1.14.14.92: benzoate 4-monooxygenase

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

Reaction

Synonyms

An09g03500, benzoate 1,2-dioxygenase, benzoate 4-hydroxylase, benzoate para-hydroxylase, benzoate-4-hydroxylase, benzoate-p-hydroxylase, benzoic 4-hydroxylase, benzoic acid 4-hydroxylase, BphA, Cyp1, CYP53A15, CYP53B1, EC 1.14.13.12, hydroxylase, benzoate 4-, More, oxygenase, benzoate 4-mono-

ECTree

     1 Oxidoreductases

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

             1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor

                1.14.14.92 benzoate 4-monooxygenase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
5	Activating Compound
38	AA Sequence
2	Application
1	CAS Registry Number
6	Cloned(Commentary)
5	Cofactor
1	Crystallization (Commentary)
1	Expression
2	General Information
5	General Stability
43	Inhibitors
3	Ki Value [mM]
16	KM Value [mM]
3	Localization
4	Metals/Ions
2	Molecular Weight [Da]
6	Natural Substrates/ Products (Substrates)
25	Organism
4	Pathway
4	pH Optimum
2	pH Range
1	pH Stability
4	Purification (Commentary)
1	Reaction
3	Reaction Type
22	Reference
3	Source Tissue
5	Specific Activity [micromol/min/mg]
3	Storage Stability
38	Substrates and Products (Substrate)
1	Subunits
20	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
1	Temperature Range [°C]
17	Turnover Number [1/s]

Crystallization

print visible entries

print all entries

Crystallization on EC 1.14.14.92 - benzoate 4-monooxygenase

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

top print hide Go to Crystallization (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

molecular docking and 3D simulation of inhibition. Reaction mechanism assumes that the enzyme is membrane-bound and suggests that the hydrophobic ligands enter the active site through a channel, that is surrounded by numerous nonpolar residues including four prolines and is adjacent to the membrane-anchoring N-terminus

Curvularia lunata

B8QM33

725603