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

BRENDA support

Literature summary extracted from

  • Caignan, G.A.; Deshmukh, R.; Wilks, A.; Zeng, Y.; Huang, H.W.; Moenne-Loccoz, P.; Bunce, R.A.; Eastman, M.A.; Rivera, M.
    Oxidation of heme to beta- and delta-biliverdin by Pseudomonas aeruginosa heme oxygenase as a consequence of an unusual seating of the heme (2002), J. Am. Chem. Soc., 124, 14879-14892.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.14.99.58 F117Y no change in regioselectivity Pseudomonas aeruginosa
1.14.99.58 N19K no change in regioselectivity Pseudomonas aeruginosa
1.14.99.58 N19K/F117Y change in regioselectivity, producing alpha-biliverdin and less beta- and delta-biliverdin, enzyme exists as a mixture of molecules exhibiting 2 distinct heme seatings, one seating is identical to wild-type, the other is similar to that typical of alpha-hydroxylating heme oxigenases Pseudomonas aeruginosa

Organism

EC Number Organism UniProt Comment Textmining
1.14.99.58 Pseudomonas aeruginosa
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.99.58 heme + electron donor + O2
-
Pseudomonas aeruginosa alpha-biliverdin + beta-biliverdin + delta-biliverdin + Fe2+ + CO + oxidized eletron donor + H2O wild-type, mutant N19K, mutant F117Y, 30% beta- and 70% delta-isomer, N19K/F117Y double mutant, 55% alpha-, 10% beta-, 35% delta-isoform ?