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1.13.11.18: persulfide dioxygenase

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

Word Map on EC 1.13.11.18

Reaction

S-sulfanylglutathione
+
O2
 +
H2O
=
glutathione
 +
sulfite
 + 2 H+

Synonyms

AFE_0269, BAE27_01805, BpPRF, cPDO-PT, CstB, ETHE1, ETHE1-like sulfur dioxygenase, Ethe2, Fe(II)-containing persulfide dioxygenase, Gly3, PDO, PRF, SDO, SOR, sulfide dioxygenase, sulfur dioxygenase, sulfur oxygenase, sulfur oxygenase/reductase

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.11 With incorporation of two atoms of oxygen
                1.13.11.18 persulfide dioxygenase

Engineering

Engineering on EC 1.13.11.18 - persulfide dioxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D130A
mutation in putative iron ligand, 0.5-2% residual activity
D130E
mutation in putative iron ligand, 0.5-2% residual activity
D130H
mutation in putative iron ligand, 0.5-2% residual activity
D141A
inactive concomitant to a decrease of melting point by 3-8 K
H113A
mutation in putative iron ligand, inactive
H113G
mutation in putative iron ligand, inactive
H171A
inactive concomitant to a decrease of melting point by 3-8 K
H57A
mutation in putative iron ligand, 6% residual activity
H57G
mutation in putative iron ligand, inactive
R139A
inactive concomitant to a decrease of melting point by 3-8 K
C161Y
mutation reported in ethylmalonic encephalopathy patients, drastic reduction in iron content
R163W
mutation reported in ethylmalonic encephalopathy patients
T136A
mutation reported in ethylmalonic encephalopathy patients
C314S
-
site-directed mutagenesis, structure comparison with wild-type enzyme. C314S BpPRF exhibits a 29fold lower kcat and an 5fold higher Km for GSSH than the wild-type
C201S
site-directed mutagenesis, the mutant protein structure is similar to the wild-type, but it shows reduced activity
C201S/C408S
site-directed mutagenesis
C2S
site-directed mutagenesis, the mutant is larger than the wild-type and is a hexamer
C408S
site-directed mutagenesis, the mutant is larger than the wild-type and is a hexamer. Substitution of the presumed Rhod active-site C408 also appears to destabilize the native protein fold. Catalytically inactive mutant
additional information