TY - JOUR
T1 - Decaprenyl pyrophosphate synthetase from Paracoccus denitrificans
AU - Ishii, Koichi
AU - Sagami, Hiroshi
AU - Ogura, Kyozo
N1 - Funding Information:
This work was supportedb y Grant-in-Aid for Scientific Research( 58470133f)r om the Ministry of Education,S ciencea nd Culture of Japan.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1985/7/9
Y1 - 1985/7/9
N2 - Decaprenyl pyrophosphate synthetase was partially purified from extracts of Paracoccus denitrificans. The enzyme catalyzed the synthesis of all-E-decaprenyl pyrophosphate from isopentenyl pyrophosphate and geranyl pyrophosphate, but it did not catalyze a reaction between isopentenyl pyrophosphate and dimethylallyl pyrophosphate. The Michaelis constants for geranyl, E,E-farnesyl pyrophosphate, and al-E-geranyl-geranyl pyrophosphate were 5.0 0.06, and 2.9 μM, respectively. The enzyme required detergent and Mg2+ for its catalytic activity and it was activated by monovalent cations such as K+ and NH4+.
AB - Decaprenyl pyrophosphate synthetase was partially purified from extracts of Paracoccus denitrificans. The enzyme catalyzed the synthesis of all-E-decaprenyl pyrophosphate from isopentenyl pyrophosphate and geranyl pyrophosphate, but it did not catalyze a reaction between isopentenyl pyrophosphate and dimethylallyl pyrophosphate. The Michaelis constants for geranyl, E,E-farnesyl pyrophosphate, and al-E-geranyl-geranyl pyrophosphate were 5.0 0.06, and 2.9 μM, respectively. The enzyme required detergent and Mg2+ for its catalytic activity and it was activated by monovalent cations such as K+ and NH4+.
KW - (P. denitrificans)
KW - Decaprenyl pyrophosphate synthetase
KW - Prenyltransferase
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U2 - 10.1016/0005-2760(85)90284-X
DO - 10.1016/0005-2760(85)90284-X
M3 - Article
AN - SCOPUS:0021844611
VL - 835
SP - 291
EP - 297
JO - BBA - Specialised Section On Lipids and Related Subjects
JF - BBA - Specialised Section On Lipids and Related Subjects
SN - 1388-1981
IS - 2
ER -