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Literature summary for 1.13.11.20 extracted from

  • Arjune, S.; Schwarz, G.; Belaidi, A.A.
    Involvement of the Cys-Tyr cofactor on iron binding in the active site of human cysteine dioxygenase (2015), Amino Acids, 47, 55-63 .
    View publication on PubMed
Search for more literature for 1.13.11.20

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
C93A site-directed mutagenesis, CDO activity of the C93A variant increases with a much lower rate of iron supplementation and consequently a much higher concentration is required to approximate saturation, it has a 18fold higher Kd value Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
2-oxoglutarate
-
 Homo sapiens
EDTA enzyme activity is completely abolished at EDTA concentrations above 0.5 mM Homo sapiens
Glutarate
-
 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten steady-state kinetics of wild-type and mutant enzymes, impact of the Cys-Tyr cofactor on kinetic properties, overview Homo sapiens
0.77
-
 L-cysteine pH 6.1, 37°C, recombinant wild-type enzyme Homo sapiens
3.1
-
 L-cysteine pH 6.1, 37°C, recombinant wild-type enzyme, under iron saturation Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-cysteine + O2 Homo sapiens
-
 3-sulfinoalanine
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q16878
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information a unique post-translational modification of human CDO consisting of a cross-link between cysteine 93 and tyrosine 157 (Cys-Tyr), which increases catalytic efficiency in a substrate-dependent manner Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-cysteine + O2
-
 Homo sapiens 3-sulfinoalanine
-
 ?

Synonyms

Synonyms Comment Organism
CDO
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
10.35
-
 L-cysteine pH 6.1, 37°C, recombinnat wild-type enzyme Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1
-
 assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
Cys-Tyr cofactor a unique post-translational modification of human CDO consisting of a cross-link between cysteine 93 and tyrosine 157 (Cys-Tyr), which increases catalytic efficiency in a substrate-dependent manner. Production of a Cys-Tyr cofactor-saturated enzyme and analysis of the Cys-Tyr cofactor on kinetic properties, overview. The Cys-Tyr cofactor strongly contributes to efficient iron coordination in the active center of CDO Homo sapiens