NDLI: A computational study on the amine-oxidation mechanism of monoamine oxidase: Insight into the polar nucleophilic mechanism

Please wait, while we are loading the content...

A unique NH-spacer for N-benzamidothiourea based anion sensors. Substituent effect on anion sensing of the ICT dual fluorescent N-(p-dimethylaminobenzamido)-N′-arylthioureas

Spontaneity in the patellamide biosynthetic pathway

RNA binding and thiolytic stability of a quinoline-containing helix-threading peptide

A computational study on the amine-oxidation mechanism of monoamine oxidase: Insight into the polar nucleophilic mechanism

Utilization of 3′-carboxy-containing tyrosine derivatives as a new class of phosphotyrosyl mimetics in the preparation of novel non-phosphorylated cyclic peptide inhibitors of the Grb2–SH2 domain

A versatile template for the formation of [2]pseudorotaxanes. 1,2-Bis(pyridinium)ethane axles and 24-crown-8 ether wheels

Synthesis of bisubstrate analogues targeting α-1,3-fucosyltransferase and their activities

Unprecedented chemical structure and biomimetic synthesis of erucalexin, a phytoalexin from the wild crucifer Erucastrum gallicum

Non-equivalence of d- and l-trehalose in stabilising alkaline phosphatase against freeze-drying and thermal stress. Is chiral recognition involved?

The influence of phenyl and phenoxy modification in the hydrophobic tails of di-n-alkyl phosphate amphiphiles on aggregate morphology

Formation of lactones from sialylated MUC1 glycopeptides

¹⁵N CIDNP investigations of the peroxynitric acid nitration of l-tyrosine and of related compounds

Incorporation of deuterium-labelled analogs of isopentenyl diphosphate for the elucidation of the stereochemistry of rubber biosynthesis

Back cover

Organic & Biomolecular Chemistry Vol - 4 Issue - 3

Organic & Biomolecular Chemistry Vol -3

Organic & Biomolecular Chemistry Vol -2

A computational study on the amine-oxidation mechanism of monoamine oxidase: Insight into the polar nucleophilic mechanism

Content Provider	Royal Society of Chemistry (RSC)
Author	Yelekçi, Kemal Erdem, Safiye Sağ Yıldız, İbrahim Karahan, Özlem
Copyright Year	2006
Abstract	The proposed polar nucleophilic mechanism of MAO was investigated using quantum chemical calculations employing the semi-empirical PM3 method. In order to mimic the reaction at the enzyme's active site, the reactions between the flavin and the p-substituted benzylamine substrate analogs were modeled. Activation energies and rate constants of all the reactions were calculated and compared with the published experimental data. The results showed that electron-withdrawing groups at the para position of benzylamine increase the reaction rate. A good correlation between the log of the calculated rate constants and the electronic parameter (σ) of the substituent was obtained. These results agree with the previous kinetic experiments on the effect of p-substituents on the reduction of MAO-A by benzylamine analogs. In addition, the calculated rate constants showed a correlation with the rate of reduction of the flavin in MAO-A. In order to verify the results obtained from the PM3 method single-point B3LYP/6-31G//PM3 calculations were performed. These results demonstrated a strong reduction in the activation energy for the reaction of benzylamine derivatives having electron-withdrawing substituents, which is in agreement with the PM3 calculations and the previous experimental QSAR study. PM3 and B3LYP/6-31G energy surfaces were obtained for the overall reaction of benzylamine with flavin. Results suggest that PM3 is a reasonable method for studying this kind of reaction. These theoretical findings support the proposed polar nucleophilic mechanism for MAO-A.
Starting Page	646
Ending Page	658
Page Count	13
File Format	HTM / HTML PDF
ISSN	14770520
Volume Number	4
Issue Number	4
Journal	Organic & Biomolecular Chemistry
DOI	10.1039/b511350d
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Enzyme Quantum mechanics Active site Quantitative structure\u2013activity relationship Substituent Benzylamine Reaction rate New Shepard Activation energy
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry Physical and Theoretical Chemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Active-Site Titration of Pig-Plasma Benzylamine Oxidase

Kinetics and mechanism of 1,3-cycloadditions of benzonitrile N-oxides to thiobenzophenones

Triple molecular target approach to selective melanoma cytotoxicity

The Mechanism of Inhibition of Benzylamine Oxidase by 3,5-Diethoxy-4-Aminomethylpyridine (B24)

Active-Site Titration of Pig-Plasma Benzylamine Oxidase with Hydrazine Derivatives

Amine Oxidation Mediated by N-Methyltryptophan Oxidase: Computational Insights into the Mechanism, Role of Active-Site Residues, and Covalent Flavin Binding

Analysis of Conserved Active Site Residues in Monoamine Oxidase A and B and Their Three-dimensional Molecular

Crystallographic snapshots of the complete reaction cycle of nicotine degradation by an amine oxidase of the monoamine oxidase (MAO) family.

Reaction Mechanism of Monoamine Oxidase from QM/MM Calculations

A computational study on the amine-oxidation mechanism of monoamine oxidase: Insight into the polar nucleophilic mechanism

Similar Documents

Active-Site Titration of Pig-Plasma Benzylamine Oxidase

Kinetics and mechanism of 1,3-cycloadditions of benzonitrile N-oxides to thiobenzophenones

Triple molecular target approach to selective melanoma cytotoxicity

The Mechanism of Inhibition of Benzylamine Oxidase by 3,5-Diethoxy-4-Aminomethylpyridine (B24)

Active-Site Titration of Pig-Plasma Benzylamine Oxidase with Hydrazine Derivatives

Amine Oxidation Mediated by N-Methyltryptophan Oxidase: Computational Insights into the Mechanism, Role of Active-Site Residues, and Covalent Flavin Binding

Analysis of Conserved Active Site Residues in Monoamine Oxidase A and B and Their Three-dimensional Molecular

Crystallographic snapshots of the complete reaction cycle of nicotine degradation by an amine oxidase of the monoamine oxidase (MAO) family.

Reaction Mechanism of Monoamine Oxidase from QM/MM Calculations

A computational study on the amine-oxidation mechanism of monoamine oxidase: Insight into the polar nucleophilic mechanism