Literature DB >> 3122748

The greater strength of arginine: carboxylate over lysine carboxylate ion pairs implications for the design of novel enzymes and drugs.

D B Wigley1, A Lyall, K W Hart, J J Holbrook.   

Abstract

The rational design of enzyme catalysts for chiral chemistry and of drugs which bind to proteins would be facilitated if rules for the recognition of one partner by the other could be formulated. This communication suggests and tests one generalization: arginine forms a tighter ion pair with a carboxylate group than does lysine and is always used for ion-pairs which are not broken during turnover in naturally-occurring enzymes.

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Year:  1987        PMID: 3122748     DOI: 10.1016/0006-291x(87)90497-9

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  4 in total

1.  Insight into the role of substrate-binding residues in conferring substrate specificity for the multifunctional polysaccharide lyase Smlt1473.

Authors:  Logan C MacDonald; Bryan W Berger
Journal:  J Biol Chem       Date:  2014-05-07       Impact factor: 5.157

2.  Allosteric Regulation in the Ligand Binding Domain of Retinoic Acid Receptorγ.

Authors:  Yassmine Chebaro; Serena Sirigu; Ismail Amal; Régis Lutzing; Roland H Stote; Cécile Rochette-Egly; Natacha Rochel; Annick Dejaegere
Journal:  PLoS One       Date:  2017-01-26       Impact factor: 3.240

3.  Evaluation of phenylpiperazines as targeting agents for neuroblastoma.

Authors:  J W Babich; W A Graham; A J Fischman
Journal:  Br J Cancer       Date:  1996-09       Impact factor: 7.640

4.  Structural basis for the interaction of the adaptor protein grb14 with activated ras.

Authors:  Rohini Qamra; Stevan R Hubbard
Journal:  PLoS One       Date:  2013-08-13       Impact factor: 3.240

  4 in total

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