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Literature summary for 2.4.2.26 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)

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

Protein Variants

Protein Variants Comment Organism
C257A 2.3fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
C285A 5.4fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
C301A 2.3fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
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
C542A 2.9fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
C561A UDP inhibition is significantly reduced Homo sapiens
C563A 2fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
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
C675A 1.5fold increase in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
C902A 1.5fold increase in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
C927A 1.4fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens
C933A 1.36fold increase in the ratio of Vmax to KM-value as compared to wild-type enzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
N-Phenylmaleimide treatment shows no effect on wild-type XT-I but strongly inactivaets the cysteine mutants C461A and C574A Homo sapiens
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]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Homo sapiens Q86Y38
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
XT-I
-
Homo sapiens
xylosyltransferase I
-
Homo sapiens