Formation of a stable and catalytically active complex of the two essential components of hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26.

  title={Formation of a stable and catalytically active complex of the two essential components of hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26.},
  author={I Yoshida and Takako Koyama and Kyozo Ogura},
  journal={Biochemical and biophysical research communications},
  volume={160 2},
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*
The crystal structure of Ml-HexPPs is determined both in the substrate-free form and in complex with 7,11-dimethyl-2,6,10-dodecatrien-1-yl diphosphate ammonium salt (3-DesMe-FPP), an analog of FPP.
Molecular Cloning, Expression, and Characterization of the Genes Encoding the Two Essential Protein Components of Micrococcus luteus B-P 26 Hexaprenyl Diphosphate Synthase
ABSTRACT The structural genes encoding the two essential components A and B of hexaprenyl diphosphate synthase, which produce the precursor of the prenyl side chain of menaquinone-6, were cloned from
Two cistrons of the gerC operon of Bacillus subtilis encode the two subunits of heptaprenyl diphosphate synthase
The two proteins (GerC1 and GerC3) encoded by the gerC locus of Bacillus subtilis were identified as dissociable heterodimers of the heptaprenyl diphosphate synthase involved in the biosynthesis of the side chain of menaquinone-7.
Polyprenyl diphosphate synthases.
It is noteworthy that in spite of the similarity of the reactions catalyzed by these prenyltransferases, the modes of expression of catalytic function are surprisingly different, varying according to
Isoprenyl diphosphate synthases.
1.14 – Prenyltransferase
Homodimeric Hexaprenyl Pyrophosphate Synthase from the Thermoacidophilic Crenarchaeon Sulfolobus solfataricus Displays Asymmetric Subunit Structures
Different side chain conformations of Trp136 in two HexPPs subunits result in weaker hydrophobic interactions at the dimer interface, in contrast to the symmetric pi-pi stacking interactions of aromatic side chains found in FPPs and OPPs.
Molecular Cloning and Nucleotide Sequences of the Genes for Two Essential Proteins Constituting a Novel Enzyme System for Heptaprenyl Diphosphate Synthesis (*)
The genes encoding two dissociable components essential for Bacillus stearothermophilus heptaprenyl diphosphate synthase were cloned and this enzyme was proved genetically to consist of two different protein components with molecular masses of 25 kDa and 36 kDa, encoded by two of the three tandem genes.


Dynamic interaction between components of hexaprenyl diphosphate synthase from Micrococcus luteus BP-26.
Evidence was obtained to show that farnesyl diphosphate (FPP) binds to the components to form an aggregate, A-B-FPP-Mg2+, which probably represents an intermediary state of enzyme catalysis.