Literature DB >> 7855594

A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acids.

P C Babbitt1, G T Mrachko, M S Hasson, G W Huisman, R Kolter, D Ringe, G A Petsko, G L Kenyon, J A Gerlt.   

Abstract

Mandelate racemase and muconate lactonizing enzyme are structurally homologous but catalyze different reactions, each initiated by proton abstraction from carbon. The structural similarity to mandelate racemase of a previously unidentified gene product was used to deduce its function as a galactonate dehydratase. In this enzyme superfamily that has evolved to catalyze proton abstraction from carbon, three variations of homologous active site architectures are now represented: lysine and histidine bases in the active site of mandelate racemase, only a lysine base in the active site of muconate lactonizing enzyme, and only a histidine base in the active site of galactonate dehydratase. This discovery supports the hypothesis that new enzymatic activities evolve by recruitment of a protein catalyzing the same type of chemical reaction.

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Year:  1995        PMID: 7855594     DOI: 10.1126/science.7855594

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  36 in total

1.  A test case for structure-based functional assignment: the 1.2 A crystal structure of the yjgF gene product from Escherichia coli.

Authors:  K Volz
Journal:  Protein Sci       Date:  1999-11       Impact factor: 6.725

2.  Functional prediction: identification of protein orthologs and paralogs.

Authors:  R Chen; S S Jeong
Journal:  Protein Sci       Date:  2000-12       Impact factor: 6.725

Review 3.  Divergence and convergence in enzyme evolution: parallel evolution of paraoxonases from quorum-quenching lactonases.

Authors:  Mikael Elias; Dan S Tawfik
Journal:  J Biol Chem       Date:  2011-11-08       Impact factor: 5.157

4.  Evolution of enzymatic activities of testis-specific short-chain dehydrogenase/reductase in Drosophila.

Authors:  Jianming Zhang; Huyuan Yang; Manyuan Long; Liming Li; Antony M Dean
Journal:  J Mol Evol       Date:  2010-08-31       Impact factor: 2.395

5.  On roads not taken in the evolution of protein catalysts: antibody steroid isomerases that use an enamine mechanism.

Authors:  C H Lin; T Z Hoffman; P Wirsching; C F Barbas; K D Janda; R A Lerner
Journal:  Proc Natl Acad Sci U S A       Date:  1997-10-28       Impact factor: 11.205

6.  The evolutionary origins and catalytic importance of conserved electrostatic networks within TIM-barrel proteins.

Authors:  Dennis R Livesay; David La
Journal:  Protein Sci       Date:  2005-05       Impact factor: 6.725

7.  An L-glucose catabolic pathway in Paracoccus species 43P.

Authors:  Tetsu Shimizu; Naoki Takaya; Akira Nakamura
Journal:  J Biol Chem       Date:  2012-10-04       Impact factor: 5.157

8.  Biosynthesis of a D-amino acid in peptide linkage by an enzyme from frog skin secretions.

Authors:  Alexander Jilek; Christa Mollay; Christa Tippelt; Jacques Grassi; Giuseppina Mignogna; Johannes Müllegger; Veronika Sander; Christine Fehrer; Donatella Barra; Günther Kreil
Journal:  Proc Natl Acad Sci U S A       Date:  2005-03-09       Impact factor: 11.205

9.  Molecular and Functional Insights into the Regulation of d-Galactonate Metabolism by the Transcriptional Regulator DgoR in Escherichia coli.

Authors:  Bhupinder Singh; Garima Arya; Neeladrita Kundu; Akshay Sangwan; Shachikanta Nongthombam; Rachna Chaba
Journal:  J Bacteriol       Date:  2019-01-28       Impact factor: 3.490

10.  Convergent evolution sheds light on the anti-beta -elimination mechanism common to family 1 and 10 polysaccharide lyases.

Authors:  Simon J Charnock; Ian E Brown; Johan P Turkenburg; Gary W Black; Gideon J Davies
Journal:  Proc Natl Acad Sci U S A       Date:  2002-09-09       Impact factor: 11.205

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