Transition of phosphopantetheine adenylyltransferase from catalytic to allosteric state is characterized by ternary complex formation in Pseudomonas aeruginosa
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- 作者：Rakesh Chatterjee rakesh.2665675@gmail.com" class="auth_mail" title="E-mail the corresponding author ; Abhisek Mondal abhisek.mndl@gmail.com" class="auth_mail" title="E-mail the corresponding author ; Abhishek Basu abasu4@rediffmail.com" class="auth_mail" title="E-mail the corresponding author ; Saumen Datta ; saumen_datta@iicb.res.in" class="auth_mail" title="E-mail the corresponding author
- 关键词：PPAT ; phosphopantetheine adenylyltransferase ; CoA ; Coenzyme A ; AcCoA ; Acetyl Coenzyme A ; IPTG ; isopropyl-β-d-1-thiogalactopyranoside ; Sulfo-EGS ; ethylene glycol bis(succinimidyl) succinate ; PPi ; pyrophosphate ; DMSO ; dimethyl sulfoxide ; PEG ; polyethylene glycol ; CD ; circular dichroism ; ATP ; adenosine triphosphate ; AMP-PNP ; adenylyl imidodiphosphate ; NTA ; nitrilo triacetic acid ; PhP ; phosphopantetheine
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2016
- 出版时间：July 2016
- 年：2016
- 卷：1864
- 期：7
- 页码：773-786
- 全文大小：3729 K
文摘
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PPAT is an allosteric enzyme catalyzing the rate limiting step in CoA biosynthesis.
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It is regulated by CoA and AcCoA which is inhibited by feedback inhibition.
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Allosteric to catalytic states are characterized by a ternary complex.
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Ca2 + ion has an influence in the inhibition of the enzyme.
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R90 and D94 play a crucial role during such process.