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Literature summary for 1.14.14.18 extracted from

  • Peng, D.; Satterlee, J.D.; Ma, L.H.; Dallas, J.L.; Smith, K.M.; Zhang, X.; Sato, M.; La Mar, G.N.
    Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis. A 1H NMR study (2011), Biochemistry, 50, 8823-8833.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information C-terminal truncation of the enzyme, e.g. by sequential deletion of three residues, His207, Arg208, His209. Deleting His209 minimally perturbs the interaction of the C-terminus, but deletion of Arg208 completely abolishes it Neisseria meningitidis

Inhibitors

Inhibitors Comment Organism Structure
azide
-
 Neisseria meningitidis
cyanide
-
 Neisseria meningitidis

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis
-
-
-

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 from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of alpha-verdoheme to alpha-biliverdin, overview Neisseria meningitidis
a

General Information

General Information Comment Organism
additional information the enzyme shows substrate-protein, specifically pyrrole-I/II-helix-2, peripheral interactions. The enzyme's C-terminus interacts with substrate in solution, interaction of the C-terminus with the active site destabilizes the crystallographic protohemin orientation, which is consistent with optimizing the His207-Asp27 H-bond, active site stress for product release, NMR analysis of wild-type and mutant enzymes, overview. Thermodynamics of substrate orientational isomerism are mapped for substrates with individual vinyl to methyl to hydrogen substitutions and with enzyme C-terminal deletions. Replacing bulky vinyls with hydrogens results in a 180 degree rotation of substrate about the alpha,gamma-meso axis in the active site Neisseria meningitidis