TitleDatePubMed ID
Crystal structure of heterodimeric hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26 reveals that the small subunit is directly involved in the product chain length regulation.2011 Feb 421068379
Substrate specificities of several prenyl chain elongating enzymes with respect to 4-methyl-4-pentenyl diphosphate.2004 Oct15502351
Artificial substrates of medium-chain elongating enzymes, hexaprenyl- and heptaprenyl diphosphate synthases.2001 Aug 2011514159
Chain length determination of prenyltransferases: both heteromeric subunits of medium-chain (E)-prenyl diphosphate synthase are involved in the product chain length determination.2000 Oct 1711027152
Molecular cloning, expression, and characterization of the genes encoding the two essential protein components of Micrococcus luteus B-P 26 hexaprenyl diphosphate synthase.1998 Mar9515931
Formation of a stable and catalytically active complex of the two essential components of hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26.1989 Apr 282541701
Protection of hexaprenyl-diphosphate synthase of Micrococcus luteus B-P 26 against inactivation by sulphydryl reagents and arginine-specific reagents.1989 Apr 62539196
Dynamic interaction between components of hexaprenyl diphosphate synthase from Micrococcus luteus BP-26.1987 Oct 202827736
Hexaprenyl pyrophosphate synthetase from Micrococcus luteus B-P 26. Separation of two essential components.1982 Dec 257174655