Crystal Structures of Pyrophosphatase from <i>Acinetobacter baumannii</i>: Snapshots of Pyrophosphate Binding and Identification of a Phosphorylated Enzyme Intermediate

Crystal Structures of Pyrophosphatase from <i>Acinetobacter baumannii</i>: Snapshots of Pyrophosphate Binding and Identification of a Phosphorylated Enzyme Intermediate

All living things have pyrophosphatases that hydrolyze pyrophosphate and release energy. This energetically favorable reaction drives many energetically unfavorable reactions. An accepted catalytic model of pyrophosphatase shows that a water molecule activated by two divalent cations (M1 and M2) wit...

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Bibliographic Details
Main Authors: Yunlong Si, Xing Wang, Guosong Yang, Tong Yang, Yuying Li, Gabriela Jaramillo Ayala, Xumin Li, Hao Wang, Jiyong Su
Format: Article
Language:English
Published: MDPI AG 2019-09-01
Series:International Journal of Molecular Sciences
Subjects:
inorganic pyrophosphatase
crystal structure
catalytic mechanism
lysine phosphorylation
mass spectrometry
<i>Acinetobacter baumannii</i>
Online Access:https://www.mdpi.com/1422-0067/20/18/4394

Internet

https://www.mdpi.com/1422-0067/20/18/4394

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