1.13.11.6: 3-hydroxyanthranilate 3,4-dioxygenase

This is an abbreviated version!
For detailed information about 3-hydroxyanthranilate 3,4-dioxygenase, go to the full flat file.

Word Map on EC 1.13.11.6

1.13.11.6

quinolinic

kynureninase

quin

2,3-dioxygenase

3-monooxygenase

excitotoxin

phosphoribosyltransferase

kynurenine-oxoglutarate

aminocarboxymuconate-semialdehyde

kynurenic

3-hydroxykynurenine

ibotenic

epilepsy-prone

picolinic

drug development

medicine

pharmacology

Reaction

Synonyms

3-HAD, 3-HAO, 3-hydroxyanthranilate 3,4-dioxygenase, 3-hydroxyanthranilate oxygenase, 3-hydroxyanthranilic acid oxidase, 3-hydroxyanthranilic acid oxygenase, 3-hydroxyanthranilic oxygenase, 3HAO, EC 1.13.1.6, HAD, HAO, oxygenase, 3-hydroxyanthranilate 3,4-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

1.13.11.6 3-hydroxyanthranilate 3,4-dioxygenase

Advanced search results

Do not include text mining results

Include

results (more...)

Include

results (more...)

Results	in table
1	Activating Compound
5583	AA Sequence
4	Application
1	CAS Registry Number
8	Cloned(Commentary)
1	Cofactor
6	Crystallization (Commentary)
24	Disease/ Diagnostics
8	General Information
2	General Stability
35	Inhibitors
8	Ki Value [mM]
18	KM Value [mM]
3	Localization
20	Metals/Ions
15	Molecular Weight [Da]
14	Natural Substrates/ Products (Substrates)
2	Organic Solvent Stability
213	Organism
8	Pathway
39	PDB ID
6	pH Optimum
4	pH Range
2	pH Stability
2	pI Value
18	Protein Variants
13	Purification (Commentary)
4	Reaction
3	Reaction Type
36	Reference
20	Source Tissue
12	Specific Activity [micromol/min/mg]
8	Storage Stability
44	Substrates and Products (Substrate)
6	Subunits
22	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
2	Temperature Range [°C]
1	Temperature Stability [°C]
5	Turnover Number [1/s]

Metals Ions

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Metals Ions on EC 1.13.11.6 - 3-hydroxyanthranilate 3,4-dioxygenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide

Go to Metals and Ions Search

(NH4)2SO4

Bos taurus

the most effective salt, the optimal concentration is 0.035 M

439364

Cupriavidus metallidurans

each monomer contains two iron binding sites. The catalytic iron is buried deep inside the beta-barrel with His51, Glu57, and His95 serving as ligands. The other iron site forms an FeS4 center close to the solvent surface in which the sulfur atoms are provided by Cys125, Cys128, Cys162, and Cys165. The two iron sites are separated by 24 A

672037

Fe2+

10 entries

Fe3+

Bos taurus

does not seem to bind to the enzyme

439365

HCl

Bos taurus

during purification of enzyme treatment with acid was used

Iron

MgCl2

NaCl

Ni2+

Saccharomyces cerevisiae

two nickel binding sites per molecule. One of the bound nickel atoms occupies the proposed ferrous-coordinated active site

677020

additional information

2 entries