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]

Posttranslational Modification

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

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

additional information

Pseudomonas aeruginosa

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heme transfer to the enzyme is independent of heme affinity and is mediated via a specific protein-protein interaction. A spin transition is involved during the transfer process with spin-state crossover occuring in the heme binding protein PhuS prior to the heme transfer step or alternatively occuring within the enzyme. Activation energies at pH 7.5 for the heme transfer from PhuS to enzyme are about 12-14 kcal per mol

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