3.5.1.9: arylformamidase

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

Reaction

Synonyms

AFMID, Bna7p, FKF, formamidase I, formamidase II, formyl kynurenine formamidase, formylase, formylkynureninase, formylkynurenine formamidase, KFA, KFase, KynB, kynurenine formamidase, kynurine formamidase

ECTree

     3 Hydrolases

         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

             3.5.1 In linear amides

                3.5.1.9 arylformamidase

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Results	in table
15	Activating Compound
5226	AA Sequence
4	Application
1	CAS Registry Number
10	Cloned(Commentary)
1	Cofactor
4	Crystallization (Commentary)
3	Expression
23	General Information
4	General Stability
166	Inhibitors
4	kcat/KM [mM/s]
11	Ki Value [mM]
38	KM Value [mM]
7	Localization
11	Metals/Ions
53	Molecular Weight [Da]
73	Natural Substrates/ Products (Substrates)
71	Organism
12	Pathway
18	PDB ID
23	pH Optimum
5	pH Range
2	pH Stability
1	pI Value
4	Protein Variants
25	Purification (Commentary)
6	Reaction
1	Reaction Type
67	Reference
55	Source Tissue
27	Specific Activity [micromol/min/mg]
4	Storage Stability
105	Substrates and Products (Substrate)
7	Subunits
40	Synonyms
1	Systematic Name
10	Temperature Optimum [°C]
1	Temperature Range [°C]
7	Temperature Stability [°C]
5	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.5.1.9 - arylformamidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

purified detagged recombinant enzyme, hanging drop vapour diffusion method, mixing of 4.0 mg/ml protein in 20 mM Tris-HCl, pH 7.4, and 200 mM NaCl, and 8 mM kynurenine, in a 1.1 ratio with reservoir solution containing 100 mM Tris-HCl, pH 8.5, 150 mM MgCl2, 30% w/v PEG 4000 and 1.5% v/v dioxane, final volume 0.002-0.004 ml, 20°C, 5 days, X-ray diffraction structure determination and analysis at 1.95 A resolution

Bacillus anthracis

Q81PP9

733300

purified detagged recombinant enzyme, sitting drop vapour diffusion method, mixing of 7.5 mg/ml protein in 25 mM Tris-HCl, pH 7.5, and 100 mM NaCl, and kynurenine, in a 1.1 ratio with reservoir solution containing 10-16% w/v PEG 3350, 5 mM CoCl2, 5 mM CdCl2, 5 mM MgCl2 and 5 mM NiCl2, final volume 0.002-0.004 ml, 5 days at room temperature, X-ray diffraction structure determination and analysis at 1.60 A resolution

Burkholderia cenocepacia

B4E9I9

733300

enzyme in complex with inhibitor PMSF, X-ray diffraction structure determination and analysis, molecular replacement using structure PDB ID 2PBL

Drosophila melanogaster

Q9VMC9

733287

purified detagged recombinant enzyme, sitting drop vapour diffusion method, mixing of 7.5 mg/ml protein in 25 mM Tris-HCl, pH 7.5, and 100 mM NaCl, and kynurenine, in a 1.1 ratio with reservoir solution containing 0.1M HEPES, pH 7.5, 20% w/v PEG 4000 and 10% v/v propan-2-ol, final volume 0.002-0.004 ml, 5 days at room temperature, X-ray diffraction structure determination and analysis at 2.37 A resolution, molecular replacement

Pseudomonas aeruginosa

Q9I234

733300