1.13.11.19: cysteamine dioxygenase

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

Reaction

Synonyms

2-aminoethanethiol dioxygenase, ADO, CDO, cysteamine oxygenase, Gm237, oxygenase, cysteamine, oxygenase, cysteamine di-, persulfurase

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

                1.13.11.19 cysteamine dioxygenase

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Results	in table
19	Activating Compound
23	AA Sequence
1	Application
1	CAS Registry Number
2	Cloned(Commentary)
2	Crystallization (Commentary)
3	Disease/ Diagnostics
4	Expression
10	General Information
1	General Stability
23	Inhibitors
3	Ki Value [mM]
8	KM Value [mM]
3	Localization
10	Metals/Ions
7	Molecular Weight [Da]
16	Natural Substrates/ Products (Substrates)
39	Organism
3	Pathway
5	PDB ID
2	pH Optimum
1	Posttranslational Modification
3	Protein Variants
4	Purification (Commentary)
1	Reaction
3	Reaction Type
39	Reference
104	Source Tissue
8	Specific Activity [micromol/min/mg]
5	Storage Stability
64	Substrates and Products (Substrate)
3	Subunits
17	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]

Crystallization

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Crystallization on EC 1.13.11.19 - cysteamine dioxygenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

structure of human ADO at a resolution of 1.78 A with a nickel-bound metal center. Crystallization is achieved through both metal substitution and C18S/C239S double mutations. The metal center resides in a tunnel close to an entry site flanked by loops. ADO appears to use extensive flexibility to handle substrates of different sizes, and also employs proline and proline pairs to maintain the core protein structure and to retain the residues critical for catalysis in place

Homo sapiens

Q96SZ5

765083

structure of cysteamine dioxygenase at 1.9 A resolution, an Fe and three-histidine (3-His) active site is situated at the end of a wide substrate access channel. Whole-protein models of ADO in complex with either cysteamine or an N-terminal-Cys peptide suggest occlusion of access to the active site by peptide substrate binding. A small tunnel that leads from the opposite face of the enzyme into the active site provides a path through which co-substrate O2 can access the Fe center. The entrance to the tunnel is guarded by two Cys residues that may form a disulfide bond to regulate O2 delivery

Mus musculus

Q6PDY2

764185