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EC Tree
IUBMB Comments This bacterial enzyme contains an iron(2+) atom coordinated by three protein-derived histidines and a Ser-His-Tyr motif. It is similar to EC 1.13.11.20, cysteine dioxygenase, and can act on L-cysteine, but has a much higher activity with its native substrate, 3-sulfanylpropanoate.
The enzyme appears in viruses and cellular organisms
Synonyms
3-mercaptopropionic acid dioxygenase, 3-sulfanylpropanoate dioxygenase, 3MDO, 3MP dioxygenase, CdoA,
H16_B1863 ,
MDO ,
NP_251292 ,
PA2602 ,
more
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3-mercaptopropionic acid dioxygenase
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3-sulfanylpropanoate dioxygenase
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3MDO
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CdoA
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H16_B1863
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MDO
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NP_251292
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PA2602
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3-sulfanylpropanoate + O2 = 3-sulfinopropanoate
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3-sulfanylpropanoate:oxygen oxidoreductase
This bacterial enzyme contains an iron(2+) atom coordinated by three protein-derived histidines and a Ser-His-Tyr motif. It is similar to EC 1.13.11.20, cysteine dioxygenase, and can act on L-cysteine, but has a much higher activity with its native substrate, 3-sulfanylpropanoate.
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(2R)-2-sulfanylbutanedioic acid + O2
?
3-mercaptopropanoate + O2
3-sulfinopropanoate
3-mercaptopropionate + O2
3-sulfinopropionate
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-
-
?
L-cysteine + O2
3-sulfinoalanine
additional information
?
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(2R)-2-sulfanylbutanedioic acid + O2
?
i.e. (R)-mercaptosuccinate, no substrate for wild-type, but mutant Q62R
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-
?
(2R)-2-sulfanylbutanedioic acid + O2
?
i.e. (R)-mercaptosuccinate, no substrate for wild-type, but mutant Q62R
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-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate
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-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate
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-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate
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-
-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate
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-
-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate
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-
-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate
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-
-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate
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-
-
?
L-cysteine + O2
3-sulfinoalanine
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reaction of EC 1.13.11.20
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-
?
L-cysteine + O2
3-sulfinoalanine
reaction of EC 1.13.11.20
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-
?
L-cysteine + O2
3-sulfinoalanine
reaction of EC 1.13.11.20
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-
?
L-cysteine + O2
3-sulfinoalanine
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reaction of EC 1.13.11.20
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-
?
L-cysteine + O2
3-sulfinoalanine
plus some cysteine sulfinic acid, reaction of EC 1.13.11.20
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-
?
L-cysteine + O2
3-sulfinoalanine
reaction of EC 1.13.11.20
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-
?
L-cysteine + O2
3-sulfinoalanine
plus some cysteine sulfinic acid, reaction of EC 1.13.11.20
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-
?
additional information
?
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enzyme exhibits a specificity for 3-mercaptopropanoate nearly 2 orders of magnitude greater than those for cysteine
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additional information
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enzyme shows only minor cysteine dioxygenase activity
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additional information
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enzyme shows only minor cysteine dioxygenase activity
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additional information
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3-mercaptopropanoate is preferred over cysteine. No substrate: cysteamine
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additional information
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3-mercaptopropanoate is preferred over cysteine. No substrate: cysteamine
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additional information
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3-mercaptopropanoate is preferred over cysteine. No substrate: cysteamine
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additional information
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enzyme shows only minor cysteine dioxygenase activity
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additional information
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recombinant 3MDO is able to oxidize both cysteine and 3-mercaptopropionic acid in vitro, with a marked preference for 3-mercaptopropionic acid. Substrate binding to the ferrous iron is through the thiol but each substrate may adopt different coordination geometries
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additional information
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recombinant 3MDO is able to oxidize both cysteine and 3-mercaptopropionic acid in vitro, with a marked preference for 3-mercaptopropionic acid. Substrate binding to the ferrous iron is through the thiol but each substrate may adopt different coordination geometries
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additional information
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recombinant 3MDO is able to oxidize both cysteine and 3-mercaptopropionic acid in vitro, with a marked preference for 3-mercaptopropionic acid. Substrate binding to the ferrous iron is through the thiol but each substrate may adopt different coordination geometries
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additional information
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no substrates: cysteine and cysteamine
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additional information
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no substrates: cysteine and cysteamine
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3-mercaptopropanoate + O2
3-sulfinopropanoate
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?
