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Literature summary extracted from

  • Müller, S.; Schöttler, M.; Schön, S.; Prante, C.; Brinkmann, T.; Kuhn, J.; Götting, C.; Kleesiek, K.
    Human xylosyltransferase I: functional and biochemical characterization of cysteine residues required for enzymic activity (2005), Biochem. J., 386, 227-236.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.2.26 soluble active form of human XT-I is expressed in High Five insect cells, Trichoplusia ni Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.4.2.26 C257A 2.3fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
2.4.2.26 C285A 5.4fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
2.4.2.26 C301A 2.3fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
2.4.2.26 C471A complete loss of catalytic activity. N-phenylmaleimide treatment shows no effect on wild-type XT-I but strongly inactivates the cysteine mutant Homo sapiens
2.4.2.26 C542A 2.9fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
2.4.2.26 C561A UDP inhibition is significantly reduced Homo sapiens
2.4.2.26 C563A 2fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
2.4.2.26 C574A complete loss of catalytic activity. N-phenylmaleimide treatment shows no effect on wild-type XT-I but strongly inactivates the cysteine mutant Homo sapiens
2.4.2.26 C675A 1.5fold increase in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
2.4.2.26 C902A 1.5fold increase in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
2.4.2.26 C927A 1.4fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
2.4.2.26 C933A 1.36fold increase in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.26 N-Phenylmaleimide treatment shows no effect on wild-type XT-I but strongly inactivaets the cysteine mutants C461A and C574A Homo sapiens
2.4.2.26 UDP inhibition on the XT-I activity of C561A mutant enzyme is significantly reduced compared with all other tested cysteine mutants Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.26 0.001
-
bikunin pH 6.5, 37°C, wild-type enzyme Homo sapiens
2.4.2.26 0.001
-
bikunin pH 6.5, 37°C, mutant enzyme C933A Homo sapiens
2.4.2.26 0.0012
-
bikunin pH 6.5, 37°C, mutant enzyme C920A Homo sapiens
2.4.2.26 0.0014
-
bikunin pH 6.5, 37°C, mutant enzyme C301A Homo sapiens
2.4.2.26 0.0014
-
bikunin pH 6.5, 37°C, mutant enzyme C675A Homo sapiens
2.4.2.26 0.0016
-
bikunin pH 6.5, 37°C, mutant enzyme C542A Homo sapiens
2.4.2.26 0.002
-
bikunin pH 6.5, 37°C, mutant enzyme C927A Homo sapiens
2.4.2.26 0.0028
-
bikunin pH 6.5, 37°C, mutant enzyme C285A Homo sapiens
2.4.2.26 0.0053
-
bikunin pH 6.5, 37°C, mutant enzyme C257A Homo sapiens
2.4.2.26 0.0119
-
bikunin pH 6.5, 37°C, mutant enzyme C563A Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.2.26 90000
-
1 * 90000, SDS-PAGE under reducing conditions Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.26 Homo sapiens Q86Y38
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.26 UDP-D-xylose + bikunin
-
Homo sapiens UDP + D-xylosyl-bikunin
-
?

Subunits

EC Number Subunits Comment Organism
2.4.2.26 monomer 1 * 90000, SDS-PAGE under reducing conditions Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.4.2.26 XT-I
-
Homo sapiens
2.4.2.26 xylosyltransferase I
-
Homo sapiens