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dam methylase from E. coli. Circular dichroism investigations of the secondary structure and influence of S-adenosylmethionine.

作者信息

Kriebardis A, Guschlbauer W

出版信息

FEBS Lett. 1987 Mar 23;213(2):297-300. doi: 10.1016/0014-5793(87)81509-0.

DOI:10.1016/0014-5793(87)81509-0
PMID:3549359
Abstract

The enzyme dam methylase which recognizes and methylates the adenine in the palindromic sequence GATC in DNA was isolated and the secondary structure was determined by CD spectroscopy and various predicting methods from the amino acid sequence. The interaction of dam methylase with S-adenosylmethionine was studied by CD spectroscopy indicating a decrease of the percentage of alpha-helix as the amount of S-adenosylmethionine bound to the enzyme was increased.

摘要

相似文献

1
dam methylase from E. coli. Circular dichroism investigations of the secondary structure and influence of S-adenosylmethionine.
FEBS Lett. 1987 Mar 23;213(2):297-300. doi: 10.1016/0014-5793(87)81509-0.
2
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The DNA and S-adenosylmethionine-binding regions of EcoDam and related methyltransferases.
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Direct role of the Escherichia coli Dam DNA methyltransferase in methylation-directed mismatch repair.大肠杆菌Dam DNA甲基转移酶在甲基化导向错配修复中的直接作用。
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The Escherichia coli dam DNA methyltransferase modifies DNA in a highly processive reaction.大肠杆菌dam DNA甲基转移酶在高度持续的反应中修饰DNA。
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Allosteric and catalytic binding of S-adenosylmethionine to Escherichia coli DNA adenine methyltransferase monitored by 3H NMR.通过³H核磁共振监测S-腺苷甲硫氨酸与大肠杆菌DNA腺嘌呤甲基转移酶的变构结合和催化结合。
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Cloning of the Dam methyltransferase gene from Haemophilus influenzae bacteriophage HP1.从流感嗜血杆菌噬菌体HP1中克隆Dam甲基转移酶基因。
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[Comparison of specific recognition sites of adenine and cytosine DNA-methylase of Yersinia Pestis EV 76 C dam and dcm by Escherichia coli methylases].[鼠疫耶尔森菌EV 76 C dam和dcm的腺嘌呤与胞嘧啶DNA甲基化酶的特异性识别位点与大肠杆菌甲基化酶的比较]
Biokhimiia. 1984 Oct;49(10):1594-7.

引用本文的文献

1
The double role of methyl donor and allosteric effector of S-adenosyl-methionine for Dam methylase of E. coli.S-腺苷甲硫氨酸作为甲基供体和大肠杆菌Dam甲基化酶变构效应剂的双重作用。
Nucleic Acids Res. 1990 Aug 11;18(15):4369-75. doi: 10.1093/nar/18.15.4369.