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耻垢分枝杆菌核苷二磷酸激酶的生化活性需要His-Gly-Ser-Asp基序中的组氨酸117。

Histidine 117 in the His-Gly-Ser-Asp motif is Required for the Biochemical Activities of Nucleoside Diphosphate Kinase of Mycobacterium smegmatis.

作者信息

Arumugam Muthu, Ajitkumar Parthasarathi

机构信息

Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore-560012, India.

出版信息

Open Biochem J. 2012;6:71-7. doi: 10.2174/1874091X01206010071. Epub 2012 Jul 27.

DOI:10.2174/1874091X01206010071
PMID:22888372
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3414718/
Abstract

Nucleoside diphosphate kinase (NDK), which is widely conserved in both prokaryotes and eukaryotes, maintains a balanced pool of nucleotide triphosphates and their deoxy derivatives. NDKs from bacterial and other systems contain the conserved HGSD motif, where the His residue is required for the biochemical activities, namely the NTPase (AT-Pase and GTPase), NTP synthesising, and autophosphorylation activities of the enzyme. Amino acid sequence homology comparison of the NDK of Mycobacterium smegmatis (MsmNDK) with the NDKs of other bacterial genera showed the presence of H(117)GSD motif. While the recombinant wild type MsmNDK showed the NTPase, NTP synthesising, and autophosphorylation activities, the H117Q mutation abolished the biochemical activities of the recombinant MsmNDK-H117Q mutant protein in vitro. These observations demonstrate that the H117 residue in the HGSD motif is required for the biochemical activities of MsmNDK.

摘要

核苷二磷酸激酶（NDK）在原核生物和真核生物中广泛保守，可维持三磷酸核苷酸及其脱氧衍生物的平衡库。来自细菌和其他系统的NDK含有保守的HGSD基序，其中His残基是该酶生化活性所必需的，即该酶的NTPase（ATPase和GTPase）、NTP合成及自磷酸化活性。耻垢分枝杆菌的NDK（MsmNDK）与其他细菌属的NDK的氨基酸序列同源性比较显示存在H(117)GSD基序。虽然重组野生型MsmNDK显示出NTPase、NTP合成及自磷酸化活性，但H117Q突变在体外消除了重组MsmNDK - H117Q突变蛋白的生化活性。这些观察结果表明，HGSD基序中的H117残基是MsmNDK生化活性所必需的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a6d/3414718/4b78aaf4b992/TOBIOCJ-6-71_F6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a6d/3414718/211b8411d71e/TOBIOCJ-6-71_F1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a6d/3414718/68d72828250e/TOBIOCJ-6-71_F2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a6d/3414718/68e29bf20ae9/TOBIOCJ-6-71_F3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a6d/3414718/b5f07df536d7/TOBIOCJ-6-71_F4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a6d/3414718/295b6d868022/TOBIOCJ-6-71_F5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a6d/3414718/4b78aaf4b992/TOBIOCJ-6-71_F6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a6d/3414718/211b8411d71e/TOBIOCJ-6-71_F1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a6d/3414718/68d72828250e/TOBIOCJ-6-71_F2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a6d/3414718/68e29bf20ae9/TOBIOCJ-6-71_F3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a6d/3414718/b5f07df536d7/TOBIOCJ-6-71_F4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a6d/3414718/295b6d868022/TOBIOCJ-6-71_F5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5a6d/3414718/4b78aaf4b992/TOBIOCJ-6-71_F6.jpg

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