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no glycoprotein
but enzyme contains 1 putative N-glycosylation site at N326
glycoprotein
presence of at least two glycosylation sites on the mature protease. Glycosylation of prolegumain is necessary for correct processing to active forms and internalization
glycoprotein
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putative Asn-glycosylation sites at Asn85 and Asn270
glycoprotein
C-terminal hexa-His-tag is cleaved off together with the pro-peptide
glycoprotein
asparagine-linked glycosylation
glycoprotein
4 potential N-glycosylation sites at Asn91, ASn167, Asn263, and Asn272
glycoprotein
the enzyme harbours 4 N-glycosylation sites resulting in a molecular weight of about 56000 Da of the fully glycosylated proenzyme
glycoprotein
IsAE2 harbors three N-glycosylation sites
glycoprotein
potential N-linked glycosylation sites (NXS/T) are detected at Asn-68 and Asn-173
glycoprotein
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4 potential N-glycosylation sites at Asn91, ASn167, Asn263, and Asn272
glycoprotein
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N-glycosylation, deglycosylation by N-glycosidase F
glycoprotein
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probably N-glycosylated
proteolytic modification
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autocatalytic processing of inactive proenzyme to the active mature enzyme by removal of C- and N-terminally propeptides, activation takes place in the vacuole or cell wall after fusion with the ER bodies
proteolytic modification
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autoactivation by removal of the propeptide, activation after arrival in the vacuole
proteolytic modification
mechanisms of autoactivation, including a plant-specific two-chain activation state, which remains conformationally stable at neutral pH, which is a prerequisite for full ligase activity and survival in different cell compartments
proteolytic modification
activation of the recombinant legumain is autocatalytic and triggered by acidic pH
proteolytic modification
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Both recombinant legumain expressed in yeast and endogenous legumain are able to be converted into active protein of approximately 37 kDa via a C-terminal autocleavage at acid pH values
proteolytic modification
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autoactivation by removal of the propeptide, activation after arrival in the vacuole
proteolytic modification
N-terminal and C-terminal cleavage sites predicted, N-terminal sequence
proteolytic modification
N-terminal and C-terminal cleavage sites predicted, N-terminal sequence indicated
proteolytic modification
cleavage site at asparagines 364-365 at the C-terminus identified in endogenous and in recombinant protein
proteolytic modification
the values expected on the basis of the predicted MW indicating that post-translational processing of HlLgm2 occurred during biosynthesis to form a mature protein through removal of 9 kDa peptides from the precursor protein, putative C-terminal autocleavage at site Asn364-365
proteolytic modification
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cleavage site at asparagines 364-365 at the C-terminus identified in endogenous and in recombinant protein
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proteolytic modification
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autocatalytic activation by cleavage of aspartic acid residues, overview
proteolytic modification
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autolytic activation upon exposure to acidic pH
proteolytic modification
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the 56 kDa proform is cleavaed to the active 46 kDa and 36 kDa forms
proteolytic modification
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autoactivation/maturation by cleavage at Asn323
proteolytic modification
legumain is synthesized as a zymogen und undergoes pH-dependent autoproteolytic activation. All but one of the autocatalytic cleavage events occur in trans, with only the release of the C-terminal propeptide being relevant to enzymatic activity. Legumain matures to the fully active form (super-activation) only when incubated at pH 4.0
proteolytic modification
human prolegumain starts with a signal peptide (Met1-Ala17) that is released during trafficking, followed by a short 8 amino acid N-terminal propeptide (Val18-Asp25), the cysteine protease domain (Gly26-Asn323) and a C-terminal prodomain (Asp324-Tyr433)
proteolytic modification
the optimum pH for the autocatalytic activation of recombinant legumain is very acidic at a pH value of 3
proteolytic modification
C-terminus, in endogenous and in recombinant protein
proteolytic modification
autocatalytic processing of inactive proenzyme to the active mature enzyme by removal of C- and N-terminally propeptides, activation takes place in the vacuole or cell wall
proteolytic modification
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different processed forms of Papaver VPE exist
proteolytic modification
putative cleavage site is N367-E368
proteolytic modification
-
autoactivation by removal of the propeptide, activation after arrival in the vacuole
proteolytic modification
-
autocatalytic processing of inactive proenzyme to the active mature enzyme by removal of C- and N-terminally propeptides, activation takes place in the vacuole or cell wall, precursor is cleaved at sites containing Asn residues at the P1 position
proteolytic modification
-
autoactivation by removal of the propeptide, activation after arrival in the vacuole
proteolytic modification
C-terminus, in endogenous and in recombinant protein
proteolytic modification
autoactivation
proteolytic modification
autoactivation
proteolytic modification
autoactivation at 37°C, pH 4.5
proteolytic modification
-
autoactivation/maturation by cleavage at Asn323
proteolytic modification
-
three-dimensional modeling shows that the propeptide, which is located in the terminal C region of legumains blocks the catalytic cleft
proteolytic modification
-
autocatalytic processing of inactive proenzyme to the active mature enzyme by removal of C- and N-terminally propeptides, activation takes place in the vacuole or cell wall after fusion with the ER bodies
proteolytic modification
-
autoactivation by removal of the propeptide, activation after arrival in the vacuole
proteolytic modification
-
autoactivation by removal of the propeptide, activation after arrival in the vacuole