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2.4.2.26: protein xylosyltransferase

This is an abbreviated version!
For detailed information about protein xylosyltransferase, go to the full flat file.

Word Map on EC 2.4.2.26

Reaction

UDP-alpha-D-xylose
+
[protein]-L-serine
=
UDP
 +
[protein]-3-O-(beta-D-xylosyl)-L-serine

Synonyms

LARGE, More, peptide O-xylosyltransferase, peptide O-xylosyltransferase 1, peptide-O-xylosyltransferase, Rumi, squashed vulva protein 6, SQV-6, UDP-alpha-D-xyloase:proteoglycan core protein beta-D-xylosyltransferase, UDP-alpha-D-xylose:proteoglycan core protein beta-D-xylosyltransferase, UDP-D-xylose:core protein beta-D-xylosyltransferase, UDP-D-xylose:core protein xylosyltransferase, UDP-D-xylose:proteoglycan core protein b-d-xylosyltransferase, UDP-D-xylose:proteoglycan core protein beta-D-xylosyltransferase, UDP-xylose-core protein beta-D-xylosyltransferase, uridine diphosphoxylose-core protein beta-xylosyltransferase, uridine diphosphoxylose-protein xylosyltransferase, XT, XT-I, XT-II, xylosyltransferase, xylosyltransferase 1, xylosyltransferase 2, xylosyltransferase I, xylosyltransferase II, xylosyltransferase sqv-6, xylosyltransferase, uridine diphosphoxylose-core protein beta-, xylosyltransferase-I, xylosyltransferases II, XylT-I, XylT-II, XYLT1, XYLT2

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.26 protein xylosyltransferase

Engineering

Engineering on EC 2.4.2.26 - protein xylosyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C257A
2.3fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C276A
-
mutation results in a nearly inactive enzyme
C285A
5.4fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C301A
2.3fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C471A
complete loss of catalytic activity. N-phenylmaleimide treatment shows no effect on wild-type XT-I but strongly inactivates the cysteine mutant
C542A
2.9fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C561A
UDP inhibition is significantly reduced
C563A
2fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C574A
complete loss of catalytic activity. N-phenylmaleimide treatment shows no effect on wild-type XT-I but strongly inactivates the cysteine mutant
C675A
1.5fold increase in the ratio of Vmax to KM-value as compared to wild-type enzyme
C902A
1.5fold increase in the ratio of Vmax to KM-value as compared to wild-type enzyme
C927A
1.4fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C933A
1.36fold increase in the ratio of Vmax to KM-value as compared to wild-type enzyme
D314G
80% of the activity of wild-type enzyme,Km-value for bikunin is 1.2fold higher than wild-type value
D316G
as active as wild-type enzyme, Km-value for bikunin is identical to wild-type value
D745E
mutant retains full activity, Km-value for bikunin is 1.2fold higher than wild-type value
D745G
loss of activity
D747E
reduced substrate affinity, about 35% of the wild-type activity, Km-value for bikunin is 4.4fold higher than wild-type value
D747G
reduced substrate affinity, about 35% of the wild-type activity, Km-value for bikunin is 7.7fold higher than wild-type value
DELTA1-184
-
KM-value for bikunin is identical to wild-type value, Vmax is 1.2fold higher than wild-type value
DELTA1-213
-
KM-value for bikunin is 1.6fold higher than wild-type value, Vmax is 1.1fold higher than wild-type value
DELTA1-260
-
KM-value for bikunin is 1.6fold higher than wild-type value, Vmax is identical to wild-type value
DELTA1-266
-
KM-value for bikunin is 5.6fold higher than wild-type value, Vmax is 1.6fold lower than wild-type value
DELTA1-272
-
KM-value for bikunin is 6fold higher than wild-type value, Vmax is 1.3fold lower than wild-type value
DELTA1-273
-
more than 98% of activity
DELTA261-272
-
inactive mutant enzyme
DELTA721-726
-
inactive mutant enzyme
E263A
-
KM-value for bikunin is 1.4fold higher than wild-type value, Vmax is 2fold higher than wild-type value
K262A
-
KM-value for bikunin is 1.2fold higher than wild-type value, Vmax is 1.7fold higher than wild-type value
K272A
-
KM-value for bikunin is 1.4fold higher than wild-type value, Vmax is 1.7fold higher than wild-type value
R270A
-
KM-value for bikunin is 1.2fold higher than wild-type value, Vmax is 1.4fold higher than wild-type value
S266A
-
KM-value for bikunin is 1.4fold higher than wild-type value, Vmax is 1.3fold higher than wild-type value
S269A
-
KM-value for bikunin is 1.3fold higher than wild-type value, Vmax is 1.1fold higher than wild-type value
W746D
about 25% of wild-type activity, Km-value for bikunin is 1.3fold higher than wild-type value
W746G
about 25% of wild-type activity, Km-value for bikunin is 1.3fold higher than wild-type value
W746N
about 25% of wild-type activity, Km-value for bikunin is 1.4fold higher than wild-type value
additional information
-
truncation of 266, 272 and 273 amino acids in the N-terminal region results in a 70, 90 and above 98% loss in catalytic activity. Deletion of the single 12 amino acid motif G261KEAISALSRAK272 leads to a loss-of-function xylosyltransferase I mutant. Heparin binding is slightly altered in mutants lacking 289 or 568 amino acids, but deletion of the potential heparin-binding motif P721KKVFKI727 does not lead to a loss of heparin binding capacity