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Literature summary for 1.13.11.20 extracted from

  • Pietra, F.
    On the dynamical behavior of the cysteine dioxygenase-L-cysteine complex in the presence of free dioxygen and L-cysteine (2017), Chem. Biodivers., 14, e1700290 .
    View publication on PubMed
Search for more literature for 1.13.11.20

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required, enzyme-bound. The iron ion is coordinated by H86, H88, H140 and a water molecule, and can further accept a coordinating L-cysteine molecule Rattus norvegicus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P21816
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Rattus norvegicus
-
kidney
-
 Rattus norvegicus
-
liver mainly Rattus norvegicus
-
lung
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-cysteine + O2
-
 Rattus norvegicus 3-sulfinoalanine
-
 ?
L-cysteine + O2 enzyme CDO-L-cysteine complex structure analysis and modeling, O2 binding structure, QM-MM simulations, detailed overview Rattus norvegicus 3-sulfinoalanine
-
 ?

Synonyms

Synonyms Comment Organism
CDO
-
 Rattus norvegicus

General Information

General Information Comment Organism
additional information structure modeling of cysteine dioxygenase in complex with L-cysteine dianion Rattus norvegicus
additional information the structure of CDO, which is highly conserved across multiple species, is built on a small alpha-helical domain containing three alpha-helices at the N-terminus, followed by 13 beta-strands. These are subdivided into a main beta-sandwich domain and two beta-hairpins at the C terminus. The entire beta-sandwich is composed of seven anti-parallel beta-strands on the lower side and six anti-parallel beta-strands on the upper side. The active site comprises an iron ion, which is located in the central portion of the cupin beta-sandwhich, and is connected to the bulk solvent through a solvent-filled channel Rattus norvegicus
physiological function in the ferrous form, CDO catalyzes irreversibly the conversion of cysteine to cysteine sulfinate, incorporating both atoms of dioxygen into the product. Cysteine sulfinate is an intermediate of several pathways related to pyruvate and sulfurated metabolites, such as sulfate, taurine, and hypotaurine. The CDO performance increases in response to high cysteine levels,either through the formation of a C93-Y157 crosslink, or a diminished degradation by the ubiquitin-proteasome system Rattus norvegicus