1.14.13.1: salicylate 1-monooxygenase

This is an abbreviated version!
For detailed information about salicylate 1-monooxygenase, go to the full flat file.

Reaction

Synonyms

Efe-shyA, FAD/NADH-dependent SA 1-hydroxylase, FAD_binding_3 domain-containing protein, FGSG_03657, FgShy1, FgShyC, flavin-dependent monooxygenase salicylate hydroxylase, NahG, NahU, NRRL3_9723, oxygenase, salicylate 1-mono-, SA 1-decarboxylase/hydroxylase, SA 1-hydroxylase, SA hydroxylase, SA1H, SahA, salA, salcylic acid 1-hydroxylase, SALH, salicylate 1-hydroxylase, Salicylate 1-monooxygenase, salicylate hydroxylase, salicylate hydroxylase (decarboxylating), salicylate monooxygenase, salicylate, NADH: oxygen oxidoreductase, salicylate, NADH: oxygen oxidoreductase (1-hydroxylating, decarboxylating), salicylate-1-hydroxylase, salicylic acid hydroxylase, salicylic hydroxylase, SalOH, SHL, Shy1, ShyA, ShyC, SlSA 1H, SlSA1H, Solyc08g063130

ECTree

     1 Oxidoreductases

         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor

                1.14.13.1 salicylate 1-monooxygenase

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Results	in table
3	Activating Compound
1317	AA Sequence
5	Application
1	CAS Registry Number
16	Cloned(Commentary)
80	Cofactor
4	Crystallization (Commentary)
16	Expression
44	General Information
3	General Stability
22	Inhibitors
10	kcat/KM [mM/s]
4	Ki Value [mM]
62	KM Value [mM]
4	Localization
3	Metals/Ions
14	Molecular Weight [Da]
36	Natural Substrates/ Products (Substrates)
114	Organism
10	Pathway
10	PDB ID
12	pH Optimum
5	pH Range
1	pH Stability
17	Protein Variants
18	Purification (Commentary)
5	Reaction
4	Reaction Type
84	Reference
20	Source Tissue
37	Specific Activity [micromol/min/mg]
3	Storage Stability
226	Substrates and Products (Substrate)
18	Subunits
152	Synonyms
1	Systematic Name
11	Temperature Optimum [°C]
2	Temperature Range [°C]
5	Temperature Stability [°C]
10	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.14.13.1 - salicylate 1-monooxygenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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Pseudomonas putida

-

389998

apoenzyme is crystallized by dialysis method, using ammonium sulfate as the precipitant

Pseudomonas putida

-

390014

complexed with FAD, sitting drop vapor diffusion method, using 1.26 M ammonium sulfate, 200 mM lithium sulfate and 100 mM Tris-HCl buffer at pH 8.5

Pseudomonas putida

-

741825

purified recombinant detagged apoform of NahG, hanging drop vapor diffusion method, crystallization from reservoir solution containing 1.5 M ammonium sulfate, 0.1 M Tris, pH 8.5, and 12% v/v glycerol, method optimization, 18°C, cryoprotectant solution is formed by the reservoir solution supplemented with 10% v/v ethylene glycol, and 0.06 M sodium iodide, X-ray diffraction structure determination and analysis at 2.0 A resolution, structure modeling using the structure with PDB ID 6BZ5 as a template

Pseudomonas putida

Q8RMN4

764872