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

scholarly journals Yeast phosphoglycerate mutate. Cyanogen bromide cleavage and amino acid sequence of an active-site peptide

1976 ◽  
Vol 153 (2) ◽  
pp. 145-149 ◽  
Author(s):  
L A Fothergill ◽  
G I Hodgson
Keyword(s):  
Amino Acid ◽  
Active Site ◽  
Cyanogen Bromide ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Phosphoglycerate Mutase ◽  
Large Fragment ◽  
X Ray ◽  
Cnbr Cleavage

The molecular weight and amino acid composition of phosphoglycerate mutase from yeast were determined. CNBr cleavage produced a large (190-residue) fragment and a small (60-residue) fragment. Tryptic and chymotryptic peptides derived from the large fragment were fractionated by ion-exchange chromatography. Peptides from two histidine-containing regions were isolated and the amino acid sequences were determined. Correlation of these data with X-ray-crystallographic evidence shows that the histidine residue in the sequence Arg-Leu Asn-Glu-Arg-His-Tyr-Gly-Asp-Leu-Glu-Gly-Lys is located at the active site.

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 Identification of Mutation Resistance Coldspots for Targeting the SARS-CoV2 Main Protease

2020 ◽  
Author(s):  
Navaneethakrishnan Krishnamoorthy ◽  
Khalid Fakhro
Keyword(s):  
Active Site ◽  
The Novel ◽  
Dimer Interface ◽  
X Ray ◽  
Main Protease ◽  
New Perspective ◽  
Function Relationship ◽  
Novel Coronavirus ◽  
Relationship Of ◽  
Structure And Activity

Abstract Most attempts to target the novel coronavirus SARS-CoV2 are focusing on the main protease (Mpro) 1-9. However, >19,000 mutations in the Mpro have already been reported 10. The mutations encompassing 282 amino acid positions and these “hotspots” might change the Mpro structure and activity, potentially rendering novel antivirals and vaccines ineffective. Here we identified 24 mutational “coldspots” that have resisted mutation since the virus was first detected. We compared the structure-function relationship of these coldspots with several SARS-CoV2 Mpro X-ray crystal structures. We found that three coldspot residues (Leu141, Phe185 and Gln192) help to form the active site, while six (Gly2, Arg4, Tyr126, Lys137, Leu141 and Leu286) contribute to dimer formation that is required for Mpro activity. The surface of the dimer interface is more resistant to mutations compared to the active site. Interestingly, 16 coldspots are found in conserved patterns when compared with other coronaviruses. Importantly, several conserved coldpots are available on the surface of the active site and at the dimer interface for targeting. The identification and short list of these coldspots offers a new perspective to target the SARS-CoV2 Mpro while avoiding mutation-based drug resistance.

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>

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.

Eds Of Radioactive Particles By Self-Induced Fluorescence

1990 ◽  
Vol 48 (2) ◽  
pp. 238-239
Author(s):  
Gregory L. Finch ◽  
Richard G. Cuddihy
Keyword(s):  
Electron Beam Irradiation ◽  
Nuclear Reactor ◽  
X Rays ◽  
Reactor Accident ◽  
Internal Radiation ◽  
X Ray ◽  
External Sources ◽  
X Irradiation ◽  
Available Information ◽  
Individual Particles

The elemental composition of individual particles is commonly measured by using energydispersive spectroscopic microanalysis (EDS) of samples excited with electron beam irradiation. Similarly, several investigators have characterized particles by using external monochromatic X-irradiation rather than electrons. However, there is little available information describing measurements of particulate characteristic X rays produced not from external sources of radiation, but rather from internal radiation contained within the particle itself. Here, we describe the low-energy (< 20 KeV) characteristic X-ray spectra produced by internal radiation self-excitation of two general types of particulate samples; individual radioactive particles produced during the Chernobyl nuclear reactor accident and radioactive fused aluminosilicate particles (FAP). In addition, we compare these spectra with those generated by conventional EDS.Approximately thirty radioactive particle samples from the Chernobyl accident were on a sample of wood that was near the reactor when the accident occurred. Individual particles still on the wood were microdissected from the bulk matrix after bulk autoradiography.

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