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Literature summary for 1.14.14.18 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)

Crystallization (Comment) Organism
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
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
heme oxygenase HO1 complexed with reaction intermediate verdoheme, X-ray diffraction structure determination and analysis at 2.2 A resolution Rattus norvegicus

Inhibitors

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Reaction

Reaction Comment Organism Reaction ID
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
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
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
heme + 3 AH2 + 3 O2
-
Homo sapiens biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
?
heme + 3 AH2 + 3 O2
-
Rattus norvegicus biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
?
heme + 3 AH2 + 3 O2
-
Corynebacterium diphtheriae biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
?
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
-
?
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
-
?
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

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

Synonyms

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

General Information

General Information Comment Organism
evolution bacterial HmuO and mammalian heme oxygenases are similar in their reaction mechanisms and structures Homo sapiens
evolution bacterial HmuO and mammalian heme oxygenases are similar in their reaction mechanisms and structures Rattus norvegicus
evolution HmuO and mammalian heme oxygenases are similar in their reaction mechanisms and structures Corynebacterium diphtheriae
malfunction mutation of the distal Asp decreases the verdoheme ring opening activity Homo sapiens
malfunction mutation of the distal Asp decreases the verdoheme ring opening activity Rattus norvegicus
malfunction mutation of the distal Asp decreases the verdoheme ring opening activity Corynebacterium diphtheriae
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
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
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