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5.3.99.2: Prostaglandin-D synthase

This is an abbreviated version!
For detailed information about Prostaglandin-D synthase, go to the full flat file.

Word Map on EC 5.3.99.2

Reaction

(5Z,13E,15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
=
(5Z,13E,15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate

Synonyms

beta-Trace, Beta-trace protein, betaTP, glutathione dependent prostaglandine D2 synthase, Glutathione-dependent PGD synthetase, glutathione-dependent prostaglandin D2 synthase, Glutathione-independent PGD synthetase, H-PGDS, haematopoietic PGD synthase, haematopoietic prostaglandin D synthase, Hematopoietic prostaglandin D synthase, hematopoietic prostaglandin D2 synthase, HPGDS, Isomerase, prostaglanin R2 D-, L-PGDS, L-prostaglandin D synthase, L-type prostaglandin synthase, lipocalin prostaglandin D synthase, lipocalin type prostaglandin D synthase, lipocalin-prostaglandin D synthase, lipocalin-type PG D synthase, lipocalin-type PGD synthase, lipocalin-type Pgds, lipocalin-type prostaglandin d synthase, lipocalin-type prostaglandin D2 synthase, lipocaline-type prostaglandin D synthase, PGD synthase, PGD-S, PGD2 synthase, PGD2 synthetase, PGDS, PGDS2, PGH-PGD isomerase, PGH2 D-isomerase, Prostaglandin D synthase, Prostaglandin D2 synthase, prostaglandin D2 synthetase, prostaglandin synthase, Prostaglandin-D synthase, Prostaglandin-H2 D-isomerase, Prostaglandin-R-prostaglandin D isomerase, PTGDS

ECTree

     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.99 Other intramolecular oxidoreductases
                5.3.99.2 Prostaglandin-D synthase

Engineering

Engineering on EC 5.3.99.2 - Prostaglandin-D synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G59C
C59 is an essential residue for enzyme activity in mammals. Mutant G59C does not show enzymic activity
C65A
inactive
C65A/C167A
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
Y8F
active site mutant
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
mutant
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
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
C186A
C65A/C89A/C186A
-
mutant is properly folded with well-defined tertiary structures
C89A/C186A
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
additional information