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Iron
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iron content is 0.8 mol of iron per mol of MDO. Addition of NO to 3-mercaptopropanoate-bound enzyme quantitatively yields an iron-nitrosyl species with EPR features consistent with a mononuclear (FeNO)7 site
Iron
iron content of 0.38 mol Fe(II) per mol of enzyme
Iron
active site iron is coordinated by 3 histidines and 3 water molecules
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EDTA
0.05 mM, 80% of initial activity, 0.1 mM, 61% of initial activity
ethylxanthate
0.002 mM, 110% of initial activity, 0.004 mM, 89% of initial activity
additional information
addition of cysteine results in a minor decrease of activity
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ethylxanthate
0.002 mM, 110% of initial activity, 0.004 mM, 89% of initial activity
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0.5
(2R)-2-sulfanylbutanedioic acid
mutant Q62R, pH not specified in the publication, temperature not specified in the publication
0.009 - 5.7
3-Mercaptopropanoate
1.4
3-Mercaptopropanoate
wild-type, TRIS buffer pH 8.5, 37ưC
0.9
3-Mercaptopropanoate
-
mutant G95C, PIPES buffer pH 6.5, 37ưC
0.9
3-Mercaptopropanoate
mutant Q62R, pH not specified in the publication, temperature not specified in the publication
0.9
3-Mercaptopropanoate
wild-type, PIPES buffer pH 6.1, 37ưC
1
3-Mercaptopropanoate
pH 7.5, 37ưC
1
3-Mercaptopropanoate
wild-type, PIPES buffer pH 6.5, 37ưC
0.9
3-Mercaptopropanoate
mutant G95C, PIPES buffer pH 6.5, 37ưC
1.4
3-Mercaptopropanoate
-
wild-type, TRIS buffer pH 8.5, 37ưC
4
3-Mercaptopropanoate
wild-type, acetate buffer pH 4.7, 37ưC
5
3-Mercaptopropanoate
wild-type, acetate buffer pH 5.5, 37ưC
5.7
3-Mercaptopropanoate
pH 6.5, 30ưC
0.009
3-Mercaptopropanoate
-
mutant Y159F, 37ưC, pH not specified in the publication
0.8
3-Mercaptopropanoate
wild-type, PIPES buffer pH 7.5, 37ưC
0.8
3-Mercaptopropanoate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.7
3-Mercaptopropanoate
wild-type, TRIS buffer pH 8.0, 37ưC
0.7
3-Mercaptopropanoate
pH not specified in the publication, temperature not specified in the publication
0.6
3-Mercaptopropanoate
wild-type, TRIS buffer pH 7.5, 37ưC
0.5
3-Mercaptopropanoate
wild-type, PIPES buffer pH 7.0, 37ưC
0.013
3-Mercaptopropanoate
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wild-type, 20ưC, pH not specified in the publication
0.013
3-Mercaptopropanoate
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pH 8.0, 25ưC
0.012
3-Mercaptopropanoate
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mutant H157N, 37ưC, pH not specified in the publication
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0.02
(2R)-2-sulfanylbutanedioic acid
mutant Q62R, pH not specified in the publication, temperature not specified in the publication
0.007 - 0.94
3-Mercaptopropanoate
0.28
3-Mercaptopropanoate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.13
3-Mercaptopropanoate
wild-type, PIPES buffer pH 7.0, 37ưC
0.19
3-Mercaptopropanoate
wild-type, PIPES buffer pH 6.5, 37ưC
0.22
3-Mercaptopropanoate
wild-type, acetate buffer pH 5.5, 37ưC
0.23
3-Mercaptopropanoate
wild-type, PIPES buffer pH 6.1, 37ưC
0.11
3-Mercaptopropanoate
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wild-type, acetate buffer pH 4.7, 37ưC
0.35
3-Mercaptopropanoate
pH not specified in the publication, temperature not specified in the publication
0.45
3-Mercaptopropanoate
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wild-type, 20ưC, pH not specified in the publication
0.67
3-Mercaptopropanoate
mutant Q62R, pH not specified in the publication, temperature not specified in the publication
0.82
3-Mercaptopropanoate
pH 6.5, 30ưC
0.94
3-Mercaptopropanoate
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pH 8.0, 25ưC
0.007
3-Mercaptopropanoate
mutant G95C, PIPES buffer pH 6.5, 37ưC
0.11
3-Mercaptopropanoate
wild-type, acetate buffer pH 4.7, 37ưC
0.11
3-Mercaptopropanoate
pH 7.5, 37ưC
0.1
3-Mercaptopropanoate
wild-type, TRIS buffer pH 7.5, 37ưC
0.1
3-Mercaptopropanoate
wild-type, PIPES buffer pH 7.5, 37ưC
0.092
3-Mercaptopropanoate
-
mutant H157N, 37ưC, pH not specified in the publication
0.081
3-Mercaptopropanoate
-
mutant Y159F, 37ưC, pH not specified in the publication
