CTC02563

Summary

Gene Symbol: CTC02563
Description: methylaspartate ammonia-lyase
Species: Clostridium tetani E88

Top Publications

  1. ncbi The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step
    Miryam Asuncion
    The Centre for Biomolecular Sciences, The University, St Andrews, Scotland, United Kingdom KY16 9ST
    J Biol Chem 277:8306-11. 2002
  2. ncbi Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymes
    E N Marsh
    Department of Biochemistry, University of Cambridge, UK
    FEBS Lett 310:167-70. 1992
  3. ncbi Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein
    S K Goda
    Division of Biotechnology, PHLS Centre for Applied Microbiology, Proton Down, Salisbury, Wiltshire, U K
    Biochemistry 31:10747-56. 1992
  4. ncbi Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum. Organization of the mut genes
    D E Holloway
    Department of Biochemistry, University of Cambridge, UK
    FEBS Lett 317:44-8. 1993
  5. ncbi Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum
    M Brecht
    Genzentrum der Universität München, Germany
    FEBS Lett 319:84-9. 1993
  6. ncbi Overexpression, purification, crystallization and data collection of 3-methylaspartase from Clostridium tetanomorphum
    M Asuncion
    The Centre for Biomolecular Sciences, The University, St Andrews KY16 9ST, Scotland, UK
    Acta Crystallogr D Biol Crystallogr 57:731-3. 2001

Detail Information

Publications6

  1. ncbi The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step
    Miryam Asuncion
    The Centre for Biomolecular Sciences, The University, St Andrews, Scotland, United Kingdom KY16 9ST
    J Biol Chem 277:8306-11. 2002
    ..This motif is the defining mechanistic characteristic of the enolase superfamily of which all have a common fold. The degree of structural conservation is remarkable given only four residues are absolutely conserved...
  2. ncbi Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymes
    E N Marsh
    Department of Biochemistry, University of Cambridge, UK
    FEBS Lett 310:167-70. 1992
    ..J. 260, 345-352] and a region of cobalamin-dependent methionine synthase which has been shown to bind cobalamin [1989, J. Biol. Chem 264, 13888-13895]...
  3. ncbi Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein
    S K Goda
    Division of Biotechnology, PHLS Centre for Applied Microbiology, Proton Down, Salisbury, Wiltshire, U K
    Biochemistry 31:10747-56. 1992
    ..The implications of these findings on the mechanism of catalysis are discussed within the context of a few emerging mode of action for methylaspartate ammonia-lyase...
  4. ncbi Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum. Organization of the mut genes
    D E Holloway
    Department of Biochemistry, University of Cambridge, UK
    FEBS Lett 317:44-8. 1993
    ..Local homology exists between mutE and a region of beta-methylaspartase which contains an active-site serine residue...
  5. ncbi Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum
    M Brecht
    Genzentrum der Universität München, Germany
    FEBS Lett 319:84-9. 1993
    ..It shows no homology to any other protein in the database, and while binding coenzyme B12, a conspicuous B12 binding motif, shared amongst other proteins, is not detectable at the sequence level...
  6. ncbi Overexpression, purification, crystallization and data collection of 3-methylaspartase from Clostridium tetanomorphum
    M Asuncion
    The Centre for Biomolecular Sciences, The University, St Andrews KY16 9ST, Scotland, UK
    Acta Crystallogr D Biol Crystallogr 57:731-3. 2001
    ..3, b = 109.9, c = 67.2 A, alpha = beta = gamma = 90 degrees. The asymmetric unit contains two monomers with 42% solvent. A self-rotation function indicates the presence of a twofold axis, consistent with a biological dimer...