Literature DB >> 25646533

Bacterial pectate lyases, structural and functional diversity.

Nicole Hugouvieux-Cotte-Pattat, Guy Condemine, Vladimir E Shevchik.   

Abstract

Pectate lyases are enzymes involved in plant cell wall degradation. They cleave pectin using a β-elimination mechanism, specific for acidic polysaccharides. They are mainly produced by plant pathogens and plant-associated organisms, and only rarely by animals. Pectate lyases are also commonly produced in the bacterial world, either by bacteria living in close proximity with plants or by gut bacteria that find plant material in the digestive tract of their hosts. The role of pectate lyases is essential for plant pathogens, such as Dickeya dadantii, that use a set of pectate lyases as their main virulence factor. Symbiotic bacteria produce their own pectate lyases, but they also induce plant pectate lyases to initiate the symbiosis. Pectin degradation products may act as signals affecting the plant–bacteria interactions. Bacterial pectate lyases are also essential for using the pectin of dead or living plants as a carbon source for growth. In the animal gut, Bacteroides pectate lyases degrade the pectin of ingested food, and this is particularly important for herbivores that depend on their microflora for the digestion of pectin. Some human pathogens, such as Yersinia enterocolitica, produce a few intracellular pectate lyases that can facilitate their growth in the presence of highly pectinolytic bacteria, at the plant surface, in the soil or in the animal gut.

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Year:  2014        PMID: 25646533     DOI: 10.1111/1758-2229.12166

Source DB:  PubMed          Journal:  Environ Microbiol Rep        ISSN: 1758-2229            Impact factor:   3.541


  45 in total

1.  Distinguishing allergens from non-allergenic homologues using Physical-Chemical Property (PCP) motifs.

Authors:  Wenzhe Lu; Surendra S Negi; Catherine H Schein; Soheila J Maleki; Barry K Hurlburt; Werner Braun
Journal:  Mol Immunol       Date:  2018-04-06       Impact factor: 4.407

2.  Transcriptome analysis of the Dickeya dadantii PecS regulon during the early stages of interaction with Arabidopsis thaliana.

Authors:  Jacques Pédron; Emilie Chapelle; Benoît Alunni; Frédérique Van Gijsegem
Journal:  Mol Plant Pathol       Date:  2017-05-03       Impact factor: 5.663

3.  The purification and characterization of a novel alkali-stable pectate lyase produced by Bacillus subtilis PB1.

Authors:  Man Zhou; Jingli Wu; Tao Wang; Lina Gao; Huijun Yin; Xin Lü
Journal:  World J Microbiol Biotechnol       Date:  2017-10-03       Impact factor: 3.312

4.  Differential proteomics reveals main determinants for the improved pectinase activity in UV-mutagenized Aspergillus niger strain.

Authors:  Weiling Lin; Xiaohong Xu; Ruirui Lv; Wei Huang; Hafeez Ul Haq; Yuanyuan Gao; Hongli Ren; Canhua Lan; Baoyu Tian
Journal:  Biotechnol Lett       Date:  2021-01-15       Impact factor: 2.461

5.  Biochemical Characterization of a Pectate Lyase AnPL9 from Aspergillus nidulans.

Authors:  Hiromitsu Suzuki; Toshiki Morishima; Atsuya Handa; Hironaka Tsukagoshi; Masashi Kato; Motoyuki Shimizu
Journal:  Appl Biochem Biotechnol       Date:  2022-07-08       Impact factor: 2.926

6.  Standard Candles for Dating Microbial Lineages.

Authors:  Gregory P Fournier; Chris W Parsons; Elise M Cutts; Erik Tamre
Journal:  Methods Mol Biol       Date:  2022

7.  Exploration of Two Pectate Lyases from Caldicellulosiruptor bescii Reveals that the CBM66 Module Has a Crucial Role in Pectic Biomass Degradation.

Authors:  Hamed I Hamouda; Nasir Ali; Hang Su; Jie Feng; Ming Lu; Fu-Li Li
Journal:  Appl Environ Microbiol       Date:  2020-08-03       Impact factor: 4.792

8.  Genomic insights from Monoglobus pectinilyticus: a pectin-degrading specialist bacterium in the human colon.

Authors:  Caroline C Kim; Genelle R Healey; William J Kelly; Mark L Patchett; Zoe Jordens; Gerald W Tannock; Ian M Sims; Tracey J Bell; Duncan Hedderley; Bernard Henrissat; Douglas I Rosendale
Journal:  ISME J       Date:  2019-02-06       Impact factor: 10.302

9.  Genes for degradation and utilization of uronic acid-containing polysaccharides of a marine bacterium Catenovulum sp. CCB-QB4.

Authors:  Go Furusawa; Nor Azura Azami; Aik-Hong Teh
Journal:  PeerJ       Date:  2021-03-09       Impact factor: 2.984

10.  Tricarboxylic Acid (TCA) Cycle Enzymes and Intermediates Modulate Intracellular Cyclic di-GMP Levels and the Production of Plant Cell Wall-Degrading Enzymes in Soft Rot Pathogen Dickeya dadantii.

Authors:  Xiaochen Yuan; Quan Zeng; Jingsheng Xu; Geoffrey B Severin; Xiang Zhou; Christopher M Waters; George W Sundin; Abasiofiok M Ibekwe; Fengquan Liu; Ching-Hong Yang
Journal:  Mol Plant Microbe Interact       Date:  2019-12-18       Impact factor: 3.422

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