A novel ATP dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-CoA

Li, Chunyang; Wang, Xiujuan; Chen, Xiu-Lan; Sheng, Qi; Zhang, Shan; Wang, Peng; Quareshy, Mussa; Rihtman, Branko; Shao, Xuan; Gao, Chao; Li, Fuchuan; Li, Shengying; Zhang, Weipeng; Zhang, Xiaohua; Yang, Gui‐Peng; Todd, Jonathan D.; Yin, Chengqing; Zhang, Yuzhong

doi:10.7554/elife.64045

Cited by 46 publications

(44 citation statements)

References 65 publications

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“…The crystal structure and mechanism of DMSP cleavage of some DMSP lyase enzymes such as DddD, DddL, DddW and Alma1 are yet to be solved. (Landa et al, 2019;Li et al, 2021). Fig.…”

Section: Discussionmentioning

confidence: 98%

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Recent insights into oceanic dimethylsulfoniopropionate biosynthesis and catabolism

Shaw

Sekar

Prabavathy

2022

Environmental Microbiology

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Dimethylsulfoniopropionate (DMSP), a globally important organosulfur compound is produced in prodigious amounts (2.0 Pg sulfur) annually in the marine environment by phytoplankton, macroalgae, heterotrophic bacteria, some corals and certain higher plants. It is an important marine osmolyte and a major precursor molecule for the production of climate-active volatile gas dimethyl sulfide (DMS). DMSP synthesis take place via three pathways: a transamination 'pathway-' in some marine bacteria and algae, a Met-methylation 'pathway-' in angiosperms and bacteria and a decarboxylation 'pathway-' in the dinoflagellate, Crypthecodinium. The enzymes DSYB and TpMMT are involved in the DMSP biosynthesis in eukaryotes while marine heterotrophic bacteria engage key enzymes such as DsyB and MmtN. Several marine bacterial communities import DMSP and degrade it via cleavage or demethylation pathways or oxidation pathway, thereby generating DMS, methanethiol, and dimethylsulfoxonium propionate, respectively. DMSP is cleaved through diverse DMSP lyase enzymes in bacteria and via Alma1 enzyme in phytoplankton. The demethylation pathway involves four different enzymes, namely DmdA, DmdB, DmdC and DmdD/AcuH. However, enzymes involved in the oxidation pathway have not been yet identified. We reviewed the recent advances on the synthesis and catabolism of DMSP and enzymes that are involved in these processes.

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“…The crystal structure and mechanism of DMSP cleavage of some DMSP lyase enzymes such as DddD, DddL, DddW and Alma1 are yet to be solved. (Landa et al, 2019;Li et al, 2021). Fig.…”

Section: Discussionmentioning

confidence: 98%

“…Here, we have concentrated on most recent findings (Alcolombri et al, 2014;Hehemann et al, 2014;Li et al, 2014;Alcolombri et al, 2015;Brummett et al, 2015;Wang et al, 2015;Brummett and Dey, 2016;Sun et al, 2016;Li et al, 2017;Schnicker et al, 2017;Peng et al, 2019;Li et al, 2021).…”

Section: Dmsp Cleavage Pathwaysmentioning

confidence: 99%

Recent insights into oceanic dimethylsulfoniopropionate biosynthesis and catabolism

Shaw

Sekar

Prabavathy

2022

Environmental Microbiology

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“…(1,3 X2) and 1,3-xylotriose (1,3 X3) were collected for further use (Supplementary Figure 1). (Li et al, 2021). The pH was adjusted to 8.0 with HCl to keep consistence with that of the sampling sites (8.0-8.2).…”

Section: 3-xylan and 13-xylooligosaccharides Preparationmentioning

confidence: 99%

Diversity of Marine 1,3-Xylan-Utilizing Bacteria and Characters of Their Extracellular 1,3-Xylanases

Sun

et al. 2021

Front. Microbiol.

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1,3-xylan is present in the cell walls of some red and green algae and is an important organic carbon in the ocean. However, information on its bacterial degradation is quite limited. Here, after enrichment with 1,3-xylan, the diversity of bacteria recovered from marine algae collected in Hainan, China, was analyzed with both the 16S rRNA gene amplicon sequencing and the culture-dependent method. Bacteria recovered were affiliated with more than 19 families mainly in phyla Proteobacteria and Bacteroidetes, suggesting a high bacterial diversity. Moreover, 12 strains with high 1,3-xylanase-secreting ability from genera Vibrio, Neiella, Alteromonas, and Gilvimarinus were isolated from the enrichment culture. The extracellular 1,3-xylanases secreted by Vibrio sp. EA2, Neiella sp. GA3, Alteromonas sp. CA13-2, and Gilvimarinus sp. HA3-2, which were taken as representatives due to their efficient utilization of 1,3-xylan for growth, were further characterized. The extracellular 1,3-xylanases secreted by these strains showed the highest activity at pH 6.0–7.0 and 30–40°C in 0–0.5M NaCl, exhibiting thermo-unstable and alkali-resistant characters. Their degradation products on 1,3-xylan were mainly 1,3-xylobiose and 1,3-xylotriose. This study reveals the diversity of marine bacteria involved in the degradation and utilization of 1,3-xylan, helpful in our understanding of the recycling of 1,3-xylan driven by bacteria in the ocean and the discovery of novel 1,3-xylanases.

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“…Liu et al (2018) demonstrated that many Alphaproteobacteria (mainly Roseobacters) and Actinobacteria can degrade DMSP. In addition, Li et al (2021) found DddX, a novel DMSP lyase, present in Firmicutes (i.e., Sporosarcina sp. P33) besides Gammaproteobacteria and Alphaproteobacteria.…”

Section: Dmsp Degradation By Dcbmentioning

confidence: 99%

Distribution and Dimethylsulfoniopropionate Degradation of Dimethylsulfoniopropionate‐Consuming Bacteria in the Yellow Sea and East China Sea

Zhang

Tian

et al. 2021

JGR Oceans

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A novel ATP dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-CoA

Cited by 46 publications

References 65 publications

Recent insights into oceanic dimethylsulfoniopropionate biosynthesis and catabolism

Recent insights into oceanic dimethylsulfoniopropionate biosynthesis and catabolism

Diversity of Marine 1,3-Xylan-Utilizing Bacteria and Characters of Their Extracellular 1,3-Xylanases

Distribution and Dimethylsulfoniopropionate Degradation of Dimethylsulfoniopropionate‐Consuming Bacteria in the Yellow Sea and East China Sea

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