EC Number   |
General Information |
Reference |
|---|
    1.14.14.18 | evolution |
bacterial HmuO and mammalian heme oxygenases are similar in their reaction mechanisms and structures |
728081 |
| 1.14.14.18 | evolution |
HmuO and mammalian heme oxygenases are similar in their reaction mechanisms and structures |
728081 |
| 1.14.14.18 | evolution |
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. In Pseudomonas aeruginosa PAO1, PigA is encoded in a cluster together with proteins involved in iron utilization while BphO is functionally and genetically coupled to the phytochrome BphP |
726833 |
| 1.14.14.18 | evolution |
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. In Pseudomonas fluorescence Pf-5, PigA is encoded in a cluster together with proteins involved in iron utilization while BphO is functionally and genetically coupled to the phytochrome BphP |
-, 726833 |
| 1.14.14.18 | evolution |
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. In Pseudomonas mendocina YMP, PigA is encoded in a cluster together with proteins involved in iron utilization while BphO is functionally and genetically coupled to the phytochrome BphP |
-, 726833 |
| 1.14.14.18 | evolution |
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. In Pseudomonas syringae DC3000, PigA is encoded in a cluster together with proteins involved in iron utilization while BphO is functionally and genetically coupled to the phytochrome BphP |
-, 726833 |
| 1.14.14.18 | evolution |
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. Only one of the two PigA homologues identified in Pseudomonas putida KT2440 is encoded in an iron-associated gene cluster |
-, 726833 |
| 1.14.14.18 | malfunction |
mutation of ChuZ abolishes the ability of Campylobacter jejuni to use hemin or hemoglobin as sources of iron |
726864 |
| 1.14.14.18 | malfunction |
mutation of the distal Asp decreases the verdoheme ring opening activity |
728081 |
| 1.14.14.18 | metabolism |
isoform HO-1 modulates the function of transcriptional factor Nuclear factor erythroid 2-related factor 2 (Nrf2). In oxidative stress, nuclear isoform HO-1 interacts with Nrf2 and stabilizes it from glycogen synthase kinase 3beta-mediated phosphorylation coupled with ubiquitin-proteasomal degradation, thereby prolonging its accumulation in the nucleus |
734274 |
