Literature summary for 1.14.14.18 extracted from

Bianchetti, C.M.; Yi, L.; Ragsdale, S.W.; Phillips, G.N.
Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2 (2007), J. Biol. Chem., 282, 37624-37631.

Search for more literature for 1.14.14.18

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of GST-tagged wild-type and mutant HO-2 in Escherichia coli strain BL21(DE3)	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
apo- and heme-bound truncated HO-2, lacking the three heme regulatory motifs and the membrane binding region, apo-HO-2: hanging drop method, 0.0015 ml of 5 mg/ml protein in 50 mM KCl, 50 mM Tris-HCl, pH 7.5, are mixed with 0.001 ml of well solution containing 40% PEG 1500, 200 mM potassium glutamate, and 100 mM triethanolamine, pH 8.5, at 4°C, heme-bound HO-2: hanging drop vapour diffusion method, 0.0015 ml of 5 mg/ml protein in 50 mM KCl, 50 mM Tris-HCl, pH 7.5, are mixed with 0.001 ml of well solution containing 33% PEG dimethlyether 500, 20 mM MgCl2, and 100 mM HEPES, pH 8.5, at 4°C, X-ray diffraction structure determination and analysis at 2.4 A resolution for the apoenzyme, and at 2.6 A resolution for the heme-bound enzyme	Homo sapiens

Crystallization (Comment)

Organism

apo- and heme-bound truncated HO-2, lacking the three heme regulatory motifs and the membrane binding region, apo-HO-2: hanging drop method, 0.0015 ml of 5 mg/ml protein in 50 mM KCl, 50 mM Tris-HCl, pH 7.5, are mixed with 0.001 ml of well solution containing 40% PEG 1500, 200 mM potassium glutamate, and 100 mM triethanolamine, pH 8.5, at 4°C, heme-bound HO-2: hanging drop vapour diffusion method, 0.0015 ml of 5 mg/ml protein in 50 mM KCl, 50 mM Tris-HCl, pH 7.5, are mixed with 0.001 ml of well solution containing 33% PEG dimethlyether 500, 20 mM MgCl2, and 100 mM HEPES, pH 8.5, at 4°C, X-ray diffraction structure determination and analysis at 2.4 A resolution for the apoenzyme, and at 2.6 A resolution for the heme-bound enzyme

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of apo- and heme-bound truncated HO-2, lacking the three heme regulatory motifs and the membrane binding region	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
heme + AH2 + O2	Homo sapiens	first step in the heme degradation pathway	biliverdin + Fe2+ + CO + A + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P30519	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant GST-tagged wild-type and mutant HO-2 from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
heme + AH2 + O2	first step in the heme degradation pathway	Homo sapiens	biliverdin + Fe2+ + CO + A + H2O	-	?
heme + AH2 + O2	proper orientation of heme in HO-2 is required for the regioselective oxidation of the alpha-mesocarbon. This is accomplished by interactions within the heme binding pocket, which is made up of two helices. The iron coordinating residue, His45, resides on the proximal helix. The distal helix contains highly conserved glycine residues that allow the helix to flex and interact with the bound heme. Tyr154, Lys199, and Arg203 orient the heme through direct interactions with the heme propionates, overview	Homo sapiens	biliverdin + Fe2+ + CO + A + H2O	-	?
additional information	structure-function analysis	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
More	structure-function analysis	Homo sapiens

Synonyms

Synonyms	Comment	Organism
heme oxygenase-2	-	Homo sapiens
HO-2	-	Homo sapiens