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Literature summary for 1.14.14.18 extracted from

  • Mourino, S.; Giardina, B.; Reyes-Caballero, H.; Wilks, A.
    Metabolite-driven regulation of heme uptake by the biliverdin IXbeta/delta-selective heme oxygenase (HemO) of Pseudomonas aeruginosa (2016), J. Biol. Chem., 291, 20503-20515 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
H26A/K34A/K132A mutant does not interact with holo-PhuS and shows no enzymatic activity Pseudomonas aeruginosa
N19K/K34A/F117Y/K132A change in regioselectivity, product is biliverdin IXalpha Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa O69002
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protoheme + [reduced NADPH-hemoprotein reductase] + O2
-
 Pseudomonas aeruginosa biliverdin IXbeta + biliverdin IXdelta + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Synonyms

Synonyms Comment Organism
biliverdin-producing heme oxygenase
-
 Pseudomonas aeruginosa
PigA
-
 Pseudomonas aeruginosa

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
54 56 melting temperature, wild-type and mutants H26A/K34A/K132A and N19K/K34A/F117Y/K132A Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
heme sprectrum shows a Soret band at 407 nm Pseudomonas aeruginosa

General Information

General Information Comment Organism
physiological function enzyme interacts and acquires heme from cytoplasmic heme transport protein holo-PhuS. In mutant strains, the absence of bilverdin IXbeta and bilverdinIXdelta leads to a decrease in extracellular levels of hemophore HasA Pseudomonas aeruginosa