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

I Yoshida; T Koyama; K Ogura

doi:10.1016/0006-291x(89)92453-4

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

Biochem Biophys Res Commun. 1989 Apr 28;160(2):448-52. doi: 10.1016/0006-291x(89)92453-4.

Authors

I Yoshida¹, T Koyama, K Ogura

Affiliation

¹ Chemical Research Institute of Non-Aqeous Solutions, Tohoku University, Sendai, Japan.

PMID: 2541701
DOI: 10.1016/0006-291x(89)92453-4

Abstract

Formation of a stable complex of the two essential components of hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26, which represents the catalytically active state of this enzyme, is observed in the presence of a relatively high concentrations of inorganic pyrophosphate or one of the substrates, isopentenyl diphosphate or farnesyl diphosphate. The apparent molecular mass of the complex is estimated to be about 50 kDa by gel filtration with Superose 12.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Alkyl and Aryl Transferases*
Catalysis
Chromatography, Gel
Dimethylallyltranstransferase / isolation & purification
Dimethylallyltranstransferase / metabolism*
Diphosphates
Enzyme Stability
Hemiterpenes*
Macromolecular Substances
Micrococcus / enzymology*
Organophosphorus Compounds
Polyisoprenyl Phosphates
Sesquiterpenes
Substrate Specificity
Transferases / metabolism*

Substances

Diphosphates
Hemiterpenes
Macromolecular Substances
Organophosphorus Compounds
Polyisoprenyl Phosphates
Sesquiterpenes
isopentenyl pyrophosphate
farnesyl pyrophosphate
Transferases
Alkyl and Aryl Transferases
Dimethylallyltranstransferase
trans-pentaprenyltranstransferase