S Smith

Summary

Publications

  1. ncbi Expression in Escherichia coli and refolding of the malonyl-/acetyltransferase domain of the multifunctional animal fatty acid synthase
    V S Rangan
    Children s Hospital Oakland Research Institute, Oakland, California 94609, USA
    J Biol Chem 271:31749-55. 1996
  2. ncbi Mapping the functional topology of the animal fatty acid synthase by mutant complementation in vitro
    V S Rangan
    Children's Hospital Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland, California 94609, USA
    Biochemistry 40:10792-9. 2001
  3. ncbi Mapping of functional interactions between domains of the animal fatty acid synthase by mutant complementation in vitro
    A K Joshi
    Children s Hospital Oakland Research Institute, California 94609, USA
    Biochemistry 36:2316-22. 1997
  4. ncbi Dibromopropanone cross-linking of the phosphopantetheine and active-site cysteine thiols of the animal fatty acid synthase can occur both inter- and intrasubunit. Reevaluation of the side-by-side, antiparallel subunit model
    A Witkowski
    Children s Hospital Oakland Research Institute, Oakland, California 94609, USA
    J Biol Chem 274:11557-63. 1999
  5. ncbi Molecular cloning and sequencing of a cDNA encoding the thioesterase domain of the rat fatty acid synthetase
    J Naggert
    Children s Hospital Oakland Research Institute, California 94609
    J Biol Chem 263:1146-50. 1988
  6. ncbi Cloning, sequencing, and characterization of Escherichia coli thioesterase II
    J Naggert
    Children s Hospital Oakland Research Institute, California 94609
    J Biol Chem 266:11044-50. 1991

Collaborators

  • J E Cronan
  • V S Rangan
  • A K Joshi
  • A Witkowski
  • A M Falick
  • H E Witkowska
  • J Naggert
  • H Cho
  • J Mikkelsen
  • L DeVeaux
  • Z I Randhawa
  • M L Narasimhan
  • B N Green

Detail Information

Publications6

  1. ncbi Expression in Escherichia coli and refolding of the malonyl-/acetyltransferase domain of the multifunctional animal fatty acid synthase
    V S Rangan
    Children s Hospital Oakland Research Institute, Oakland, California 94609, USA
    J Biol Chem 271:31749-55. 1996
    ..These results indicate that His-683 plays an essential role in catalysis, likely by accepting a proton from the active site serine, thus increasing its nucleophilicity...
  2. ncbi Mapping the functional topology of the animal fatty acid synthase by mutant complementation in vitro
    V S Rangan
    Children's Hospital Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland, California 94609, USA
    Biochemistry 40:10792-9. 2001
    ..These results are discussed in the context of a revised model for the fatty acid synthase...
  3. ncbi Mapping of functional interactions between domains of the animal fatty acid synthase by mutant complementation in vitro
    A K Joshi
    Children s Hospital Oakland Research Institute, California 94609, USA
    Biochemistry 36:2316-22. 1997
    ....
  4. ncbi Dibromopropanone cross-linking of the phosphopantetheine and active-site cysteine thiols of the animal fatty acid synthase can occur both inter- and intrasubunit. Reevaluation of the side-by-side, antiparallel subunit model
    A Witkowski
    Children s Hospital Oakland Research Institute, Oakland, California 94609, USA
    J Biol Chem 274:11557-63. 1999
    ..These results show that the two polypeptides of the fatty acid synthase are oriented such that head-to-tail contacts are formed both between and within subunits, and provide the first structural evidence in support of the new model...
  5. ncbi Molecular cloning and sequencing of a cDNA encoding the thioesterase domain of the rat fatty acid synthetase
    J Naggert
    Children s Hospital Oakland Research Institute, California 94609
    J Biol Chem 263:1146-50. 1988
    ....
  6. ncbi Cloning, sequencing, and characterization of Escherichia coli thioesterase II
    J Naggert
    Children s Hospital Oakland Research Institute, California 94609
    J Biol Chem 266:11044-50. 1991
    ..coli. Over-expression of the recombinant enzyme, under control of the lac promoter, did not alter the fatty acids synthesized by E. coli at any stage of cell growth and the physiological role of this enzyme remains an enigma...