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Identification and characterization of geranylgeraniol kinase and geranylgeranyl phosphate kinase from the Archaebacterium Sulfolobus acidocaldarius.
Ohnuma S, Watanabe M, Nishino T. Ohnuma S, et al. J Biochem. 1996 Mar;119(3):541-7. doi: 10.1093/oxfordjournals.jbchem.a021275. J Biochem. 1996. PMID: 8830051
Activities of geranylgeraniol kinase and geranylgeranyl phosphate kinase were detected in a cell lysate of S. acidocaldarius. ...
Activities of geranylgeraniol kinase and geranylgeranyl phosphate kinase were detected in a cell lysate of S. acidocaldarius. ...
Overexpression of an archaeal geranylgeranyl diphosphate synthase in Escherichia coli cells.
Ohto C, Nakane H, Hemmi H, Ohnuma S, Obata S, Nishino T. Ohto C, et al. Among authors: ohnuma s. Biosci Biotechnol Biochem. 1998 Jun;62(6):1243-6. doi: 10.1271/bbb.62.1243. Biosci Biotechnol Biochem. 1998. PMID: 9692210
We purified 24.3 mg of MBP (maltose-binding protein)-fusion protein and 5.4 mg of GST (glutathione S-transferase)-fusion protein from a one-liter culture of E. coli. ...
We purified 24.3 mg of MBP (maltose-binding protein)-fusion protein and 5.4 mg of GST (glutathione S-transferase)-fusion protein from …
Effects of random mutagenesis in a putative substrate-binding domain of geranylgeranyl diphosphate synthase upon intermediate formation and substrate specificity.
Ohnuma S, Hemmi H, Ohto C, Nakane H, Nishino T. Ohnuma S, et al. J Biochem. 1997 Apr;121(4):696-704. doi: 10.1093/oxfordjournals.jbchem.a021642. J Biochem. 1997. PMID: 9163520
Recognition of allylic substrates in Sulfolobus acidocaldarius geranylgeranyl diphosphate synthase: analysis using mutated enzymes and artificial allylic substrates.
Ohnuma S, Hemmi H, Koyama T, Ogura K, Nishino T. Ohnuma S, et al. J Biochem. 1998 Jun;123(6):1036-40. doi: 10.1093/oxfordjournals.jbchem.a022040. J Biochem. 1998. PMID: 9603990
Identification of genes affecting lycopene formation in Escherichia coli transformed with carotenoid biosynthetic genes: candidates for early genes in isoprenoid biosynthesis.
Hemmi H, Ohnuma S, Nagaoka K, Nishino T. Hemmi H, et al. Among authors: ohnuma s. J Biochem. 1998 Jun;123(6):1088-96. doi: 10.1093/oxfordjournals.jbchem.a022047. J Biochem. 1998. PMID: 9603997
Mechanism of product chain length determination for heptaprenyl diphosphate synthase from Bacillus stearothermophilus.
Hirooka K, Ohnuma S, Koike-Takeshita A, Koyama T, Nishino T. Hirooka K, et al. Among authors: ohnuma s. Eur J Biochem. 2000 Jul;267(14):4520-8. doi: 10.1046/j.1432-1327.2000.01502.x. Eur J Biochem. 2000. PMID: 10880976
Protein design of geranyl diphosphate synthase. Structural features that define the product specificities of prenyltransferases.
Narita K, Ohnuma S, Nishino T. Narita K, et al. Among authors: ohnuma s. J Biochem. 1999 Sep;126(3):566-71. doi: 10.1093/oxfordjournals.jbchem.a022487. J Biochem. 1999. PMID: 10467173
Conversion of product specificity of archaebacterial geranylgeranyl-diphosphate synthase. Identification of essential amino acid residues for chain length determination of prenyltransferase reaction.
Ohnuma S, Hirooka K, Hemmi H, Ishida C, Ohto C, Nishino T. Ohnuma S, et al. J Biol Chem. 1996 Aug 2;271(31):18831-7. doi: 10.1074/jbc.271.31.18831. J Biol Chem. 1996. PMID: 8702542
Amino acid alignment of known prenyltransferases around this position and our previous observations on farnesyl-diphosphate synthase (Ohnuma, S....
Amino acid alignment of known prenyltransferases around this position and our previous observations on farnesyl-diphosphate synthase (Ohn
Conversion from farnesyl diphosphate synthase to geranylgeranyl diphosphate synthase by random chemical mutagenesis.
Ohnuma S, Nakazawa T, Hemmi H, Hallberg AM, Koyama T, Ogura K, Nishino T. Ohnuma S, et al. J Biol Chem. 1996 Apr 26;271(17):10087-95. doi: 10.1074/jbc.271.17.10087. J Biol Chem. 1996. PMID: 8626566
From the libraries, the mutants that showed the activity of geranylgeranyl diphosphate (GGPP) synthase were selected by the red-white screening method (Ohnuma, S....
From the libraries, the mutants that showed the activity of geranylgeranyl diphosphate (GGPP) synthase were selected by the red-white screen …
Alteration of the product specificities of prenyltransferases by metal ions.
Ohnuma S, Koyama T, Ogura K. Ohnuma S, et al. Biochem Biophys Res Commun. 1993 Apr 30;192(2):407-12. doi: 10.1006/bbrc.1993.1430. Biochem Biophys Res Commun. 1993. PMID: 8484753
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