Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs
Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs
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植物和细菌丙酮酸磷酸二激酶、细菌磷酸烯醇丙酮酸酶 I：糖磷酸转移酶系统和其他 PEP 利用酶的序列同源性分析。
DOI：
10.1021/bi00500a006
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发表时间：
1990
期刊：
影响因子：
2.9
通讯作者：
Dunaway-Mariano,D
中科院分区：
文献类型：
--
作者：
Pocalyko,DJ;Carroll,LJ;Martin,BM;Babbitt,PC;Dunaway-Mariano,D
化学和生物化学系，马里兰州大学，College Park，马里兰州20742，分子神经遗传学单位，临床神经科学分支，国家精神卫生研究所，Bethesda，马里兰州20892，和药物化学系，加州大学，San弗朗西斯科，加州94143，1990年4月10日接收;摘要：在本文中，我们报告的氨基酸序列的丙酮酸磷酸二激酶（PPDK）从共生拟杆菌的PPDK基因的核苷酸序列测定。比较B。共生菌PPDK氨基酸序列与玉米PPDK的氨基酸序列[Matsuoka，M.，Ozeki，Y.，Yam-amoto，N.，Hirano，H.，Kamo-Murakami，Y.，& Tanaka，Y.（1988）J.Biol.Chem.263，11080]揭示了同源序列的长延伸（> 70%同一性），其导致53%的总体序列同一性。圆二色谱，亲水性配置文件，并计算二级结构元素的两个双激酶表明，他们可能有非常相似的三级结构，以及。将玉米和B的氨基酸序列进行了比较。共生菌二激酶与其它已知蛋白质序列的同源性显示，集中在三段序列中，与一种机械相关的酶，大肠杆菌PEP：糖磷酸转移酶系统的酶I [Saffen，D. W.，Presper，KA，Doering，TL，Roseman，S.（1987）J.Biol.Chem.262，16241]，提出（i）这三段序列构成PEP结合和催化的位点以及调节酶活性的可能位点，和（ii）保守序列存在于第三种机制相关的酶PEP合酶中。丙酮酸磷酸二激酶（PPDK）1催化丙酮酸和正磷酸与单个ATP分子的α-和γ-磷酰基的可逆磷酸化（Reeves等人，1968年;埃文斯和伍德，1968年）：07 7 0
Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, Molecular Neurogenetics Unit, Clinical Neuroscience Branch, National Institute of Mental Health, Bethesda, Maryland 20892, and Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94143 Received April 10, 1990; Revised Manuscript Received July 30, 1990 abstract: In this paper we report the amino acid sequence of pyruvate phosphate dikinase (PPDK) from Bacteroides symbiosus as determined from the nucleotide sequence of the PPDK gene. Comparison of the B. symbiosus PPDK amino acid sequence with that of the maize PPDK [Matsuoka, M., Ozeki, Y., Yam-amoto, N., Hirano, H., Kamo-Murakami, Y., & Tanaka, Y.(1988) J. Biol. Chem. 263, 11080] revealed long stretches of homologous sequence (> 70% identity), which contributed to an overall sequence identity of 53%. The circular dichrosim spectra, hydropathy profiles, and calculated secondary structural elements of the two dikinases suggest that they may have very similar tertiary structures as well. A comparison made between the amino acid sequence of the maize and B. symbiosus dikinase with other known protein sequences revealed homology, concentrated in three stretches of sequences, to a mechanistically related enzyme, enzyme I of the Escherichia coli PEP: sugar phosphotransferase system [Saffen, D. W., Presper, KA, Doering, TL, Roseman, S.(1987) J. Biol. Chem. 262, 16241], It is proposed that (i) these three stretches of sequence constitute the site for PEP binding and catalysis and a possible site for the regulation of enzymatic activity and (ii) the conserved sequences exist in a third mechanistically related enzyme, PEPsynthase. i^ ruvate phosphate dikinase (PPDK) 1 catalyzes the rever-sible phosphorylation of pyruvate and orthophosphate with the ß-and y-phosphoryl groups of a single molecule of ATP (Reeves et al., 1968; Evans & Wood, 1968): 07 7 0