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Literature summary extracted from

  • Hu, Y.; Jiang, F.; Guo, Y.; Shen, X.; Zhang, Y.; Zhang, R.; Guo, G.; Mao, X.; Zou, Q.; Wang, D.C.
    Crystal structure of HugZ, a novel heme oxygenase from Helicobacter pylori (2011), J. Biol. Chem., 286, 1537-1544.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.18 expression of His6-tagged HugZ in Escherichia coli strain BL21(DE3) Helicobacter pylori

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.14.18 purified recombinant HugZ, hanging-drop vapour diffusion method, mixing of 0.001 ml of 25 mg/ml HugZ-hemin in 20 mM Tris, pH 8.0, 5 mM sodium azide, with 0.001 ml of reservoir solution consisting of 16% w/v PEG 3350, 3% Tacsimate, 0.1 M imidazole, pH 7.5, and 12% methanol, X-ray diffraction structure determination and analysis at 1.8-2.3 A resolution Helicobacter pylori

Protein Variants

EC Number Protein Variants Comment Organism
1.14.14.18 H245A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Helicobacter pylori
1.14.14.18 H245A/R166A site-directed mutagenesis, inactive mutant Helicobacter pylori
1.14.14.18 H245N/R166A site-directed mutagenesis, inactive mutant Helicobacter pylori
1.14.14.18 H245Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Helicobacter pylori
1.14.14.18 R166A site-directed mutagenesis, the mutation completely abolished the HO activity of HugZ Helicobacter pylori

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.18 heme + 3 AH2 + 3 O2 Helicobacter pylori
-
 biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.18 Helicobacter pylori
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.14.18 recombinant His6-tagged HugZ from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Helicobacter pylori

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.18 heme + 3 AH2 + 3 O2
-
 Helicobacter pylori biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.14.18 dimer HugZ is a dimer in solution, that adopts a split-barrel fold. HugZ-hemin crystallizes as a trimer of dimers. Structure overview Helicobacter pylori

Synonyms

EC Number Synonyms Comment Organism
1.14.14.18 HugZ
-
 Helicobacter pylori
1.14.14.18 More HugZ belongs to a distinct heme-binding protein family with a split-barrel fold Helicobacter pylori

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.14.18 7.6
-
 assay at Helicobacter pylori

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.18 heme the heme is located at the intermonomer interface and is bound by both monomers. The heme iron is coordinated by the side chain of His245 and an azide molecule when it is present in crystallization conditions Helicobacter pylori

General Information

EC Number General Information Comment Organism
1.14.14.18 physiological function HugZ is part of the iron acquisition mechanism of Helicobacter pylori, and is required for the adaptive colonization of the pathogen in human hosts. Arg166, which is involved in azide binding, is essential for HugZ enzymatic activity, whereas His245 is not, implying that HugZ has an enzymatic mechanism distinct from other heme oxygenases Helicobacter pylori