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A cis ‐prenyltransferase from Methanosarcina acetivorans catalyzes both head‐to‐tail and nonhead‐to‐tail prenyl condensation
Author(s) -
Ogawa Takuya,
Emi Kohichi,
Koga Kazushi,
Yoshimura Tohru,
Hemmi Hisashi
Publication year - 2016
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.13749
Subject(s) - prenylation , prenyltransferase , methanosarcina , allylic rearrangement , chemistry , stereochemistry , glycosyl , enzyme , condensation reaction , catalysis , biochemistry , archaea , gene
Cis ‐prenyltransferase usually consecutively catalyzes the head‐to‐tail condensation reactions of isopentenyl diphosphate to allylic prenyl diphosphate in the production of ( E,Z ‐mixed) polyprenyl diphosphate, which is the precursor of glycosyl carrier lipids. Some recently discovered homologs of the enzyme, however, catalyze the nonhead‐to‐tail condensation reactions between allylic prenyl diphosphates. In this study, we characterize a cis ‐prenyltransferase homolog from a methanogenic archaeon, Methanosarcina acetivorans , to obtain information on the biosynthesis of the glycosyl carrier lipids within it. This enzyme catalyzes both head‐to‐tail and nonhead‐to‐tail condensation reactions. The kinetic analysis shows that the main reaction of the enzyme is consecutive head‐to‐tail prenyl condensation reactions yielding polyprenyl diphosphates, while the chain lengths of the major products seem shorter than expected for the precursor of glycosyl carrier lipids. On the other hand, a subsidiary reaction of the enzyme, i.e., nonhead‐to‐tail condensation between dimethylallyl diphosphate and farnesyl diphosphate, gives a novel diterpenoid compound, geranyllavandulyl diphosphate.