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glycoprotein
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glycoprotein
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sialoglycoprotein
glycoprotein
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both subunits are glycoproteins
glycoprotein
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20% carbohydrate
glycoprotein
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rich in carbohydrates
glycoprotein
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contains neutral and amino sugars and sialic acid
glycoprotein
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Ggt1 occurrs as a very large glycoprotein complex
glycoprotein
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sialoglycoprotein
glycoprotein
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comparison of sugar content of enzymes from tumour and normal tissue source, overview
glycoprotein
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recombinant wild-type and mutant
glycoprotein
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rich in carbohydrates
glycoprotein
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binding of concanavalin A
glycoprotein
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binding of lentil lectin
glycoprotein
autocatalytic cleavage of human gamma-glutamyl transpeptidase is highly dependent on N-glycosylation at asparagine 95. The large subunit of the enzyme contains six N-glycosylation sites (Asn-95, -120, -230, -266, -297, and -344), and the small subunit contains a single site (Asn-511)
glycoprotein
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rich in carbohydrates
glycoprotein
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enzyme form GGT A
glycoprotein
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enzyme form GGT B
glycoprotein
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enzyme form GGT I
glycoprotein
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enzyme form GGT II
glycoprotein
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sialoglycoprotein
glycoprotein
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post-translational multiple forms differing in sugar portion
glycoprotein
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rich in carbohydrates
glycoprotein
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heterogenous, tissue-dependent glycosylation pattern
glycoprotein
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both subunits are glycoproteins, structure
glycoprotein
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binding of concanavalin A
glycoprotein
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36% carbohydrate
glycoprotein
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31.4% carbohydrates, binds lentil lectin
glycoprotein
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31.4% carbohydrates, binds lentil lectin
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glycoprotein
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isoforms I and II
glycoprotein
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binding of concanavalin A
lipoprotein
the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
lipoprotein
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the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
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lipoprotein
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the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
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lipoprotein
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the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
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lipoprotein
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the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
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lipoprotein
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the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane
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proteolytic modification
the two separate polypeptide chains of 45.7 and 19.7 kDa forming the GGT heterodimeric enzyme are generated via autocatalytic cleavage from a precursor
proteolytic modification
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the two separate polypeptide chains of 45.7 and 19.7 kDa forming the GGT heterodimeric enzyme are generated via autocatalytic cleavage from a precursor
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proteolytic modification
maturation mechanism of autocatalytic processing of BlGGT proceeds with residue Thr417 functioning as the activator. In the structure of T399A-BlGGT, the side-chain of Thr417 is located at a competent position to activate the catalytic threonine (Thr399) and the main chain atoms of this residue is held in position by the side chain of Arg571, which in turn interacts with the side chain of Glu398 through electrostatic interactions. Then, the side chains of Glu398 and Arg571 are held in their spatial positions by the hydrogen bond networks involving His401, Ser479, Gly481, Gly482, Thr484, Asn550, and two water molecules. In this respect, residues Gly481 and Gly482 may play a role in the autocatalytic processing of BlGGT
proteolytic modification
Q62WE3
the enzyme is synthetized as single-chain precursor, and then self-processes to form the mature enzyme. Analysis of autocatalytic processing of recombinant mutant enzymes expressed in Escherichia coli strain M15
proteolytic modification
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
proteolytic modification
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the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
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proteolytic modification
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the enzyme is synthetized as single-chain precursor, and then self-processes to form the mature enzyme. Analysis of autocatalytic processing of recombinant mutant enzymes expressed in Escherichia coli strain M15
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proteolytic modification
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the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
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proteolytic modification
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the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
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proteolytic modification
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the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
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the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
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the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
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the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
proteolytic modification
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the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
-
proteolytic modification
the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
proteolytic modification
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the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
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proteolytic modification
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the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
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proteolytic modification
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the GGT heterodimeric enzyme is generated via autocatalytic cleavage from a precursor
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proteolytic modification
the enzyme is expressed as a single inactive pre-protein that undergoes posttranslational proteolytic self-cleavage
proteolytic modification
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the enzyme is expressed as a single inactive pre-protein that undergoes posttranslational proteolytic self-cleavage
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proteolytic modification
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the enzyme is expressed as a single inactive pre-protein that undergoes posttranslational proteolytic self-cleavage
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proteolytic modification
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the enzyme is expressed as a single inactive pre-protein that undergoes posttranslational proteolytic self-cleavage
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proteolytic modification
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the enzyme is expressed as a single inactive pre-protein that undergoes posttranslational proteolytic self-cleavage
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proteolytic modification
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the enzyme is expressed as a single inactive pre-protein that undergoes posttranslational proteolytic self-cleavage
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proteolytic modification
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the enzyme is synthesized as a precursor homotetrameric protein of 60-kDa per subunit, and undergoes an internal post-translational cleavage of the 60 kDa monomer into 40- and 21-kDa shorter subunits, which are then assembled into an active heterotetramer composed of two 40- and two 21-kDa subunits
proteolytic modification
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the enzyme is synthesized as a precursor homotetrameric protein of 60-kDa per subunit, and undergoes an internal post-translational cleavage of the 60 kDa monomer into 40- and 21-kDa shorter subunits, which are then assembled into an active heterotetramer composed of two 40- and two 21-kDa subunits
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proteolytic modification
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the 60000 Da proenzyme is kinetically competent to form the mature 40000 and 20000 Da subunits and exhibits maximal autoprocessing activity at neutral pH. Processing is required for enzymatic activity
proteolytic modification
protein is processed to subunits of 23000 and 40000 Da
proteolytic modification
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protein is processed to subunits of 23000 and 40000 Da
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proteolytic modification
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rat gammaGT is synthesized as a propeptide of 568 amino acids and is cleaved to yield a stable heterodimer with a large amphipathic subunit (379 amino acids) and a smaller hydrophilic subunit (189 amino acids). gammaGT propeptide cleavage occurs within the endoplasmic reticulum