The reaction mechanism of phenylethanolamine N-methyltransferase: a density functional theory study. - Wikidata - wikimedia - TriplyDB

The reaction mechanism of phenylethanolamine N-methyltransferase: a density functional theory study.

The reaction mechanism of phenylethanolamine N-methyltransferase: a density functional theory study.

http://www.wikidata.org/entity/Q37384529

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Structures of dimethylsulfoniopropionate-dependent demethylase from the marine organismPelagabacter ubique Kinetic and pH studies on human phenylethanolamine N-methyltransferase.Computational enzymatic catalysis--clarifying enzymatic mechanisms with the help of computers.The chemical biology of dimethylsulfoniopropionate.Exploring the Dependence of QM/MM Calculations of Enzyme Catalysis on the Size of the QM Region.Kinetic Isotope Effects and Transition State Structure for Human Phenylethanolamine N-Methyltransferase.Theoretical study of methyl group transfer assisted by proton transfer reaction in the N-acylated imidates.

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P2860

The reaction mechanism of phenylethanolamine N-methyltransferase: a density functional theory study.

http://www.wikidata.org/entity/Q37384529

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 03 September 2009

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vedecký článok

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vetenskaplig artikel

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The reaction mechanism of phen ...... nsity functional theory study.

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The reaction mechanism of phen ...... nsity functional theory study.

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The reaction mechanism of phen ...... nsity functional theory study.

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The reaction mechanism of phen ...... nsity functional theory study.

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J.BBAPAP.2009.08.022

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Biochimica et Biophysica Acta

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The reaction mechanism of phen ...... ensity functional theory study

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Fahmi Himo

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Qian Wu

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Density-functional exchange-energy approximation with correct asymptotic behavior

Very fast prediction and rationalization of pKa values for protein-ligand complexes

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Catalytic mechanism of glycine N-methyltransferase

Molecular recognition of sub-micromolar inhibitors by the epinephrine-synthesizing enzyme phenylethanolamine N-methyltransferase

Enzyme adaptation to inhibitor binding: a cryptic binding site in phenylethanolamine N-methyltransferase

Disulfide-linked dimers of human adrenaline synthesizing enzyme PNMT are catalytically active

Catalytic mechanism of guanidinoacetate methyltransferase: crystal structures of guanidinoacetate methyltransferase ternary complexes

Many paths to methyltransfer: a chronicle of convergence

Very fast empirical prediction and rationalization of protein pKa values

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