0.05
3-Mercaptopropanoate
wild-type, TRIS buffer pH 8.0, 37ưC
0.03
3-Mercaptopropanoate
wild-type, TRIS buffer pH 8.5, 37ưC
0.007
3-Mercaptopropanoate
-
mutant G95C, PIPES buffer pH 6.5, 37ưC
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0.04
(2R)-2-sulfanylbutanedioic acid
mutant Q62R, pH not specified in the publication, temperature not specified in the publication
0.03 - 110
3-Mercaptopropanoate
0.26
3-Mercaptopropanoate
-
wild-type, PIPES buffer pH 6.1, 37ưC
110
3-Mercaptopropanoate
pH 7.5, 37ưC
72
3-Mercaptopropanoate
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pH 8.0, 25ưC
27
3-Mercaptopropanoate
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wild-type, 20ưC, pH not specified in the publication
9
3-Mercaptopropanoate
-
mutant Y159F, 37ưC, pH not specified in the publication
7.8
3-Mercaptopropanoate
-
mutant H157N, 37ưC, pH not specified in the publication
0.74
3-Mercaptopropanoate
mutant Q62R, pH not specified in the publication, temperature not specified in the publication
0.7
3-Mercaptopropanoate
wild-type, TRIS buffer pH 8.0, 37ưC
0.5
3-Mercaptopropanoate
pH not specified in the publication, temperature not specified in the publication
0.35
3-Mercaptopropanoate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.27
3-Mercaptopropanoate
wild-type, PIPES buffer pH 7.0, 37ưC
0.03
3-Mercaptopropanoate
wild-type, acetate buffer pH 4.7, 37ưC
0.26
3-Mercaptopropanoate
wild-type, PIPES buffer pH 6.1, 37ưC
0.2
3-Mercaptopropanoate
wild-type, PIPES buffer pH 6.5, 37ưC
0.18
3-Mercaptopropanoate
wild-type, TRIS buffer pH 8.5, 37ưC
0.18
3-Mercaptopropanoate
wild-type, TRIS buffer pH 7.5, 37ưC
0.144
3-Mercaptopropanoate
pH 6.5, 30ưC
0.12
3-Mercaptopropanoate
wild-type, PIPES buffer pH 7.5, 37ưC
0.05
3-Mercaptopropanoate
wild-type, acetate buffer pH 5.5, 37ưC
0.03
3-Mercaptopropanoate
-
wild-type, acetate buffer pH 4.7, 37ưC
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additional information
the monoprotonated ES complexes with 3-mercaptopropionic acid and cysteine have different pKs. At higher pH, kcat decreases sigmoidally with a similar pK regardless of substrate. Loss of reactivity at high pH is attributed to deprotonation of tyrosine 159 and its influence on dioxygen binding
additional information
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the monoprotonated ES complexes with 3-mercaptopropionic acid and cysteine have different pKs. At higher pH, kcat decreases sigmoidally with a similar pK regardless of substrate. Loss of reactivity at high pH is attributed to deprotonation of tyrosine 159 and its influence on dioxygen binding
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5.8
calculated from sequence
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brenda
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UniProt
brenda
cf. EC 1.13.11.91
UniProt
brenda
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UniProt
brenda
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UniProt
brenda
cf. EC 1.13.11.91
UniProt
brenda
-
UniProt
brenda
cf. EC 1.13.11.91
UniProt
brenda
-
UniProt
brenda
cf. EC 1.13.11.91
UniProt
brenda
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physiological function
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a network of hydrogen bonds connects residues H157-Y159 and Fe-bound ligands within the enzymatic Fe site. The hydroxyl group of Y159 hydrogen bonds to Fe-bound NO and, by extension, Fe-bound oxygen during native catalysis. This interaction alters both the NO binding affinity and rhombicity of the 3-mercaptopropanoate-bound iron-nitrosyl site
physiological function
mutants are impaired in growth on 3,3-thiodipropionic acid
physiological function
the monoprotonated ES complexes with 3-mercaptopropionic acid and cysteine have different pKs. At higher pH, kcat decreases sigmoidally with a similar pK regardless of substrate. Loss of reactivity at high pH is attributed to deprotonation of tyrosine 159 and its influence on dioxygen binding. A mechanism model shows deprotonation of tyrosine 159 both blocks oxygen binding and concomitantly promotes cystine formation
physiological function
