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Literature summary for 1.14.14.18 extracted from

  • Zhou, W.P.; Zhong, W.W.; Zhang, X.H.; Ding, J.P.; Zhang, Z.L.; Xia, Z.W.
    Comparison of the crystal structure and function to wild-type and His25Ala mutant human heme oxygenase-1 (2009), Int. J. Mol. Med., 23, 379-387.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information the proximal residue histidine 25 plays a key role in HO-1 activity Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
710-bp fragment encoded amino acids of wild-type and mutant HO-1 constructed in the plasmids pET28b(+)-hHO-1(w) and (m), expressed in Escherichia coli BL21 (DE3) Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type and mutant H25A, by hanging drop vapor diffusion method, at 2.8 A resolution. Mutant heme-HO-1 crystal is monoclinic, space group P21, there are four molecules in an asymmetric unit cell. The molecular surfaces of wild-type and mutant are of little difference, though the active pocket in the mutant is larger. The two have the same substrate affinity in electrostatic potential. A positive charge region on the edge of heme forms around the catalytic reaction pocket. After mutation, Ala is still located in the surface and does not influence the electrostatic potential of the reaction pocket Homo sapiens

Protein Variants

Protein Variants Comment Organism
H25A mutation leads to an empty pocket underneath the ferric ion in the heme, leading to loss of binding iron ligand. Enzymatic activity is reduced by 90.5%. By supplementing imidazole, the HO-1 activity is restored approximately 87.5% to its normal level Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28000
-
x * 28000, wild-type and mutant, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
on Ni-NTA column, wild-type 32fold purified and mutant H25A 31fold purified, more than 95% pure Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
heme + electron donor + O2
-
Homo sapiens biliverdin + Fe2+ + CO + oxidized electron donor + H2O
-
?

Subunits

Subunits Comment Organism
? x * 28000, wild-type and mutant, SDS-PAGE Homo sapiens

Synonyms

Synonyms Comment Organism
heme oxygenase-1
-
Homo sapiens
HO-1
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Homo sapiens