1.14.99.58: heme oxygenase (biliverdin-IX-beta and delta-forming)

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For detailed information about heme oxygenase (biliverdin-IX-beta and delta-forming), go to the full flat file.

Reaction

Synonyms

biliverdin IXbeta/delta-selective heme oxygenase, BphO, heme-PigA heme oxygenase, heme-PigA(HO), HemO, PigA

ECTree

     1 Oxidoreductases

         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

             1.14.99 Miscellaneous

                1.14.99.58 heme oxygenase (biliverdin-IX-beta and delta-forming)

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Results	in table
1	Activating Compound
17	AA Sequence
1	Application
16	Cloned(Commentary)
8	Cofactor
2	Crystallization (Commentary)
1	General Information
13	Inhibitors
6	KM Value [mM]
1	Metals/Ions
2	Molecular Weight [Da]
30	Natural Substrates/ Products (Substrates)
29	Organism
3	Pathway
3	pH Optimum
5	pH Range
1	Posttranslational Modification
19	Protein Variants
11	Purification (Commentary)
4	Reaction
29	Reference
44	Substrates and Products (Substrate)
3	Subunits
28	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
1	Temperature Stability [°C]

Crystallization

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Crystallization on EC 1.14.99.58 - heme oxygenase (biliverdin-IX-beta and delta-forming)

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

Carr-Purcell-Meiboom-Gill NMR study on ferric enzyme state inhibited by cyanide and azide, and its ferrous state inhibited by carbon monoxide. The nature of the coordinated distal ligand affects the conformational freedom of the polypeptide in regions of the enzyme far removed from the heme iron and distal ligand. In addition to proton delivery to the nascent FeIII-OO- intermediate during catalysis, the hydrogen-bonding network serves to propagate the electronic state in each of the distinct steps of the catalytic cycle to key but remote sections of the polypeptide and to modulate the conformational freedom of the enzyme

Pseudomonas aeruginosa

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680357

NMR-spectroscopy studies of paramagnetic cyanide-inhibited and azide-inhibited enzyme forms. The protein in the azide-inhibited complex is significantly less prone to H/D exchange than the cyanide-inhibited form. Unpaired spin delocalization from the heme iron into the G15-N atom via formation of a hydrogen bond between the coordinated azide nitrogen and the G125 N-H

Pseudomonas aeruginosa

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678184