Journal de biochimie et de biologie cellulaire

Abstrait

Structure and Function of alpha 1,3-Glucanase from Streptomyces thermodiastaticus HF3-3

1,3-glucan (mutan) is a water-insoluble, direct -1,3-connected homopolymer of glucose, which is the principle part of extracellular polysaccharide, was integrated from sucrose by Streptococcus mutans by means of glycosyltransferases (GTFs) that are reason for dental plague in human. It has likewise been found in parasites as a segment of cell divider, carbon source and destructive factor of pathogenic growths. Considering from this foundation, we have keen on examining -1,3-glucanase (mutanase) that can hydrolyze -1,3-glycosidic obligation of -1,3-glucan. In the past investigation was resolved the amino corrosive succession of GH 87 -1,3-glucanase from Streptomyces thermodiastaticus HF3-3 (Agl-ST2) which was classified as another gathering of -1,3-glucanase, multi-areas compound including N-terminal restricting space, starch restricting module family 35 (CBM35), C-terminal synergist area and discoidin area (DS), individually. The correlation  of Agl-ST2 with the related proteins uncovered high closeness to mycodextranase (85%), while had low homology with the known -1,3-glucanase. In any case, the properties demonstrated that Agl-ST2 has a place with -1,3-glucanase. Since Agl-ST1 is created from Agl-ST2 by truncation of DS district, Agl-ST1 has the equivalent multi-area as Agl-ST2 however without DS. In this examination to comprehend area structure and capacity of Agl-ST 1&2), we decided every space structure and capacity of the Agl-STs in the -1,3-glucan authoritative and hydrolysis by developing a few area cancellations and site-coordinated transformation in synergist area. The outcomes indicated that Agl-ST with site-coordinated change at the basic amino deposits had little exercises of hydrolysis -1,3-glucan, while the catalysts lacking synergist space lower restricting exercises than the wild sort.