Leucine-684: A conserved residue of an AMP-acetyl CoA synthetase (AceCS) from Leishmania donovani is involved in substrate recognition, catalysis and acetylation
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- 作者：Neelagiri Soumyaa ; Hitendra Tandanb ; Mangesh V. Damreb ; Rahul P. Gangwalb ; Abhay T. Sangamwarb ; Sushma Singha ; sushmasingh@niper.ac.in" class="auth_mail" title="E-mail the corresponding author
- 关键词：AMP ; Adenosine monophosphate ; AceCS ; Acetyl CoA synthetase ; CD ; Circular Dichroism ; L ; Leucine ; P ; Proline ; CoA ; Coenzyme A ; ATP ; Adenosne triphosphate ; HIV ; human immunodeficiency virus ; PAT ; Protein acetyltransferase ; Ld ; Leishmania donovani ; NBT ; Nitro blue tetrazolium ; BCIP ; 5-bromo-4-chloro3-indolyl phosphate disodium salt ; DOPE ; Discrete Optimized Protein Energy ; MD ; Molecular dynamic ; BLAST ; Basic local alignment search tool
- 刊名：Gene
- 出版年：2016
- 出版时间：15 April 2016
- 年：2016
- 卷：580
- 期：2
- 页码：125-133
- 全文大小：1092 K
文摘
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Leishmania donovani AceCS enzyme possesses a conserved leucine at 684 position (L684).
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Leucine to Proline mutation affects binding of the enzyme with ATP and acetate but not CoA.
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L684 is not involved in maintaining structural integrity of the enzyme.
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L684P mutation affects acetylation of AceCS.
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Changes in kinetic parameters upon mutation are validated by in silico modeling of enzyme.