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Enzymes and Their Reaction Mechanisms in Dimethylsulfoniopropionate Cleavage and Biosynthesis of Dimethylsulfide by Marine Bacteria

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Title
Enzymes and Their Reaction Mechanisms in Dimethylsulfoniopropionate Cleavage and Biosynthesis of Dimethylsulfide by Marine Bacteria
Other Titles
Dimethylsulfoniopropionate (DMSP) 물질의 분해와 Dimethylsulfide (DMS) 의 합성에 관여하는 해양 미생물이가지는 효소들의 기작에 대한 리뷰논문
Authors
Do, Hackwon
Hwang, Jisub
Lee, Sung Gu
Lee, Jun Hyuck
Keywords
DimethylsulfideDimethylsulfoniopropionateMolecular modelingMethylmalonate semialdehyde dehydrogenaseSulfur recycle
Issue Date
2021-06
Citation
Do, Hackwon, et al. 2021. "Enzymes and Their Reaction Mechanisms in Dimethylsulfoniopropionate Cleavage and Biosynthesis of Dimethylsulfide by Marine Bacteria". 한국해양생명과학회지, 6(1): 1-8.
Abstract
In marine ecosystems, the biosynthesis and catabolism of dimethylsulfoniopropionate (DMSP) by marine bacteria is critical to microbial survival and the ocean food chain. Furthermore, these processes also influence sulfur recycling and climate change. Recent studies using emerging genome sequencing data and extensive bioinformatics analysis have enabled us to identify new DMSP-related genes. Currently, seven bacterial DMSP lyases (DddD, DddP, DddY, DddK, DddL, DddQ and DddW), two acrylate degrading enzymes (DddA and DddC), and four demethylases (DmdA, DmdB, DmdC, and DmdD) have been identified and characterized in diverse marine bacteria. In this review, we focus on the biochemical properties of DMSP cleavage enzymes with special attention to DddD, DddA, and DddC pathways. These three enzymes function in the production of acetyl coenzyme A (CoA) and CO2 from DMSP. DddD is a DMSP lyase that converts DMSP to 3-hydroxypropionate with the release of dimethylsulfide. 3-Hydroxypropionate is then converted to malonate semialdehyde by DddA, an alcohol dehydrogenase. Then, DddC transforms malonate semialdehyde to acetyl-CoA and CO2 gas. DddC is a putative methylmalonate semialdehyde dehydrogenase that requires nicotinamide adenine dinucleotide and CoA cofactors. Here we review recent insights into the structural characteristics of these enzymes and the molecular events of DMSP degradation.
URI
https://repository.kopri.re.kr/handle/201206/13041
Type
Article
Station
해당사항없음
Indexed
KCI등재후보
Appears in Collections  
2021-2021, Development of potential candidates as antibiotics based on polar genetic resources (21-21) / Lee, Jun Hyuck (PM21030)
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