Action of poly (alpha-L-guluronate) lyase from Corynebacterium sp. ALY-1 strain on saturated oligoguluronates

• Published in: Bioscience, biotechnology, and biochemistry Vol. 62; no. 6; pp. 1055 - 1060
• Main Authors: Matsubara, Y. (Kagawa-ken. Fermentation and Food Experimental Station, Uchinomi (Japan)), Iwasaki, K, Muramatsu, T
• Format: Journal Article
• Language: English
• Published: Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.01.1998; Japan Society for Bioscience Biotechnology and Agrochemistry
• Subjects: active site; ACTIVIDAD ENZIMATICA; ACTIVITE ENZYMATIQUE; Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Bacteriology; Base Sequence; Biological and medical sciences; Chromatography, High Pressure Liquid; Cloning, Molecular; CORYNEBACTERIUM; Corynebacterium - enzymology; Corynebacterium - genetics; Corynebacterium sp; DEGRADACION; DEGRADATION; Enzymes and enzyme inhibitors; ENZYMIC ACTIVITY; Fundamental and applied biological sciences. Psychology; Genes, Bacterial; Hexuronic Acids - pharmacology; HIDROLASAS; HPLC; HYDROLASE; HYDROLASES; Kinetics; Lyases; Mannose - analogs & derivatives; Mannose - pharmacology; Metabolism. Enzymes; Microbiology; Molecular Sequence Data; Oligosaccharides - pharmacology; POLISACARIDOS; poly(α-L-guluronate)lyase; POLYHOLOSIDE; Polysaccharide-Lyases - metabolism; POLYSACCHARIDES; Protein Conformation; Species Specificity; subsite; Uronic Acids - pharmacology; Subsite; Polysaccharide-lyases; Enzyme; Active site; Lyases; Alginates; Oligomer; Poly(α-L-guluronate) lyase; Corynebacterium; Enzymatic activity; Uronic acid; Enzymatic digestion; Reaction mechanism; Bacteria; Actinomycetes; Corynebacteriaceae; Kinetics; Carbon-oxygen lyases
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.62.1055

A kinetic analysis of degradation of saturated oligoguluronates by poly(alpha-L-guluronate)lyase from Corynebacterium sp. ALY-1 strain was done. The saturated oligoguluronates were prepared by hydrolyzing poly alpha1,4-L-guluronate from alginate with HCl, and then by gel filtration of a Bio Gel P-6 column. The saturated pentaguluronate or above were rapidly degraded by the enzyme, while tetraguluronate was slowly degraded. From the dependency of the catalytic rate constant (k-cat) on the degree of polymerization of substrates, the enzyme was found to have a subsite size corresponding to hexaguluronate units. The action pattern of the enzyme on hexaguluronate suggested that the catalytic site of the enzyme was matched to the linkage between the second and third uronic residue from the non-reducing end, since the substrate was mainly split into a unsaturated tetramer and a saturated dimer from a HPLC analysis