The Role of Binding Pocket Amino Acid Residues in Substrate Specificity Towards Xanthine Oxidase Enzyme

Temesgen Nurlign Chekol

doi:doi:10.11648/j.ajcbe.20180202.12

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The Role of Binding Pocket Amino Acid Residues in Substrate Specificity Towards Xanthine Oxidase Enzyme

Temesgen Nurlign Chekol

Published in American Journal of Chemical and Biochemical Engineering (Volume 2, Issue 2)

Received: 26 October 2018 Accepted: 3 December 2018 Published: 3 January 2019

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Abstract

Xanthine oxidase is one of the most useful molybdenum containing enzymes, which catalyzes a wide range of purine derivative heterocyclic substrates. In order for the interaction between the reactants to take place, the substrates are expected to enter the binding pocket and attain a proper orientation with the help of binding pocket amino acid residues. Therefore, the study is mainly focused to understand the role of binding pocket amino acid residues in providing the substrates proper orientation for the nucleophilic reaction to take place. The binding pocket amino acids residues in particular, Glu₈₀₂ and Arg₈₈₀ were proposed to create a hydrogen bonding microenvironment and modulate the near attack conformation (NAC) in the presence of substrates. In order to probe the behavior of the substrates, inside the binding pocket, the electronic structure calculations were performed. Moreover, the activation of the active site was proposed to take place after the acidic proton is abstracted from the HOeq by [bmXOR]-Glu₁₂₆₁. The Oxyanion of the active site is responsible for the nucleophilic attack on the deficient carbon center of the given substrates. In general, the purpose of the study is to relate the roles of amino acid residues in the reactivities of enzyme catalyzed reactions and to determine the most favorable path way during the activation of the active site by Glu₁₂₆₁.

Published in	American Journal of Chemical and Biochemical Engineering (Volume 2, Issue 2)
DOI	10.11648/j.ajcbe.20180202.12
Page(s)	27-49
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2019. Published by Science Publishing Group

Keywords

Xanthine Oxidase, Amino Acid Residues, Proper Orientation, Active Site, Substrate, Catalysis

References

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APA Style

Temesgen Nurlign Chekol. (2019). The Role of Binding Pocket Amino Acid Residues in Substrate Specificity Towards Xanthine Oxidase Enzyme. American Journal of Chemical and Biochemical Engineering, 2(2), 27-49. https://doi.org/10.11648/j.ajcbe.20180202.12

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ACS Style

Temesgen Nurlign Chekol. The Role of Binding Pocket Amino Acid Residues in Substrate Specificity Towards Xanthine Oxidase Enzyme. Am. J. Chem. Biochem. Eng. 2019, 2(2), 27-49. doi: 10.11648/j.ajcbe.20180202.12

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AMA Style

Temesgen Nurlign Chekol. The Role of Binding Pocket Amino Acid Residues in Substrate Specificity Towards Xanthine Oxidase Enzyme. Am J Chem Biochem Eng. 2019;2(2):27-49. doi: 10.11648/j.ajcbe.20180202.12

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@article{10.11648/j.ajcbe.20180202.12,
  author = {Temesgen Nurlign Chekol},
  title = {The Role of Binding Pocket Amino Acid Residues in Substrate Specificity Towards Xanthine Oxidase Enzyme},
  journal = {American Journal of Chemical and Biochemical Engineering},
  volume = {2},
  number = {2},
  pages = {27-49},
  doi = {10.11648/j.ajcbe.20180202.12},
  url = {https://doi.org/10.11648/j.ajcbe.20180202.12},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajcbe.20180202.12},
  abstract = {Xanthine oxidase is one of the most useful molybdenum containing enzymes, which catalyzes a wide range of purine derivative heterocyclic substrates. In order for the interaction between the reactants to take place, the substrates are expected to enter the binding pocket and attain a proper orientation with the help of binding pocket amino acid residues. Therefore, the study is mainly focused to understand the role of binding pocket amino acid residues in providing the substrates proper orientation for the nucleophilic reaction to take place. The binding pocket amino acids residues in particular, Glu802 and Arg880 were proposed to create a hydrogen bonding microenvironment and modulate the near attack conformation (NAC) in the presence of substrates. In order to probe the behavior of the substrates, inside the binding pocket, the electronic structure calculations were performed. Moreover, the activation of the active site was proposed to take place after the acidic proton is abstracted from the HOeq by [bmXOR]-Glu1261. The Oxyanion of the active site is responsible for the nucleophilic attack on the deficient carbon center of the given substrates. In general, the purpose of the study is to relate the roles of amino acid residues in the reactivities of enzyme catalyzed reactions and to determine the most favorable path way during the activation of the active site by Glu1261.},
 year = {2019}
}

