caa a22 4500 397558430 CHVBK 20180308164809.0 cr unu---uuuuu 161202e199603 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021275 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021275 Identification and Characterization of Geranylgeraniol Kinase and Geranylgeranyl Phosphate Kinase from the Archaebacterium Sulfolobus acidocaldariu [Elektronische Daten] [Shin-ichi Ohnuma, Masatada Watanabe, Tokuzo Nishino] Geranylgeranyl diphosphate is an important precursor of archaebacterial ether-linked lipids, and it has been thought that all of this compound is "de novo” synthesized by geranylgeranyl diphosphate synthase. We studied the phosphorylation of geranylgeraniol, which seems to be related to the salvage pathway of biosynthesis of archaebacterial ether-linked lipids, in the Archaebacterium Sulfolobus acidocaldarius. Activities of geranylgeraniol kinase and geranylgeranyl phosphate kinase were detected in a cell lysate of S.acidocaldarius. The two enzymes were easily separated by ultracentrifugation. The membrane fraction and the cytosolic fraction contained geranylgeraniol kinase activity and geranylgeranyl phosphate kinase activity, respectively. Geranylgeraniol kinase, which requires divalent cation such as Mg2+, Co2+, and Mn2+ and NTP (ATP, GTP, CTP, UTP), catalyzes monophosphorylation of (all-E)-geranylgeraniol to produce geranylgeranyl phosphate. (all-E)-Farnesol, (all-E)-hexaprenol, and (all-E)-octaprenol were also active as substrates, though they were less effective than (all-E)-geranylgeraniol. However, neither geraniol nor (2E,6E,10Z,14Z,18Z,22Z,26Z,30Z,34Z,38Z)-undecaprenol was active. This enzyme is extremely thermostable and its pH optimal is between 6.5 and 8.5. The Michaelis constants for (all-E)-geranylgeraniol and ATP are 27 nM and 650μM, respectively. © by the Journal of Biochemistry Regular Papers nationallicence Archaebacterium nationallicence geranylgeraniol nationallicence isoprenoids nationallicence kinase nationallicence lipid nationallicence Ohnuma Shin-ichi Department of Biochemistry and Engineering, Tohoku University, Aoba Aramaki, Aoba-ku, Sendai 980-77 aut Watanabe Masatada Department of Biochemistry and Engineering, Tohoku University, Aoba Aramaki, Aoba-ku, Sendai 980-77 aut Nishino Tokuzo Department of Biochemistry and Engineering, Tohoku University, Aoba Aramaki, Aoba-ku, Sendai 980-77 aut The Journal of Biochemistry Oxford University Press 119/3(1996-03), 541-547 0021-924X 119:3<541 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021275 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021275 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Ohnuma Shin-ichi Department of Biochemistry and Engineering, Tohoku University, Aoba Aramaki, Aoba-ku, Sendai 980-77 aut NATIONALLICENCE 700 1- Watanabe Masatada Department of Biochemistry and Engineering, Tohoku University, Aoba Aramaki, Aoba-ku, Sendai 980-77 aut NATIONALLICENCE 700 1- Nishino Tokuzo Department of Biochemistry and Engineering, Tohoku University, Aoba Aramaki, Aoba-ku, Sendai 980-77 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/3(1996-03), 541-547 0021-924X 119:3<541 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford