Literature DB >> 26419727

Environmental roles of microbial amino acid racemases.

Sara B Hernández1, Felipe Cava1.   

Abstract

Enzymes catalysing the stereo-chemical inter-conversion of amino acids are known as amino acid racemases. In bacteria, these enzymes are fundamental to synthesize the D-Ala and D-Glu that are critical components of the peptidoglycan. In addition to this structural function in cell wall assembly, D-amino acids produced by microbial amino acid racemases have been described as relevant constituents in other prokaryotic structures (e.g. capsule, non-ribosomal peptides) and have been associated to growth fitness and to processes such as biofilm development, spore germination and signalling. The recent discovery of broad spectrum racemases able to produce and release several D-amino acids to the environment suggests that these enzymes might have a great impact in microbial ecology. Consequently, new data on the biochemistry and regulation of racemases is key to understand the biological significance of D-enantiomers in nature, in particular their effect on microbial social networks. This review summarizes current knowledge on the environmental roles of bacterial racemases with an emphasis on the potential roles of the new broad spectrum enzymes in natural environments.
© 2015 Society for Applied Microbiology and John Wiley & Sons Ltd.

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Year:  2015        PMID: 26419727     DOI: 10.1111/1462-2920.13072

Source DB:  PubMed          Journal:  Environ Microbiol        ISSN: 1462-2912            Impact factor:   5.491


  19 in total

1.  D-fining DarR: a LysR-type transcriptional regulator that responds to D-aspartate.

Authors:  Mark J Mandel
Journal:  J Bacteriol       Date:  2018-03-19       Impact factor: 3.490

2.  Vibrio fischeri DarR Directs Responses to d-Aspartate and Represents a Group of Similar LysR-Type Transcriptional Regulators.

Authors:  Richard M Jones; David L Popham; Alicia L Schmidt; Ellen L Neidle; Eric V Stabb
Journal:  J Bacteriol       Date:  2018-07-10       Impact factor: 3.490

3.  TK1211 Encodes an Amino Acid Racemase towards Leucine and Methionine in the Hyperthermophilic Archaeon Thermococcus kodakarensis.

Authors:  Ren-Chao Zheng; Xia-Feng Lu; Hiroya Tomita; Shin-Ichi Hachisuka; Yu-Guo Zheng; Haruyuki Atomi
Journal:  J Bacteriol       Date:  2021-03-08       Impact factor: 3.490

4.  Identification and biochemical characterization of threonine dehydratase from the hyperthermophile Thermotoga maritima.

Authors:  Tetsuya Miyamoto; Masumi Katane; Yasuaki Saitoh; Masae Sekine; Kumiko Sakai-Kato; Hiroshi Homma
Journal:  Amino Acids       Date:  2021-05-03       Impact factor: 3.520

5.  Function of alanine racemase in the physiological activity and cariogenicity of Streptococcus mutans.

Authors:  Shiyu Liu; Yuan Wei; Xuedong Zhou; Keke Zhang; Xian Peng; Biao Ren; Vivian Chen; Lei Cheng; Mingyun Li
Journal:  Sci Rep       Date:  2018-04-13       Impact factor: 4.379

Review 6.  New Insights Into the Mechanisms and Biological Roles of D-Amino Acids in Complex Eco-Systems.

Authors:  Alena Aliashkevich; Laura Alvarez; Felipe Cava
Journal:  Front Microbiol       Date:  2018-04-06       Impact factor: 5.640

7.  Understanding the Interactions between Staphylococcus aureus and the Raw-Meat-Processing Environment Isolate Klebsiella oxytoca in Dual-Species Biofilms via Discovering an Altered Metabolic Profile.

Authors:  Xiaoxue Chen; Yunan Hu; Simin Tian; Beizhong Han
Journal:  Microorganisms       Date:  2021-03-24

8.  Microbial turnover times in the deep seabed studied by amino acid racemization modelling.

Authors:  Stefan Braun; Snehit S Mhatre; Marion Jaussi; Hans Røy; Kasper U Kjeldsen; Christof Pearce; Marit-Solveig Seidenkrantz; Bo Barker Jørgensen; Bente Aa Lomstein
Journal:  Sci Rep       Date:  2017-07-18       Impact factor: 4.379

9.  d-Amino Acids Are Exuded by Arabidopsis thaliana Roots to the Rhizosphere.

Authors:  Claudia Hener; Sabine Hummel; Juan Suarez; Mark Stahl; Üner Kolukisaoglu
Journal:  Int J Mol Sci       Date:  2018-04-07       Impact factor: 5.923

10.  A Novel PLP-Dependent Alanine/Serine Racemase From the Hyperthermophilic Archaeon Pyrococcus horikoshii OT-3.

Authors:  Ryushi Kawakami; Tatsuya Ohshida; Haruhiko Sakuraba; Toshihisa Ohshima
Journal:  Front Microbiol       Date:  2018-07-09       Impact factor: 5.640

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