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TY  - JOUR
T1  - The Role of Binding Pocket Amino Acid Residues in Substrate Specificity Towards Xanthine Oxidase Enzyme
AU  - Temesgen Nurlign Chekol
Y1  - 2019/01/03
PY  - 2019
N1  - https://doi.org/10.11648/j.ajcbe.20180202.12
DO  - 10.11648/j.ajcbe.20180202.12
T2  - American Journal of Chemical and Biochemical Engineering
JF  - American Journal of Chemical and Biochemical Engineering
JO  - American Journal of Chemical and Biochemical Engineering
SP  - 27
EP  - 49
PB  - Science Publishing Group
SN  - 2639-9989
UR  - https://doi.org/10.11648/j.ajcbe.20180202.12
AB  - Xanthine oxidase is one of the most useful molybdenum containing enzymes, which catalyzes a wide range of purine derivative heterocyclic substrates. In order for the interaction between the reactants to take place, the substrates are expected to enter the binding pocket and attain a proper orientation with the help of binding pocket amino acid residues. Therefore, the study is mainly focused to understand the role of binding pocket amino acid residues in providing the substrates proper orientation for the nucleophilic reaction to take place. The binding pocket amino acids residues in particular, Glu802 and Arg880 were proposed to create a hydrogen bonding microenvironment and modulate the near attack conformation (NAC) in the presence of substrates. In order to probe the behavior of the substrates, inside the binding pocket, the electronic structure calculations were performed. Moreover, the activation of the active site was proposed to take place after the acidic proton is abstracted from the HOeq by [bmXOR]-Glu1261. The Oxyanion of the active site is responsible for the nucleophilic attack on the deficient carbon center of the given substrates. In general, the purpose of the study is to relate the roles of amino acid residues in the reactivities of enzyme catalyzed reactions and to determine the most favorable path way during the activation of the active site by Glu1261.
VL  - 2
IS  - 2
ER  -

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Author Information

Temesgen Nurlign Chekol

Department of Chemistry, College of Natural and Computational Science, Wolikite University, Wolikite, Ethiopia

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APA Style

Temesgen Nurlign Chekol. (2019). The Role of Binding Pocket Amino Acid Residues in Substrate Specificity Towards Xanthine Oxidase Enzyme. American Journal of Chemical and Biochemical Engineering, 2(2), 27-49. https://doi.org/10.11648/j.ajcbe.20180202.12

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ACS Style

Temesgen Nurlign Chekol. The Role of Binding Pocket Amino Acid Residues in Substrate Specificity Towards Xanthine Oxidase Enzyme. Am. J. Chem. Biochem. Eng. 2019, 2(2), 27-49. doi: 10.11648/j.ajcbe.20180202.12

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AMA Style

Temesgen Nurlign Chekol. The Role of Binding Pocket Amino Acid Residues in Substrate Specificity Towards Xanthine Oxidase Enzyme. Am J Chem Biochem Eng. 2019;2(2):27-49. doi: 10.11648/j.ajcbe.20180202.12

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@article{10.11648/j.ajcbe.20180202.12,
  author = {Temesgen Nurlign Chekol},
  title = {The Role of Binding Pocket Amino Acid Residues in Substrate Specificity Towards Xanthine Oxidase Enzyme},
  journal = {American Journal of Chemical and Biochemical Engineering},
  volume = {2},
  number = {2},
  pages = {27-49},
  doi = {10.11648/j.ajcbe.20180202.12},
  url = {https://doi.org/10.11648/j.ajcbe.20180202.12},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajcbe.20180202.12},
  abstract = {Xanthine oxidase is one of the most useful molybdenum containing enzymes, which catalyzes a wide range of purine derivative heterocyclic substrates. In order for the interaction between the reactants to take place, the substrates are expected to enter the binding pocket and attain a proper orientation with the help of binding pocket amino acid residues. Therefore, the study is mainly focused to understand the role of binding pocket amino acid residues in providing the substrates proper orientation for the nucleophilic reaction to take place. The binding pocket amino acids residues in particular, Glu802 and Arg880 were proposed to create a hydrogen bonding microenvironment and modulate the near attack conformation (NAC) in the presence of substrates. In order to probe the behavior of the substrates, inside the binding pocket, the electronic structure calculations were performed. Moreover, the activation of the active site was proposed to take place after the acidic proton is abstracted from the HOeq by [bmXOR]-Glu1261. The Oxyanion of the active site is responsible for the nucleophilic attack on the deficient carbon center of the given substrates. In general, the purpose of the study is to relate the roles of amino acid residues in the reactivities of enzyme catalyzed reactions and to determine the most favorable path way during the activation of the active site by Glu1261.},
 year = {2019}
}

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TY  - JOUR
T1  - The Role of Binding Pocket Amino Acid Residues in Substrate Specificity Towards Xanthine Oxidase Enzyme
AU  - Temesgen Nurlign Chekol
Y1  - 2019/01/03
PY  - 2019
N1  - https://doi.org/10.11648/j.ajcbe.20180202.12
DO  - 10.11648/j.ajcbe.20180202.12
T2  - American Journal of Chemical and Biochemical Engineering
JF  - American Journal of Chemical and Biochemical Engineering
JO  - American Journal of Chemical and Biochemical Engineering
SP  - 27
EP  - 49
PB  - Science Publishing Group
SN  - 2639-9989
UR  - https://doi.org/10.11648/j.ajcbe.20180202.12
AB  - Xanthine oxidase is one of the most useful molybdenum containing enzymes, which catalyzes a wide range of purine derivative heterocyclic substrates. In order for the interaction between the reactants to take place, the substrates are expected to enter the binding pocket and attain a proper orientation with the help of binding pocket amino acid residues. Therefore, the study is mainly focused to understand the role of binding pocket amino acid residues in providing the substrates proper orientation for the nucleophilic reaction to take place. The binding pocket amino acids residues in particular, Glu802 and Arg880 were proposed to create a hydrogen bonding microenvironment and modulate the near attack conformation (NAC) in the presence of substrates. In order to probe the behavior of the substrates, inside the binding pocket, the electronic structure calculations were performed. Moreover, the activation of the active site was proposed to take place after the acidic proton is abstracted from the HOeq by [bmXOR]-Glu1261. The Oxyanion of the active site is responsible for the nucleophilic attack on the deficient carbon center of the given substrates. In general, the purpose of the study is to relate the roles of amino acid residues in the reactivities of enzyme catalyzed reactions and to determine the most favorable path way during the activation of the active site by Glu1261.
VL  - 2
IS  - 2
ER  -

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