PMID- 29089943
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20200930
IS  - 1664-302X (Print)
IS  - 1664-302X (Electronic)
IS  - 1664-302X (Linking)
VI  - 8
DP  - 2017
TI  - Molecular Insight into the Acryloyl-CoA Hydration by AcuH for Acrylate 
      Detoxification in Dimethylsulfoniopropionate-Catabolizing Bacteria.
PG  - 2034
LID - 10.3389/fmicb.2017.02034 [doi]
LID - 2034
AB  - Microbial cleavage of dimethylsulfoniopropionate (DMSP) producing dimethyl 
      sulfide (DMS) and acrylate is an important step in global sulfur cycling. 
      Acrylate is toxic for cells, and thus should be metabolized effectively for 
      detoxification. There are two proposed pathways for acrylate metabolism in 
      DMSP-catabolizing bacteria, the AcuN-AcuK pathway and the PrpE-AcuI pathway. AcuH 
      is an acryloyl-CoA hydratase in DMSP-catabolizing bacteria and can catalyze the 
      hydration of toxic acryloyl-CoA to produce 3-hydroxypropionyl-CoA (3-HP-CoA) in 
      both the AcuN-AcuK pathway and the side path of the PrpE-AcuI pathway. However, 
      the structure and catalytic mechanism of AcuH remain unknown. Here, we cloned a 
      putative acuH gene from Roseovarius nubinhibens ISM, a typical DMSP-catabolizing 
      bacterium, and expressed it (RdAcuH) in Escherichia coli. The activity of RdAcuH 
      toward acryloyl-CoA was detected by liquid chromatography-mass spectrometry 
      (LC-MS), which suggests that RdAcuH is a functional acryloyl-CoA hydratase. Then 
      we solved the crystal structure of RdAcuH. Each asymmetric unit in the crystal of 
      RdAcuH contains a dimer of trimers and each RdAcuH monomer contains an N-terminal 
      domain (NTD) and a C-terminal domain (CTD). There are three active centers in 
      each trimer and each active center is located between the NTD of a subunit and 
      the CTD of the neighboring subunit. Site-directed mutagenesis analysis indicates 
      that two highly conserved glutamates, Glu112 and Glu132, in the active center are 
      essential for catalysis. Based on our results and previous research, we analyzed 
      the catalytic mechanism of AcuH to hydrate acryloyl-CoA, in which Glu132 acts as 
      the catalytic base. This study sheds light on the mechanism of acrylate 
      detoxification in DMSP-catabolizing bacteria.
FAU - Cao, Hai-Yan
AU  - Cao HY
AD  - State Key Laboratory of Microbial Technology, Marine Biotechnology Research 
      Center, Institute of Marine Science and Technology, Shandong University, Jinan, 
      China.
FAU - Wang, Peng
AU  - Wang P
AD  - State Key Laboratory of Microbial Technology, Marine Biotechnology Research 
      Center, Institute of Marine Science and Technology, Shandong University, Jinan, 
      China.
FAU - Xu, Fei
AU  - Xu F
AD  - State Key Laboratory of Microbial Technology, Marine Biotechnology Research 
      Center, Institute of Marine Science and Technology, Shandong University, Jinan, 
      China.
FAU - Li, Ping-Yi
AU  - Li PY
AD  - State Key Laboratory of Microbial Technology, Marine Biotechnology Research 
      Center, Institute of Marine Science and Technology, Shandong University, Jinan, 
      China.
FAU - Xie, Bin-Bin
AU  - Xie BB
AD  - State Key Laboratory of Microbial Technology, Marine Biotechnology Research 
      Center, Institute of Marine Science and Technology, Shandong University, Jinan, 
      China.
FAU - Qin, Qi-Long
AU  - Qin QL
AD  - State Key Laboratory of Microbial Technology, Marine Biotechnology Research 
      Center, Institute of Marine Science and Technology, Shandong University, Jinan, 
      China.
FAU - Zhang, Yu-Zhong
AU  - Zhang YZ
AD  - State Key Laboratory of Microbial Technology, Marine Biotechnology Research 
      Center, Institute of Marine Science and Technology, Shandong University, Jinan, 
      China.
AD  - Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for 
      Marine Science and Technology, Qingdao, China.
FAU - Li, Chun-Yang
AU  - Li CY
AD  - State Key Laboratory of Microbial Technology, Marine Biotechnology Research 
      Center, Institute of Marine Science and Technology, Shandong University, Jinan, 
      China.
FAU - Chen, Xiu-Lan
AU  - Chen XL
AD  - State Key Laboratory of Microbial Technology, Marine Biotechnology Research 
      Center, Institute of Marine Science and Technology, Shandong University, Jinan, 
      China.
LA  - eng
PT  - Journal Article
DEP - 20171017
PL  - Switzerland
TA  - Front Microbiol
JT  - Frontiers in microbiology
JID - 101548977
PMC - PMC5651017
OTO - NOTNLM
OT  - DMSP
OT  - acrylate
OT  - acryloyl-CoA hydratase
OT  - catalytic mechanism
OT  - detoxification
EDAT- 2017/11/02 06:00
MHDA- 2017/11/02 06:01
PMCR- 2017/10/17
CRDT- 2017/11/02 06:00
PHST- 2017/07/20 00:00 [received]
PHST- 2017/10/05 00:00 [accepted]
PHST- 2017/11/02 06:00 [entrez]
PHST- 2017/11/02 06:00 [pubmed]
PHST- 2017/11/02 06:01 [medline]
PHST- 2017/10/17 00:00 [pmc-release]
AID - 10.3389/fmicb.2017.02034 [doi]
PST - epublish
SO  - Front Microbiol. 2017 Oct 17;8:2034. doi: 10.3389/fmicb.2017.02034. eCollection 
      2017.