKGRNDLM, corresponds to residues 148-161 of the amino acid sequence deduced from the cDNA nucleotide sequence determined by Bock et al. [Nucleic Acids Res 11:6505-6512, 1983], and has a high homology with the sequences of ATP-binding sites proposed for several ATP-requiring enzymes.

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