Article
Structural and molecular basis for the novel catalytic mechanism and evolution of DddP, an abundant peptidase-like bacterial Dimethylsulfoniopropionate lyase: a new enzyme from an old fold.
Molecular microbiology - 1 Oct 2015
Wang Peng, Chen Xiu-Lan, Li Chun-Yang, Gao Xiang, Zhu De-yu, Xie Bin-Bin, Qin Qi-Long, Zhang Xi-Ying, Su Hai-Nan, Zhou Bai-Cheng, Xun Lu-ying, Zhang Yu-Zhong
Abstract excerpt
The microbial cleavage of dimethylsulfoniopropionate (DMSP) generates volatile dimethyl sulfide (DMS) and is an important step in global sulfur and carbon cycles. DddP is a DMSP lyase in marine bacteria, and the deduced dddP gene product is abundant in marine metagenomic data sets. However, DddP belongs to the M24 peptidase family according to sequence alignment. Peptidases hydrolyze C-N bonds, but DddP is...
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