Literature DB >> 11513844

Expansion of the zinc metallo-hydrolase family of the beta-lactamase fold.

H Daiyasu1, K Osaka, Y Ishino, H Toh.   

Abstract

Recently, the zinc metallo-hydrolase family of the beta-lactamase fold has grown quite rapidly, accompanied by the accumulation of sequence and structure data. The variety of the biological functions of the family is higher than expected. In addition, the members often have mosaic structures with additional domains. The family includes class B beta-lactamase, glyoxalase II, arylsulfatase, flavoprotein, cyclase/dehydrase, an mRNA 3'-processing protein, a DNA cross-link repair enzyme, a DNA uptake-related protein, an alkylphosphonate uptake-related protein, CMP-N-acetylneuraminate hydroxylase, the romA gene product, alkylsulfatase, and insecticide hydrolases. In this minireview, the functional and structural varieties of the growing protein family are described.

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Year:  2001        PMID: 11513844     DOI: 10.1016/s0014-5793(01)02686-2

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  107 in total

1.  Spectroscopic signature of a ubiquitous metal binding site in the metallo-β-lactamase superfamily.

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2.  The Ti plasmid of Agrobacterium tumefaciens harbors an attM-paralogous gene, aiiB, also encoding N-Acyl homoserine lactonase activity.

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Journal:  Appl Environ Microbiol       Date:  2003-08       Impact factor: 4.792

3.  Update of the standard numbering scheme for class B beta-lactamases.

Authors:  Gianpiero Garau; Isabel García-Sáez; Carine Bebrone; Christine Anne; Paola Mercuri; Moreno Galleni; Jean-Marie Frère; Otto Dideberg
Journal:  Antimicrob Agents Chemother       Date:  2004-07       Impact factor: 5.191

4.  In vivo impact of Met221 substitution in GOB metallo-β-lactamase.

Authors:  Jorgelina Morán-Barrio; María-Natalia Lisa; Alejandro J Vila
Journal:  Antimicrob Agents Chemother       Date:  2012-01-17       Impact factor: 5.191

Review 5.  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

6.  Euryarchaeal beta-CASP proteins with homology to bacterial RNase J Have 5'- to 3'-exoribonuclease activity.

Authors:  Béatrice Clouet-d'Orval; Dana Rinaldi; Yves Quentin; Agamemnon J Carpousis
Journal:  J Biol Chem       Date:  2010-04-07       Impact factor: 5.157

7.  Characterization of a novel metallo-β-lactamases fold hydrolase from Pelagibacterium halotolerans, a marine halotolerant bacterium isolated from East China Sea.

Authors:  Beiwen Zheng; Xiawei Jiang; Zemin Xu; Yunhui Fang; Lanjuan Li
Journal:  Extremophiles       Date:  2015-11-03       Impact factor: 2.395

8.  Functional Profiling and Crystal Structures of Isothiocyanate Hydrolases Found in Gut-Associated and Plant-Pathogenic Bacteria.

Authors:  Tijs J M van den Bosch; Kemin Tan; Andrzej Joachimiak; Cornelia U Welte
Journal:  Appl Environ Microbiol       Date:  2018-07-02       Impact factor: 4.792

9.  The quorum-quenching metallo-gamma-lactonase from Bacillus thuringiensis exhibits a leaving group thio effect.

Authors:  Jessica Momb; Pei W Thomas; Robert M Breece; David L Tierney; Walter Fast
Journal:  Biochemistry       Date:  2006-11-07       Impact factor: 3.162

10.  Metallo-beta-lactamase fold within nucleic acids processing enzymes: the beta-CASP family.

Authors:  Isabelle Callebaut; Despina Moshous; Jean-Paul Mornon; Jean-Pierre de Villartay
Journal:  Nucleic Acids Res       Date:  2002-08-15       Impact factor: 16.971

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