Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.14.18 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
Search for more literature for 1.14.14.18

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Helicobacter pylori
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
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

General Information Comment Organism
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