No abstract

Polyprenyl groups, products of isoprenoid metabolism, are utilized in peptidoglycan biosynthesis, protein N -glycosylation, and other processes. These groups are formed by cis -prenyltransferases, which use allylic prenyl pyrophosphates as prenyl-donors to catalyze the C -prenylation of the general acceptor substrate, isopentenyl pyrophosphate. Repetition of this reaction forms ( Z,E -mixed)-polyprenyl pyrophosphates, which are converted later into glycosyl carrier lipids, such as undecaprenyl phosphate and dolichyl phosphate. MM_0014 from the methanogenic archaeon Methanosarcina mazei is known as a versatile cis -prenyltransferase that accepts both isopentenyl pyrophosphate and dimethylallyl pyrophosphate as acceptor substrates. To learn more about this enzyme’s catalytic activity, we determined the X-ray crystal structures of MM_0014 in the presence or absence of these substrates. Surprisingly, one structure revealed a complex with O -prenylglycerol, suggesting that the enzyme catalyzed the prenylation of glycerol contained in the crystallization buffer. Further analyses confirmed that the enzyme could catalyze the O -prenylation of small alcohols, such as 2-propanol, expanding our understanding of the catalytic ability of cis -prenyltransferases.