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Literature summary extracted from

  • Unno, M.; Matsui, T.; Ikeda-Saito, M.
    Crystallographic studies of heme oxygenase complexed with an unstable reaction intermediate, verdoheme (2012), J. Inorg. Biochem., 113, 102-109.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.14.18 heme oxygenase HmuO in tertiary complex with reaction intermediate verdoheme and N3, X-ray diffraction structure determination and analysis at 1.7 resolution Corynebacterium diphtheriae
1.14.14.18 heme oxygenase HO1 complexed with reaction intermediate verdoheme, and in tertiary complex with verdoheme and NO, X-ray diffraction structure determination and analysis at 2.2 and 2.1 A resolution, respectively Homo sapiens
1.14.14.18 heme oxygenase HO1 complexed with reaction intermediate verdoheme, X-ray diffraction structure determination and analysis at 2.2 A resolution Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.18 CO the third reaction step is inhibited by CO Corynebacterium diphtheriae
1.14.14.18 CO the third reaction step is inhibited by CO Homo sapiens
1.14.14.18 CO the third reaction step is inhibited by CO Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.18 heme + 3 AH2 + 3 O2 Homo sapiens
-
 biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?
1.14.14.18 heme + 3 AH2 + 3 O2 Rattus norvegicus
-
 biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?
1.14.14.18 heme + 3 AH2 + 3 O2 Corynebacterium diphtheriae
-
 biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.18 Corynebacterium diphtheriae Q54AI1
-
-
1.14.14.18 Homo sapiens P09601
-
-
1.14.14.18 Rattus norvegicus P06762
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.14.18 protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme. Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices. Reaction mechanism, overview Homo sapiens
a
1.14.14.18 protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme. Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices. Reaction mechanism, overview Rattus norvegicus
a
1.14.14.18 protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme. Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices. Reaction mechanism, overview Corynebacterium diphtheriae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.18 heme + 3 AH2 + 3 O2
-
 Homo sapiens biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?
1.14.14.18 heme + 3 AH2 + 3 O2
-
 Rattus norvegicus biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?
1.14.14.18 heme + 3 AH2 + 3 O2
-
 Corynebacterium diphtheriae biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?
1.14.14.18 heme + 3 AH2 + 3 O2 reaction intermediate verdoheme and the verdoheme-enzyme complex are gradually degraded in the presence of O2 Homo sapiens biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?
1.14.14.18 heme + 3 AH2 + 3 O2 reaction intermediate verdoheme and the verdoheme-enzyme complex are gradually degraded in the presence of O2 Rattus norvegicus biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?
1.14.14.18 heme + 3 AH2 + 3 O2 reaction intermediate verdoheme and the verdoheme-enzyme complex are gradually degraded in the presence of O2 Corynebacterium diphtheriae biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.14.18 More structure comparisons, overview Homo sapiens
1.14.14.18 More structure comparisons, overview Rattus norvegicus
1.14.14.18 More structure comparisons, overview Corynebacterium diphtheriae

Synonyms

EC Number Synonyms Comment Organism
1.14.14.18 HmuO
-
 Corynebacterium diphtheriae
1.14.14.18 Ho1
-
 Homo sapiens
1.14.14.18 Ho1
-
 Rattus norvegicus

General Information

EC Number General Information Comment Organism
1.14.14.18 evolution bacterial HmuO and mammalian heme oxygenases are similar in their reaction mechanisms and structures Homo sapiens
1.14.14.18 evolution bacterial HmuO and mammalian heme oxygenases are similar in their reaction mechanisms and structures Rattus norvegicus
1.14.14.18 evolution HmuO and mammalian heme oxygenases are similar in their reaction mechanisms and structures Corynebacterium diphtheriae
1.14.14.18 malfunction mutation of the distal Asp decreases the verdoheme ring opening activity Homo sapiens
1.14.14.18 malfunction mutation of the distal Asp decreases the verdoheme ring opening activity Rattus norvegicus
1.14.14.18 malfunction mutation of the distal Asp decreases the verdoheme ring opening activity Corynebacterium diphtheriae
1.14.14.18 additional information heme oxygenase is an enzyme that catalyzes the regiospecific conversion of heme to biliverdin IXalpha, carbon monoxide, and free Fe(II). Heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme, Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices Homo sapiens
1.14.14.18 additional information heme oxygenase is an enzyme that catalyzes the regiospecific conversion of heme to biliverdin IXalpha, carbon monoxide, and free Fe(II). Heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme, Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices Rattus norvegicus
1.14.14.18 additional information heme oxygenase is an enzyme that catalyzes the regiospecific conversion of heme to biliverdin IXalpha, carbon monoxide, and free Fe(II). Heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme. Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices Corynebacterium diphtheriae