title: Purification and properties of a glucuronan lyase from Sinorhizobium meliloti M5N1CS (NCIMB 40472).
abstract: A glucuronan lyase extracted from Sinorhizobium meliloti strain M5N1CS was purified to homogeneity by anion-exchange chromatography. The purified enzyme corresponds to a monomer with a molecular mass of 20 kDa and a pI of 4.9. A specific activity was found only for polyglucuronates leading to the production of 4,5-unsaturated oligoglucuronates. The enzyme activity was optimal at pH 6.5 and 50 degrees C. Zn(2+), Cu(2+), and Hg(2+) (1 mM) inhibited the enzyme activity. No homology of the enzyme N-terminal amino acid sequence was found with any of the previously published protein sequences. This enzyme purified from S. meliloti strain M5N1CS corresponding to a new lyase was classified as an endopolyglucuronate lyase.
authors.affiliation: Laboratoire des Polysaccharides Microbiens et Végétaux, IUT, Département de Génie Biologique, Université de Picardie Jules Verne, Avenue des Facultés, Le Bailly, 80025 Amiens Cedex, France.
authors.forename: A
authors.initials: A
authors.lastname: Da Costa
authors.forename: P
authors.initials: P
authors.lastname: Michaud
authors.forename: E
authors.initials: E
authors.lastname: Petit
authors.forename: A
authors.initials: A
authors.lastname: Heyraud
authors.forename: P
authors.initials: P
authors.lastname: Colin-Morel
authors.forename: B
authors.initials: B
authors.lastname: Courtois
authors.forename: J
authors.initials: J
authors.lastname: Courtois
mesh_terms: D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D011133:Polysaccharide-Lyases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D016962:Sinorhizobium meliloti / Q000201:enzymology* / Q000254:growth & development; D013379:Substrate Specificity
chemical_list: D011133:Polysaccharide-Lyases; C109209:glucuronan lyase