the enzyme contains glucose and/or mannose. The carbohydrate moiety appears to be a key determinant of the enzymes sucrose hydrolysis activity, substrate affinity, and thermal stability
deglycosylation by PMGase F, the glycosylation of isozyme lbbetafruct2 differs in the different plant tissues and between native and recombinant enzyme, overview
deglycosylation by PMGase F, the glycosylation of isozyme lbbetafruct3 differs in the different plant tissues and between native and recombinant enzyme, overview
glycoprotein with a protein to carbohydrate ratio of 3.2. Presence of mannose and glucose as the major components along with smaller amounts of galactose
the extracellular enzyme contains 18 N-acetylglucosamine residues in addition to mannose. The intracellular enzyme does not contain mannose and N-acetylglucosamine
carbohydrate moiety does not affect the mechanism of folding and association of invertase. However glycosylation improves the solubility of unfolded or partially folded invertase molecules and hence leads to a suppression of irreversible aggregation
isoforms EINV1, EINV2, EINV3, EINV4 share identical protein parts but differ in glycosylation, thermal stability and surface charge density due to variation in the amount of phosphate groups bound to the polymannan components
contains 67% of carbohydrate, equimolar amounts of mannose and galactose, a small amounts of glucosamine is probably involved in the linkage to the protein moiety
after deglycosylation of the enzymes, denoted D-INVAAOX1and D-INVBAOX1, they exhibit a 1.3- and 3-fold lower catalytic efficiency (107 and 164 s-1*mM-1, respectively), and a 1.3- to 5-fold lower thermal stability than the glycosylated forms at temperatures of 35-45°C. After deglycosylation no effect is observed in optimal pH, being of 5.5 for INVAAOX1, INVBAOX1, D-INVAAOX1 and D-INVBAOX1
after deglycosylation of the enzymes, denoted D-INVAAOX1and D-INVBAOX1, they exhibit a 1.3- and 3-fold lower catalytic efficiency (107 and 164 s-1*mM-1, respectively), and a 1.3- to 5-fold lower thermal stability than the glycosylated forms at temperatures of 35-45°C. After deglycosylation no effect is observed in optimal pH, being of 5.5 for INVAAOX1, INVBAOX1, D-INVAAOX1 and D-INVBAOX1
isoforms EINV1, EINV2, EINV3, EINV4 share identical protein parts but differ in glycosylation, thermal stability and surface charge density due to variation in the amount of phosphate groups bound to the polymannan components
invertase SUC2 is ubiquitinated at three lysine residue sites (K185, K312 and K430), ubiquitination of SUC2 in the site of 185 contributes to the high enzyme activity. Deubiquitination of K185 slightly affects the thermal stability of SUC2
invertase SUC2 is ubiquitinated at three lysine residue sites (K185, K312 and K430), ubiquitination of SUC2 in the site of 185 contributes to the high enzyme activity. Deubiquitination of K185 slightly affects the thermal stability of SUC2