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G59C
C59 is an essential residue for enzyme activity in mammals. Mutant G59C does not show enzymic activity
C89A/C167A/C186A
site-directed mutagenesis
C89A/C186A
site-directed mutagenesis
D93N
not activated by Ca2+ or Mg2+
D96N
very high basal activity, no activation in the presence of Ca2+ or Mg2+
D97N
not activated by Ca2+ or Mg2+
F83A
the mutation reduces the catalytic efficiency by almost 10fold
K59A
the mutation enhances the catalytic efficiency by more than 2fold
L131A
the mutation reduces the catalytic efficiency by almost 10fold
L79A
the mutation reduces the catalytic efficiency by almost 10fold
M64A
the mutation reduces the catalytic efficiency by almost 10fold
M94A
the mutation reduces the catalytic efficiency
S45A
the mutation reduces the catalytic efficiency
S81A
the mutation reduces the catalytic efficiency
T147A
the mutation slightly enhances the catalytic efficiency
W43F/C65A/C167A
site-directed mutagenesis, the W43F mutant cannot be purified owing to the inclusion body formation of protein
W54A
the mutation reduces the catalytic efficiency
W54F/C65A/W112F/C167A
site-directed mutagenesis, the mutant still provides the disulfide bond between Cys89 and Cys186
Y149A
the mutation enhances the catalytic efficiency by more than 2fold
Y63S/T67S/C89A/C186A
site-directed mutagenesis
C65A
-
mutant binds all-trans-retinoic acid, bilirubin and biliverdin with high affinity. Radius of gyration is 19.4 A for the free enzyme, and it become compact after binding of these ligands
C89A/C186A
mutant retains wild-type like activity and is stable
DELTA1-24_C65A L-PGDS
mutant, preserves a disulfide bond between Cys89 and Cys186
DELTA1-24_C65A+H111A
mutant
DELTA1-24_C65A+P110A
mutant
DELTA1-24_C65A+W54A
mutant
DELTA1-24_L-PGDS+H111A
mutant
DELTA1-24_L-PGDS+H116A
mutant
DELTA1-24_L-PGDS+P110A
mutant
DELTA1-24_L-PGDS+S45A
mutant
DELTA1-24_L-PGDS+S45A/S81A
mutant
DELTA1-24_L-PGDS+S45A/T67A
mutant
DELTA1-24_L-PGDS+S45A/T67A/S81A
mutant
DELTA1-24_L-PGDS+S81A
mutant
DELTA1-24_L-PGDS+T67A
mutant
DELTA1-24_L-PGDS+T67A/S81A
mutant
DELTA1-24_L-PGDS+W45A
mutant
DELTA1-24_L-PGDS+W54A/H111A
mutant
W54A
mutant retains wild-type like activity and is stable
A106S
-
creation of a new protein kinase C phosphorylation site, significant inhibition of the ability of enzyme to induce apoptosis and significant decrease in catalytic activity
C156L
loss of prostaglandin D synthase activity, retention of glutathione S-transferase activity
C156Y
loss of prostaglandin D synthase activity, retention of glutathione S-transferase activity
C65A/C89A/C186A
-
mutant is properly folded with well-defined tertiary structures
D51A
-
creation of new glycosylation site 1, significant inhibition of the ability of enzyme to induce apoptosis and significant decrease in catalytic activity
D78A
-
creation of new glycosylation site 2, no significant changes in enzyme activity or ability to induce apoptosis
K112E
retention of prostaglandin D synthase and glutathione S-transferase activity
K198E
retention of prostaglandin D synthase and glutathione S-transferase activity
L199F
retention of prostaglandin D synthase and glutathione S-transferase activity
R14E
complete loss of prostaglandin D synthase activity and glutathione S-transferase activity
R14K
complete loss of prostaglandin D synthase activity and glutathione S-transferase activity
W104I
complete loss of prostaglandin D synthase activity and glutathione S-transferase activity
Y152F
retention of prostaglandin D synthase and glutathione S-transferase activity
Y8F
complete loss of prostaglandin D synthase activity and glutathione S-transferase activity
C65A/C167A
inactive
C65A/C167A
site-directed mutagenesis
C65A/C167A
site-directed mutagenesis, the mutant still provides the disulfide bond between Cys89 and Cys186
C65A/C167A
site-directed mutagenesis, the mutation limits incorrect intra- and intermolecular disulfide bonds and protein aggregation during recombinant enzyme expression and purification
C65A/C167A
the mutations abolish enzymatic activity
C186A
-
mutant is properly folded with well-defined tertiary structures
C186A
-
no significant change in conformation. Decrease in stability and in dissociation constants for 8-anilino-1-naphthalenesulfonic acid and retinoic acid. Urea-induced unfolding at 2.875 mol/l compared with 5.75 mol/l for wild-type
C65A
-
mutation of active site, significant inhibition of the ability of enzyme to induce apoptosis and significant decrease in catalytic activity
C65A
-
mutant is properly folded with well-defined tertiary structures
C65A
-
no significant change in conformation. Urea-induced unfolding at 5.125 mol/l compared with 5.75 mol/l for wild-type
C89A/C186A
-
mutant is properly folded with well-defined tertiary structures
C89A/C186A
-
no significant change in conformation. Decrease in stability and in dissociation constants for 8-anilino-1-naphthalenesulfonic acid. Urea-induced unfolding at 2.625 mol/l compared with 5.75 mol/l for wild-type
additional information
chimeric protein construct carrying the mouse amino-terminal portion from D25 to L84, and zebrafish carboxyl-terminal portion from K79 to A184, shows weak enzymic activity
additional information
-
chimeric protein construct carrying the mouse amino-terminal portion from D25 to L84, and zebrafish carboxyl-terminal portion from K79 to A184, shows weak enzymic activity
additional information
-
transgenic expression of hematopoitic prostaglandin synthase in ApcMin/+ mice have 80% fewer intestinal adenomas
additional information
-
apoptosis induced by chemotherapeutics paclitaxel, cisplatin and 5-fluorouracil is prevented by siRNA targeting lipocalin-type prostaglandin synthase-D
additional information
knockdown of the enzyme expression by siRNA in SH-SY5Y cells, two different siRNAs
additional information
-
chimeric protein construct carrying the mouse amino-terminal portion from D25 to L84, and zebrafish carboxyl-terminal portion from K79 to A184, shows weak enzymic activity
additional information
-
disruption of gene for hematopoietic prostaglandin synthase in ApcMin/+ mice bearing a defect in the adenomatous polyposis coli gene which leads to development of many adenomas leads to 50% more intestinal adenomas compared with controls. Tumour size is not affected
additional information
-
enzyme knockout animals and transgenic animals. Knockout mice display a more severe inflammatory response that fails to resolve, whereas transgenic mice have little detectable inflammation. Lymphocytes isolated from inguinal lymph nodes of knockout mice show hyperproliferation and increased IL-2 synthesis effects that are rescued by 15-deoxy-DELTA12,14-prostaglandin J2, but not prostaglandin D2
additional information
-
transgenic mice overexpressing the enzyme improve clearance of Pseudomonas from the lung compared with nontransgenic mice, as does intratracheal instillation of prostaglandin D2. Enzyme knock-out mice show impaired ability to remove Pseudomonas from the lung
additional information
-
adipocytes from lipocalin-type prostaglandin synthase-D knockout mice are significantly less sensitive to insulin-stimulated glucose transport than wild-type
additional information
-
generation of double knock out mice lacking lipocalin prostaglandin D synthase and PPARgamma2
additional information
-
generation of double knock out mice lacking lipocalin prostaglandin D synthase and PPARgamma2
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