Research Topics
Genomes and GenesSpecies | CTC02563SummaryGene Symbol: CTC02563 Description: methylaspartate ammonia-lyase Species: Clostridium tetani E88 Top Publications
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Detail Information
Publications
Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymesE 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]...
Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant proteinS 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...
Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum. Organization of the mut genesD 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...
Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphumM 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...
Overexpression, purification, crystallization and data collection of 3-methylaspartase from Clostridium tetanomorphumM 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...
The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical stepMiryam 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...
