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2.6.1.98: UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase

This is an abbreviated version!
For detailed information about UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase, go to the full flat file.

Reaction

UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
+
2-oxoglutarate
=
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate
+
L-glutamate

Synonyms

aminotransferase WbpE, PGN_1236, PorR, WbpE, WlbC, WpbE

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.98 UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase

Engineering

Engineering on EC 2.6.1.98 - UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D156A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
H308A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
K185A
site-directed mutagenesis, the activity of the catalytic site mutant is completely abolished
N227A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
Q159A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
R229A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
S180A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
T60A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
Y309A
site-directed mutagenesis, the mutant shows only slightly affected activity and slight loss of binding affinity compared to the wild-type
additional information
-
construction of a nonpolar knockout of each of wbpA, wbpB, wbpE, wbpD, and wbpI genes. Expression of Bordetella pertussis genes wbpO1629 and wbpO3150 complements a wbpA knockout of Pseudomonas aeruginosa. B-band LPS production is restored to Pseudomonas aeruginosa knockout mutants when the relevant Bordetella pertussis genes are supplied in trans