Phosphoryl transfer reaction catalyzed by membrane diacylglycerol kinase: a theoretical mechanism study

2015 ◽  
Vol 17 (38) ◽  
pp. 25228-25234 ◽  
Author(s):  
Yafei Jiang ◽  
Hongwei Tan ◽  
Jimin Zheng ◽  
Xichen Li ◽  
Guangju Chen ◽  
...  
Keyword(s):  
Active Site ◽  
Transfer Reaction ◽  
Diacylglycerol Kinase ◽  
Phosphoryl Transfer ◽  
Mechanism Study ◽  
Theoretical Mechanism ◽  
Kinase A

Despite a unique composite active site formed by two monomers, DgkA catalyzes phosphotransfer reaction using the canonical kinase mechanism.

scholarly journals How a Second Mg2+ Ion Affects the Phosphoryl Transfer Mechanism in a Protein Kinase: A Computational Study

2020 ◽  
Author(s):  
Rodrigo Recabarren ◽  
Kirill Zinovjev ◽  
Iñaki Tuñón ◽  
Jans Alzate-Morales
Keyword(s):  
Free Energy ◽  
Quantum Mechanics ◽  
Active Site ◽  
Transfer Reaction ◽  
Computational Study ◽  
Free Energy Calculations ◽  
Phosphoryl Transfer ◽  
Activation Free Energy ◽  
Lower Activation ◽  
Kinase A

<div>In this contribution, the phosphoryl transfer reaction in CDK2 has been studied in detail considering the presence of an additional Mg2+ ion in the active site. For this purpose, QM/MM (quantum mechanics/molecular mechanics) free energy calculations with the adaptive string method were performed, which showed that indeed the system containing two Mg2+ ions exhibits a lower activation free energy, corroborating the experimental observations.</div>

scholarly journals How a Second Mg2+ Ion Affects the Phosphoryl Transfer Mechanism in a Protein Kinase: A Computational Study

2020 ◽  
Author(s):  
Rodrigo Recabarren ◽  
Kirill Zinovjev ◽  
Iñaki Tuñón ◽  
Jans Alzate-Morales
Keyword(s):  
Free Energy ◽  
Quantum Mechanics ◽  
Active Site ◽  
Transfer Reaction ◽  
Computational Study ◽  
Free Energy Calculations ◽  
Phosphoryl Transfer ◽  
Activation Free Energy ◽  
Lower Activation ◽  
Kinase A

<div>In this contribution, the phosphoryl transfer reaction in CDK2 has been studied in detail considering the presence of an additional Mg2+ ion in the active site. For this purpose, QM/MM (quantum mechanics/molecular mechanics) free energy calculations with the adaptive string method were performed, which showed that indeed the system containing two Mg2+ ions exhibits a lower activation free energy, corroborating the experimental observations.</div>

Structure and activity of phosphoglycerate mutase

1981 ◽  
Vol 293 (1063) ◽  
pp. 121-130 ◽  
Keyword(s):  
Active Site ◽  
Transfer Reaction ◽  
Chemical Kinetic ◽  
Phosphoglycerate Mutase ◽  
Phosphoryl Transfer ◽  
X Ray ◽  
Histidine Residues ◽  
Ping Pong ◽  
Available Information ◽  
Structure And Activity

The structure of yeast phosphoglycerate mutase determined by X-ray crystallographic and amino acid sequence studies has been interpreted in terms of the chemical, kinetic and mechanistic observations made on this enzyme. There are two histidine residues at the active site, with imidazole groups almost parallel to each other and approximately 0.4 nm apart, positioned close to the 2 and 3 positions of the substrate. The simplest interpretation of the available information suggests that a ping-pong type mechanism operates in which at least one of these histidine residues participates in the phosphoryl transfer reaction. The flexible C-terminal region also plays an important role in the enzymic reaction.

scholarly journals Characterizing Active Site Conformational Heterogeneity along the Trajectory of an Enzymatic Phosphoryl Transfer Reaction

2016 ◽  
Vol 55 (38) ◽  
pp. 11533-11537 ◽  
Author(s):  
Cathleen Zeymer ◽  
Nicolas D. Werbeck ◽  
Sabine Zimmermann ◽  
Jochen Reinstein ◽  
D. Flemming Hansen
Keyword(s):  
Active Site ◽  
Transfer Reaction ◽  
Phosphoryl Transfer ◽  
Conformational Heterogeneity

scholarly journals Characterizing Active Site Conformational Heterogeneity along the Trajectory of an Enzymatic Phosphoryl Transfer Reaction

2016 ◽  
Vol 128 (38) ◽  
pp. 11705-11709
Author(s):  
Cathleen Zeymer ◽  
Nicolas D. Werbeck ◽  
Sabine Zimmermann ◽  
Jochen Reinstein ◽  
D. Flemming Hansen
Keyword(s):  
Active Site ◽  
Transfer Reaction ◽  
Phosphoryl Transfer ◽  
Conformational Heterogeneity

Benchmark calculations on models of the phosphoryl transfer reaction catalyzed by protein kinase A

2009 ◽  
Vol 124 (3-4) ◽  
pp. 197-215 ◽  
Author(s):  
Manuel Montenegro ◽  
Mireia Garcia-Viloca ◽  
Àngels González-Lafont ◽  
José M. Lluch
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Transfer Reaction ◽  
Phosphoryl Transfer ◽  
Kinase A
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