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side-chain modification
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the enzyme is phosphorylated
glycoprotein
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glycoprotein
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contains 6.6% sugars, mannose and glucosamine
glycoprotein
the model of enzyme HrGA with two molecules in the asymmetric unit includes residues 29-616 and up to seven N-glycosylation sites and has acarbose bound in the active site. The full-length structure of HrGA shows extensive N-glycosylation, where the resolved sites are at Asn99, Asn200, Asn427, Asn500, Asn514, Asn528 and Asn587. Asn200 is the only site that shows branching of the glycosylation chain
glycoprotein
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O-glycosylation
glycoprotein
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carbohydrate content of the enzyme is 26.3%, 34% glycosyl content is lost at 2.1 mM of periodate
glycoprotein
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two N-linked and about forty short mannose-bearing O-linked sugars per molecule. O-linked sugars essentially contribute to the stabilization of glucoamylase domains
glycoprotein
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glycosyl chains of 5 and 8 sugar residues are linked to Asp171 and Asp395 respectively
glycoprotein
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deglycosylation of the enzyme leads to reduced thermal stability and a decrease in enzyme secretion, O-glycosylation
glycoprotein
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deglycosylation of the enzyme leads to reduced thermal stability and a decrease in enzyme secretion, O-glycosylation
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glycoprotein
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carbohydrate groups seem to play an important role in stabilizing the structure against inactivation by heat and storage
glycoprotein
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glucoamylase I and glucoamylase II contain 53.0 mol of carbohydrate per mol of enzyme
glycoprotein
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carbohydrate groups seem to play an important role in stabilizing the structure against inactivation by heat and storage
glycoprotein
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glucoamylase I contains 52.2 mol of carbohydrate per mol of enzyme, glucoamylase II contains 48.5 mol of carbohydrate per mol of enzyme
glycoprotein
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O-glycosylation
glycoprotein
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contains 23% carbohydrate
glycoprotein
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the glycoprotein composition is estimated as 15% for the crude enzyme and 5.5% for the purified glucoamylase
glycoprotein
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the glycoprotein composition is estimated as 15% for the crude enzyme and 5.5% for the purified glucoamylase
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glycoprotein
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carbohydrate groups seem to play an important role in stabilizing the structure against inactivation by heat and storage
glycoprotein
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effects of deglycosylation on enzyme structure, activity and stability, overview, deglycosylation by alpha-mannosidase does not affect the pH optimum or the active site and catalytic reaction mechanism including conformational changes of the enzyme, the secondary enzyme structure remains unaltered, deglycosylation increases the enzyme aggregation and reduces the thermal stability, the deglycosylated enzyme is more sensitive to proteolytic degradation by subtilisin than the native enzyme
glycoprotein
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O-glycosylation, required for enzyme stability and activity, structure overview
glycoprotein
the linker region between starch-binding and catalytic domains is heavily glycosylated. The O-glycosylated residues are Ser467(443), Ser468(444), Thr476(452), Ser477(453), Ser483(459), Ser484(460) and Thr486(462)
glycoprotein
O-glycosylation is observed in enzyme AnGA, in particular in the linker domain, which connects to the carbohydrate-binding domain. Only two sites, at Ser483 and Ser484, can be modelled with confidence. The catalytic domain of AnGA has two resolved N-glycosylation sites at Asn195 and Asn419, with two GlcNAc residues visible at Asn195 and one at Asn419
glycoprotein
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O-glycosylation, required for enzyme stability and activity, structure overview
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glycoprotein
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4.8% glucosamine and 7.8% neutral saccharide
glycoprotein
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alpha-D-mannopyranose is the dominant sugar present - about 91 residues. Hexosamine is also present as a minor component, 2.6% of the total carbohydrate. 41 alpha-D-mannopyranose residues are O-2 and O-3 glycosylated and 17 alpha-D-mannopyranose residues are involved in O-4 glycosylation
glycoprotein
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O-glycosylation
glycoprotein
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contains 0.55% glucosamine and 12% neutral sugar which consists of a large amount of mannose and small amounts of galactose and glucose
glycoprotein
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carbohydrate groups seem to play an important role in stabilizing the structure against inactivation by heat and storage
glycoprotein
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glucoamylase II contains 40 mol of carbohydrate per mol of enzyme
glycoprotein
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glucoamylase M1 contains 18% neutral sugar and 0.77% glucosamine
glycoprotein
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glucoamylase M1 contains 102 mol of carbohydrate per mol of enzyme, glucoamylase M2 contains 57 mol of carbohydrate per mol of enzyme
glycoprotein
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O-glycosylation
glycoprotein
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O-glycosylation
glycoprotein
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O-glycosylation
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glycoprotein
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O-glycosylation
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glycoprotein
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glucoamylase G1 contains 8.1% carbohydrate, glucoamylase G2 contains 7.6% carbohydrate, glucoamylase G3 contains 8.0% carbohydrate, glucoamylase G4 and G5 contain 7.5% carbohydrate
glycoprotein
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glucoamylase G1 contains 8.1% carbohydrate, glucoamylase G2 contains 7.6% carbohydrate, glucoamylase G3 contains 8.0% carbohydrate, glucoamylase G4 and G5 contain 7.5% carbohydrate
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glycoprotein
Cephalosporium eichhorniae
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glycoprotein
Cephalosporium eichhorniae
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contains 28% carbohydrate by weight
glycoprotein
Endomycopsis fibuligera
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glycoprotein
recombinant N-terminal catalytic subunit secreted from transformed S2 cells
glycoprotein
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2.4% carbohydrate content, recombinant enzyme
glycoprotein
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glucoamylase I contains 7.5% carbohydrate, glucoamylase II contains 6.5% carbohydrate
glycoprotein
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7.4% neutral carbohydrate
glycoprotein
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7.4% neutral carbohydrate
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glycoprotein
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O-glycosylation
glycoprotein
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O-glycosylation
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glycoprotein
