Literature summary for 1.13.11.41 extracted from

Keegan, R.; Lebedev, A.; Erskine, P.; Guo, J.; Wood, S.P.; Hopper, D.J.; Rigby, S.E.; Cooper, J.B.
Structure of the 2,4'-dihydroxyacetophenone dioxygenase from Alcaligenes sp. 4HAP (2014), Acta Crystallogr. Sect. D, 70, 2444-2454 .

Search for more literature for 1.13.11.41

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)	Alcaligenes sp.

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant His-tagged chymotrypsinolysed enzyme, 5 mg/ml protein in 50 mM Tris, pH 7.5, 100 mM NaCl, 1 mM 2-mercaptoethanol is mixed with a solution containing 10% w/v PEG 1000 and 10% PEG 8000, X-ray diffraction structure determination and analysis at 2.2 A resolution. The use of limited chymotrypsinolysis, which apparently results in removal of the first 20 or so N-terminal residues of DAD, is necessary for crystallization of the protein	Alcaligenes sp.

Crystallization (Comment)

Organism

purified recombinant His-tagged chymotrypsinolysed enzyme, 5 mg/ml protein in 50 mM Tris, pH 7.5, 100 mM NaCl, 1 mM 2-mercaptoethanol is mixed with a solution containing 10% w/v PEG 1000 and 10% PEG 8000, X-ray diffraction structure determination and analysis at 2.2 A resolution. The use of limited chymotrypsinolysis, which apparently results in removal of the first 20 or so N-terminal residues of DAD, is necessary for crystallization of the protein

Alcaligenes sp.

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	one non-heme iron per enzyme subunit. The catalytic iron is coordinated by three histidine residues, H76, H78 and H114 in strands II and VII, within a buried active-site cavity, and an additional ligand	Alcaligenes sp.

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2,4'-dihydroxyacetophenone + O2	Alcaligenes sp.	-	4-hydroxybenzoate + formate	-	?
additional information	Alcaligenes sp.	enzyme DAD is very unusual in that it is involved in C-C bond cleavage in a substituent of the aromatic ring instead of cleaving within the aromatic ring of the substrate	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Alcaligenes sp.	Q9REI7	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	Alcaligenes sp.

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
2,4'-dihydroxyacetophenone + O2	-	Alcaligenes sp.	4-hydroxybenzoate + formate	-	?
additional information	enzyme DAD is very unusual in that it is involved in C-C bond cleavage in a substituent of the aromatic ring instead of cleaving within the aromatic ring of the substrate	Alcaligenes sp.	?	-	?
additional information	modeling of substrate binding in the active site, overview	Alcaligenes sp.	?	-	?

Subunits

Subunits	Comment	Organism
More	enzyme tertiary and quarternary structure analysis	Alcaligenes sp.
tetramer	4 * 20300, recombinant wild-type enzyme, SDS-PAGE	Alcaligenes sp.

Synonyms

Synonyms	Comment	Organism
DAD	-	Alcaligenes sp.

General Information

General Information	Comment	Organism
additional information	active site structure and substrate binding structure, modeling, overview	Alcaligenes sp.