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Literature summary for 1.14.14.18 extracted from

  • Peng, D.; Ma, L.H.; Smith, K.M.; Zhang, X.; Sato, M.; La Mar, G.N.
    Role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis: a nuclear magnetic resonance study (2012), Biochemistry, 51, 7054-7063.
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
propionate the enzyme requires only a single propionate interacting with the buried terminus of Lys16 to exhibit full activity, and it tolerates the existence of a propionate at the exposed 8-position Neisseria meningitidis

Inhibitors

Inhibitors Comment Organism Structure
azide binding structure, NMR analysis, overview Neisseria meningitidis
cyanide binding structure, NMR analysis, overview Neisseria meningitidis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
heme + 3 AH2 + 3 O2 Neisseria meningitidis
-
 biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
heme + 3 AH2 + 3 O2
-
 Neisseria meningitidis biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?
heme + 3 reduced ascorbate + 3 O2
-
 Neisseria meningitidis biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O
-
 ?

Cofactor

Cofactor Comment Organism Structure
ascorbate
-
 Neisseria meningitidis

General Information

General Information Comment Organism
additional information analysis of enzyme-protohemin substrate variant complexes and of enzyme-propionate substrate complexes by NMR, active site structure, overview. The enzyme's C-terminal fragment interacts with the active site of the enzyme. The C-terminal dipeptide Arg208-His209 cleaves spontaneously. Stronger hydrophobic contacts between pyrroles A and B with the enzyme contribute more substantially to the substrate binding free energy than in mammalian HOs, liberating one propionate to stabilize the C-terminus Neisseria meningitidis