Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer: Role of an active site asparagine residue in activation of methyl transfer by methyltransferases

Journal of Biological Chemistry

Volumn 282, Issue 9, 2007, Pages 6609-6618

  Doukov, Tzanko I ^b,c   Hemmi, Hisashi ^a,d   Drennan, Catherine L ^b   Ragsdale, Stephen W ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^c SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

^d NAGOYA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE RESIDUE; ELECTROPHILIC ACTIVATION; NUCLEOSIDE PHOSPHORYLASE; PROTON DONORA;

AMIDES; CATALYSIS; HYDROGEN BONDS; REACTION KINETICS; WATER;

ENZYME KINETICS;

5 METHYLTETRAHYDROFOLIC ACID; ASPARAGINE; CARBON DIOXIDE; CARBON MONOXIDE; COBALAMIN; CORRINOID IRON SULFUR PROTEIN; GLUTAMIC ACID; IRON SULFUR PROTEIN; METHYL GROUP; METHYLTRANSFERASE; PURINE NUCLEOSIDE PHOSPHORYLASE; UNCLASSIFIED DRUG; WATER; FOLIC ACID; PROTON;

ARTICLE; ATOM; BINDING KINETICS; CARBON FIXATION; CATALYSIS; CONTROLLED STUDY; ENERGY; ENZYME ACTIVE SITE; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME STRUCTURE; HYDROGEN BOND; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; STRUCTURE ANALYSIS; BINDING SITE; CHEMISTRY; ENZYME ACTIVATION; KINETICS; METABOLISM;

ASPARAGINE; BINDING SITES; CATALYSIS; ENZYME ACTIVATION; FOLIC ACID; HYDROGEN BONDING; KINETICS; METHYLTRANSFERASES; PROTONS; WATER;

EID: 34250362770     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M609828200     Document Type: Article

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