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the pL-dependent activity of MDO can be rationalized assuming a diprotic enzyme model in which three ionic forms of the enzyme are present [cationic, E(z+1), neutral, Ez, and anionic, E(z-1)]. The activities observed for substrates 3-mercaptopropanoate and cysteine appear to be dominated by electrostatic interactions within the enzymatic active site
physiological function
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the monoprotonated ES complexes with 3-mercaptopropionic acid and cysteine have different pKs. At higher pH, kcat decreases sigmoidally with a similar pK regardless of substrate. Loss of reactivity at high pH is attributed to deprotonation of tyrosine 159 and its influence on dioxygen binding. A mechanism model shows deprotonation of tyrosine 159 both blocks oxygen binding and concomitantly promotes cystine formation
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3MDO_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
201
0
22548
Swiss-Prot
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B9U5L8_VARPD
195
0
21607
TrEMBL
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Q0K029_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
205
0
22587
TrEMBL
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?
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x * 22696, calculated from sequence, x * 23000, SDS-PAGE
?
x * 23746, calculated from sequence
?
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x * 23746, calculated from sequence
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dimer
2 * 22580, calculated from sequence
dimer
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2 * 22580, calculated from sequence
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dimer
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2 * 22580, calculated from sequence
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no modification
no posttranslational modification observed
no modification
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no posttranslational modification observed
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comparison with mammalian cysteine dioxygenase. The overall active site geometry is conserved but the different substrate specificity may be related to replacement of an arginine by a glutamine in the active site
structure of variant G95C
structural comparison with cysteine dioxygenase homologs that conserve an active site Gln residue, cf. EC 1.13.11.20
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H157N
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over 3fold reduction in kcat/Km value
Y159F
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3fold reduction in kcat/Km value. Fe coordination of cysteine is switched from thiolate only to bidentate (thiolate/amine) for the variant
G95C
variant is able to form a cysteine-tyrosine crosslink homologous to that found in mammalian cysteine dioxygenases. Activity of this variant is severely impaired
Q62R
variant retains both 3-mercaptopropanoate and cysteine dioxygenase activity
R168A
variant does not fold properly
R168C
variant does not fold properly
G95C
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variant is able to form a cysteine-tyrosine crosslink homologous to that found in mammalian cysteine dioxygenases. Activity of this variant is severely impaired
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Q62R
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variant retains both 3-mercaptopropanoate and cysteine dioxygenase activity
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R168A
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variant does not fold properly
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R168C
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variant does not fold properly
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expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
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low expression under standard growth conditions
low expression under standard growth conditions
low expression under standard growth conditions
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-
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Wenning, L.; Stoeveken, N.; Wuebbeler, J.H.; Steinbuechel, A.
