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Literature summary for 3.2.1.31 extracted from

  • Tanaka, J.; Gasa, S.; Sakurada, K.; Miyazaki, T.; Kasai, M.; Makita, A.
    Characterization of the subunits and sugar moiety of human placental and leukemic beta-glucuronidase (1992), Biol. Chem. Hoppe-Seyler, 373, 57-62.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein glycosylated at Asn173 and Asn420 with high mannose-type oligosaccharides Homo sapiens
phosphoprotein both the placental 80000 Da and 64000 Da peptides, though not the 18000 Da one, are apparently phosphorylated, whereas the enzyme of leukemic cells is poorly phosphorylated Homo sapiens
proteolytic modification the 80000 Da form is a protein from which a 22000 amino-acid-N-terminal signal peptide has been removed. A second cleavage occurs between the 159th and 160th amino acid to produce the 64000 Da and 18000 Da polypeptides. Thus the 18000 Da polypeptide of 137 amino acids represents the N-terminal part of the 80000 Da precursor Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
leukemia cell chronic myelogenous Homo sapiens
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placenta
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Homo sapiens
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Subunits

Subunits Comment Organism
More the enzyme is composed of three components of 18000, 64000 and 80000 Da Homo sapiens