QM Study on the Mechanism of Carbonic Anhydrase II Inhibition with Glycosylcoumarin as Non-Zinc Mediated Inhibitors from Thermodynamic View Point Article Swipe
Mina Ghiasi
,
Mina Seifi
·
YOU?
·
· 2017
· Open Access
·
· DOI: https://doi.org/10.5281/zenodo.3336408
YOU?
·
· 2017
· Open Access
·
· DOI: https://doi.org/10.5281/zenodo.3336408
Carbonic anhydrase is an enzyme which has the zinc as the metallic part of it. This enzyme catalyzes the reversible reaction of turning carbon dioxide into bicarbonate. In this research the mechanism of inhibition a new class of inhibitor of this enzyme, glycosyl coumarin has been modeled using the density functional theory (DFT). First, the most constant confirmer of this four coumarin sugar derivatives which includes galactose, mannose, ribose and glucose has been selected and then they had been interacted as inhibitor with CA (II) enzyme’s active site. In further for showing the effect of sugar in these molecules, coumarin itself had been chosen as inhibitor and the inhibitory effect is surveyed. All calculations have been done by density functional theory in level of B3LYP with basic set 6-31G* and with Minnesota function M06 with basic set 6-31+G*. Thermodynamic functions like enthalpy of formation, entropy of formation and Gibbs free energy for CA-inhibitor have been computed. The results indicate that the reaction among these groups of inhibitors and Carbonic anhydrase is not of the type of direct and syndetic but the enzyme is deactivated with space effect and addition to this, the computed thermodynamic functions show that although this coumarin sugar derives have deterrence in the range of micro molar but, coumarin without sugar is a stronger deterrence for CA II. Finally, the interaction between the most constant confirmer (galactose coumarin) is surveyed as the best deterrence using the explicit solvent method.
Related Topics
Concepts
Carbonic anhydrase
Mechanism (biology)
Zinc
Chemistry
Carbonic anhydrase II
Enzyme
Biochemistry
Philosophy
Epistemology
Organic chemistry
Metadata
- Type
- article
- Language
- en
- Landing Page
- https://zenodo.org/record/3336408
- OA Status
- green
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4300226049
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4300226049Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.5281/zenodo.3336408Digital Object Identifier
- Title
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QM Study on the Mechanism of Carbonic Anhydrase II Inhibition with Glycosylcoumarin as Non-Zinc Mediated Inhibitors from Thermodynamic View PointWork title
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articleOpenAlex work type
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enPrimary language
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2017Year of publication
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2017-07-15Full publication date if available
- Authors
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Mina Ghiasi, Mina SeifiList of authors in order
- Landing page
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https://zenodo.org/record/3336408Publisher landing page
- Open access
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YesWhether a free full text is available
- OA status
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greenOpen access status per OpenAlex
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https://zenodo.org/record/3336408Direct OA link when available
- Concepts
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Carbonic anhydrase, Mechanism (biology), Zinc, Chemistry, Carbonic anhydrase II, Enzyme, Biochemistry, Philosophy, Epistemology, Organic chemistryTop concepts (fields/topics) attached by OpenAlex
- Cited by
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0Total citation count in OpenAlex
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10Other works algorithmically related by OpenAlex
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| citation_normalized_percentile.value | 0.26282535 |
| citation_normalized_percentile.is_in_top_1_percent | False |
| citation_normalized_percentile.is_in_top_10_percent | False |