Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.2.1.169: protein O-GlcNAcase

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

Word Map on EC 3.2.1.169

Reaction

[protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine
+
H2O
=
[protein]-L-serine
 +
N-acetyl-D-glucosamine

Synonyms

beta-N-acetylglucosaminidase, BtGH84, CP40, CpNagJ, CpOGA, cytoplasmic O-GlcNAcase, endo-beta-N-acetylglucosaminidase, EndoS-like endoglycosidase, glycoside hydrolase O-GlcNAcase, hexosaminidase, hOGA, mNCOAT, NagJ, NCOAT, neutral hexosaminidase C, neutral O-GlcNAcase, O-GlcNAc hydrolase, O-GlcNAc selective N-acetyl-beta-D-glucosaminidase, O-GlcNAc specific beta-N-acetylglucosaminidase, O-GlcNAc-selective N-acetyl-beta-D-glucosaminidase, O-GlcNAc-selective-N-acetyl-beta-D-glucosaminidase, O-GlcNAcase, O-linked beta-N-acetyl glucosaminase, O-linked N-acetylglucosaminase, OGA, OGA-FL, OGA-NV

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.169 protein O-GlcNAcase

Engineering

Engineering on EC 3.2.1.169 - protein O-GlcNAcase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D242A
site-directed mutant, 2800fold lower catalytic efficiency than wild-type
D242N
D243A
site-directed mutant, 110fold lower catalytic efficiency than wild-type
D243N
N372A
site-directed mutant
Y137F
site-directed mutant
Y282F
site-directed mutant
D297N
rather inactive mutant
D298N
D401A
N390A
as active as wild-type
N396A
rather inactive mutant
V331C
mutation of Val331 to cysteine results in a mutant enzyme with unaltered steady-state kinetics compared with wild-type CpOGA
W490A
Y335F
rather inactive mutant
D298N
-
inactive mutant which retains the ability to bind to O-GlcNAcylated peptides
D401A
-
the mutant displays 5fold increase in KM and 2400fold decrease in kcat compared to the wild type enzyme
C896W
-
site-specific mutagenesis, in the tryptic peptide LGCFEIAK (894-901). Site-specific mutagenesis of the C-terminal glycine and cysteine residues (G895A and C896W) present in the tryptic peptide LGCFEIAK (894–901) causes little or no inhibition of O-GlcNAcase activity (72.3% of control and 129.9% of control, respectively)
D174A
-
generated mutant, reveals severely impaired catalytic activity across a broad range of substrates alongside a pH-activity profile consistent with deletion of a key catalytic residue
D175A
-
generated mutant, significant decrease in catalytic efficiency with substrates bearing poor leaving groups (up to 3000fold), while for substrates bearing good leading groups the difference is much smaller (7fold). Mutant enzyme cleaves thioglycosides with essentially the same catalytic efficiency as the wild-type enzyme
D175N
inactive
DELTA1-350
-
deletion construct comprising amino acids 1-350 of human O-GlcNAcase
DELTA351-916
-
deletion construct comprising amino acids 351-916 of human O-GlcNAcase
E130A
-
site-specific mutagenesis, in the tryptic peptide EYEIEFIYAISPGLDITFSNPK (128-149), retains almost full enzymatic activity (97.3% of control)
F133V
-
site-specific mutagenesis, in the tryptic peptide EYEIEFIYAISPGLDITFSNPK (128-149), no O-GlcNAcase activity (3.3% of control)
G895A
-
site-specific mutagenesis, in the tryptic peptide LGCFEIAK (894-901). Site-specific mutagenesis of the C-terminal glycine and cysteine residues (G895A and C896W) present in the tryptic peptide LGCFEIAK (894–901) causes little or no inhibition of O-GlcNAcase activity (72.3% of control and 129.9% of control, respectively)
S138I
-
site-specific mutagenesis, in the tryptic peptide EYEIEFIYAISPGLDITFSNPK (128-149), exhibits greatly reduced activity (15.4% of control)
v-O-GlcNAcase
-
variant OGlcNAcase, isoform lacking the C-terminal third of the full-length O-GlcNAcase
Y129F
-
site-specific mutagenesis, in the tryptic peptide EYEIEFIYAISPGLDITFSNPK (128-149), retains almost full enzymatic activity (90.5% of control)
C166S
site-directed mutagenesis
C878S
site-directed mutagenesis, comparable level of O-GlcNAcase activity as wild-type enzyme
D174N
site-directed mutagenesis
D175A
site-directed mutagenesis
D177N
site-directed mutagenesis
DELTA250-345
protein missing amino acids 250-345, due to the removal of exon 8
DELTA250-398
lacks amino acids 250-398 in the protein due to the specific excision of exons 8 and 9