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Literature summary for 2.4.1.135 extracted from

  • Ouzzine, M.; Gulberti, S.; Netter, P.; Magdalou, J.; Fournel-Gigleux, S.
    Structure/function of the human Ga1beta1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues (2000), J. Biol. Chem., 275, 28254-28260.
    View publication on PubMed
Search for more literature for 2.4.1.135

Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris Homo sapiens

Protein Variants

Protein Variants Comment Organism
C301A mutant is not N-glycosylated, molecular weight is about 4000 Da less than that of the wild-type protein, enzyme is completely inactive Homo sapiens
C33A mutation abolishes the ability of the protein to form dimers Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
N-Phenylmaleimide
-
 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Homo sapiens
0.09489
-
 UDPglucuronate wild-type enzyme Homo sapiens
0.287
-
 UDPglucuronate mutant enzyme C33A Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
 2 * 43000, SDS-PAGE after disulfide reduction Homo sapiens
85000
-
 SDS-PAGE under nonreducing conditions Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens expressed in Pichia pastoris ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information expressed in Pichia pastoris Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 43000, SDS-PAGE after disulfide reduction Homo sapiens