Biochemical and Biophysical Research Communications
Volume 160, Issue 2, 28 April 1989, Pages 448-452
Formation of a stable and catalytically active complex of the two essential components of hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26
References (5)
- et al.
J. Biol. Chem.
(1982) - et al.
FEBS Lett.
(1983)
There are more references available in the full text version of this article.
Cited by (16)
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, Journal of Biological ChemistryCitation Excerpt :In contrast, the function of heterooligomeric enzymes is not well understood. Only limited numbers of the enzymes in this class are known as heterodimeric or heterotetrameric enzymes (Fig. 1B) (44–57). The heterooligomeric enzymes are composed of two different components, large and small subunits, and are shown to be unable to catalyze the chain elongation reaction without either of the two components (49, 51, 52, 54–56, 58).
Artificial substrates of medium-chain elongating enzymes, hexaprenyl- and heptaprenyl diphosphate synthases
2001, Bioorganic and Medicinal Chemistry LettersIsoprenyl diphosphate synthases
2000, Biochimica et Biophysica Acta - Molecular and Cell Biology of LipidsSpringer handbook of enzymes: Second edition
2013, Springer Handbook of Enzymes: Second EditionPrenyltransferase
2010, Comprehensive Natural Products II: Chemistry and Biology
Copyright © 1989 Published by Elsevier Inc.