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enzyme form E3 contains 7% carbohydrate, enzyme form E4 contains 9% carbohydrate, enzyme form E4' contains 2.7% carbohydrate. Degree of N-glycosylation causes the conformational difference between the multiple forms of glucoamylase. Removal of N-linked sugar leeds to a significant thermostability decrease, wheras it has little effect on the catalytic activity
glycoprotein
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carbohydrate content of isozymes GA-I and GA-II is 15.0% and 16.2%, respectively
glycoprotein
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enzyme form GA-I contains 13.5% carbohydrate, enzyme form GA-II contains 9.4% carbohydrate
glycoprotein
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enzyme form GA-I contains 13.5% carbohydrate, enzyme form GA-II contains 9.4% carbohydrate
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glycoprotein
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O-glycosylation
glycoprotein
Mucor rouxians
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glycoprotein
Mucor rouxians
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O-glycosylation
glycoprotein
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2.74% neutral sugar
glycoprotein
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20% carbohydrate content
glycoprotein
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9.8% glucans
glycoprotein
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O-glycosylation
glycoprotein
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10% carbohydrate content
glycoprotein
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50% carbohydrate content
glycoprotein
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carbohydrate content 9.8%
glycoprotein
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20% carbohydrate content
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glycoprotein
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50% carbohydrate content
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glycoprotein
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10% carbohydrate content
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glycoprotein
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20% carbohydrate content
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glycoprotein
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50% carbohydrate content
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glycoprotein
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glucoamylase I and II
glycoprotein
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glucoamylase I and II
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glycoprotein
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contains 5.1% carbohydrate
glycoprotein
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O-glycosylation, 5.1% carbohydrate content
glycoprotein
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the enzyme contains 5.1% carbohydrate
glycoprotein
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sialoglycoprotein
glycoprotein
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glucoamylase I contains 3.93% neutral sugar and glucoamylase II contains 3.22% neutral sugar
glycoprotein
glycosylation may occur during enzyme protein expression
glycoprotein
the enzyme is N-glycosylated. The purified recombinant enzyme is treated with enzyme Endo H to minimize N-glycosylation. The full-length structure of PoGA shows a greater degree of N-glycosylation, PoGA three glycosylation sites at Asn184, Asn410 and Asn514 are observed, most extensive at Asn184
glycoprotein
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the enzyme is N-glycosylated. The purified recombinant enzyme is treated with enzyme Endo H to minimize N-glycosylation. The full-length structure of PoGA shows a greater degree of N-glycosylation, PoGA three glycosylation sites at Asn184, Asn410 and Asn514 are observed, most extensive at Asn184
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glycoprotein
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the enzyme is N-glycosylated. The purified recombinant enzyme is treated with enzyme Endo H to minimize N-glycosylation. The full-length structure of PoGA shows a greater degree of N-glycosylation, PoGA three glycosylation sites at Asn184, Asn410 and Asn514 are observed, most extensive at Asn184
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glycoprotein
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glycosylation may occur during enzyme protein expression
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glycoprotein
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enzyme contains 32 mol of carbohydrate per mol of enzyme
glycoprotein
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carbohydrate groups seem to play an important role in stabilizing the structure against inactivation by heat and storage
glycoprotein
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enzyme contains 89 mol of carbohydrate per mol of enzyme
glycoprotein
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O-glycosylation
glycoprotein
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O-glycosylation
glycoprotein
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O-glycosylation, isozymes glucoamylase C and D have 14.9% and 12.7% carbohydrate content, respectively
glycoprotein
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glucoamylase C and D contain 14.9% and 12.7% carbohydrate, respectively
glycoprotein
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80% of the enzyme is carbohydrate
glycoprotein
Sta1p is hyperglycosylized, over 80% carbohydrate content
glycoprotein
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80% of the enzyme is carbohydrate
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glycoprotein
Thermochaetoides thermophila
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glycoprotein
Thermochaetoides thermophila
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glycoprotein
Thermochaetoides thermophila CT2
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glycoprotein
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9.0-10.5% carbohydrate
glycoprotein
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contains 10-12% carbohydrate
glycoprotein
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contains 10-12% carbohydrate
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glycoprotein
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five potential sites for N-glycosylation
glycoprotein
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contains 5% carbohydrate
glycoprotein
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O-glycosylation
proteolytic modification
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acid proteinases are involved in generating multiple glucoamylase forms in the fungus Aspergillus awamori through limited hydrolysis of this enzyme decreasing the stability of the enzyme in a pH-dependent manner, methods for removal of proteolytic activity, overview
proteolytic modification
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proteolytic modification
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the small enzyme form G2 consists of two molecular species identical to the residues 1-512 and 1-513 of the large enzyme form G1. The enzyme form G2 is generated by limited proteolysis of the larger enzyme form G1
proteolytic modification
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cleavage of signal peptide of the recombinant enzyme expressed in Saccharomyces cerevisiae
proteolytic modification
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enzyme form GI and GII are transformed products of enzyme form GIII due to the limited action of proteases and glucosidases. GII is formed from GIII upon the release of a peptide portion of approximately 8000 Da. Enzyme form GI is formed from enzyme form GII and GIII on the removal of both peptide and carbohydrate chains and/or glycopeptide fragments
additional information
the extracellular enzyme contains a signal sequence
additional information
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no potential signal peptide sequence