Substrate and cofactor range differences of two cysteine dioxygenases from Ralstonia eutropha H16
Appl. Environ. Microbiol.
82
910-921
2015
Cupriavidus necator (Q0K029), Cupriavidus necator DSM 428 (Q0K029)
brenda
Driggers, C.M.; Hartman, S.J.; Karplus, P.A.
Structures of Arg- and Gln-type bacterial cysteine dioxygenase homologs
Protein Sci.
24
154-161
2015
Variovorax paradoxus (B9U5L8)
brenda
Crowell, J.K.; Sardar, S.; Hossain, M.S.; Foss, F.W.; Pierce, B.S.
Non-chemical proton-dependent steps prior to O2-activation limit Azotobacter vinelandii 3-mercaptopropionic acid dioxygenase (MDO) catalysis
Arch. Biochem. Biophys.
604
86-94
2016
Azotobacter vinelandii
brenda
Pierce, B.S.; Subedi, B.P.; Sardar, S.; Crowell, J.K.
The ''Gln-Type'' thiol dioxygenase from Azotobacter vinelandii is a 3-mercaptopropionic acid dioxygenase
Biochemistry
54
7477-7490
2015
Azotobacter vinelandii
brenda
Fellner, M.; Aloi, S.; Tchesnokov, E.P.; Wilbanks, S.M.; Jameson, G.N.
Substrate and pH-dependent kinetic profile of 3-mercaptopropionate dioxygenase from Pseudomonas aeruginosa
Biochemistry
55
1362-1371
2016
Pseudomonas aeruginosa (Q9I0N5), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (Q9I0N5)
brenda
Aloi, S.; Davies, C.G.; Karplus, P.A.; Wilbanks, S.M.; Jameson, G.N.L.
Substrate specificity in thiol dioxygenases
Biochemistry
58
2398-2407
2019
Cupriavidus necator (Q9I0N5), Cupriavidus necator, Cupriavidus necator JMP 134 (Q9I0N5), Pseudomonas aeruginosa (Q9I0N5), Pseudomonas aeruginosa DSM 22644 (Q9I0N5)
brenda
Sardar, S.; Weitz, A.; Hendrich, M.P.; Pierce, B.S.
Outer-sphere tyrosine 159 within the 3-mercaptopropionic acid dioxygenase S-H-Y motif gates substrate-coordination denticity at the non-heme iron active site
Biochemistry
58
5135-5150
2019
Azotobacter vinelandii
brenda
Bruland, N.; Wuebbeler, J.H.; Steinbuechel, A.
3-Mercaptopropionate dioxygenase, a cysteine dioxygenase homologue, catalyzes the initial step of 3-mercaptopropionate catabolism in the 3,3-thiodipropionic acid-degrading bacterium variovorax paradoxus
J. Biol. Chem.
284
660-672
2009
Variovorax paradoxus (B9U5L8), Variovorax paradoxus
brenda
Tchesnokov, E.P.; Fellner, M.; Siakkou, E.; Kleffmann, T.; Martin, L.W.; Aloi, S.; Lamont, I.L.; Wilbanks, S.M.; Jameson, G.N.
The cysteine dioxygenase homologue from Pseudomonas aeruginosa is a 3-mercaptopropionate dioxygenase
J. Biol. Chem.
290
24424-24437
2015
Pseudomonas aeruginosa (Q9I0N5), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (Q9I0N5)
brenda
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