1.13.11.20: cysteine dioxygenase

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

Word Map on EC 1.13.11.20

Reaction

L-cysteine
+
O2
=
3-sulfinoalanine

Synonyms

3-mercaptopropionate dioxygenase, Arg-type CDO, BsCDO, CDO, CDO1, CDO2, CdoA, CdoB, cysteine dioxygenase, cysteine oxidase, Fe(II) cysteine dioxygenase, H16_A1614, H16_B1863, oxygenase, cysteine di-

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
                1.13.11.20 cysteine dioxygenase

Engineering

Engineering on EC 1.13.11.20 - cysteine dioxygenase

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
C164A
-
mutation of C164 shows a about 20% abatement of enzymatic activity
C164S
-
mutation of C164 shows a about 20% abatement of enzymatic activity
C93S
-
C93 mutation reduces activity to 50%, zinc content of about 45%, specific activity of Cys-93 mutants is proportional to the measured iron content.
R60A
-
similar results as R60Q, R60 mutation reduces activity to 30%
R60Q
-
R60 mutation reduces activity to 30%
Y157F
-
in the gel-filtration chromatography Y157F shows an additional peak with an estimated molecular weight equivalent to a cysteine dioxygenase dimer. The results for monomer and dimer are similar. Activity reduced to 5% of the wild type activity. Zinc content of about 45%
C164A
-
mutations of nonessential residues has little effect
C93A
-
site-directed mutagenesis, mutation of the active site residue, no crosslink formation resulting in reduced activity compared to the wild-type enzyme. The mutant variant structure has a new chloride ion coordinating the active site iron. Cys binding is also different from wild-type CDO, and no Cys-persulfenate forms in the C93A active site at pH 6.2 or pH 8.0
C93S
-
mutant can not be converted to the mature form due to the loss of the cysteine residue involved in thioether crosslink formation
R60A
-
mutant forms with low activity, which has a markedly decreased affinity for cysteine, probably due to the loss of the hydrogen bonding partner for the carboxylate of the substrate, forms the crosslink more slowly
S153A
-
mutations of nonessential residues has little effect
Y157F
-
site-directed mutagenesis, mutation of the active site residue, no crosslink formation resulting in reduced activity compared to the wild-type enzyme. The mutant variant structure has a new chloride ion coordinating the active site iron. Cys binding is also different from wild-type CDO, and no Cys-persulfenate forms in the Y157F active site at pH 6.2 or pH 8.0
additional information