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Literature summary for 1.13.11.52 extracted from

  • Freewan, M.; Rees, M.D.; Plaza, T.S.; Glaros, E.; Lim, Y.J.; Wang, X.S.; Yeung, A.W.; Witting, P.K.; Terentis, A.C.; Thomas, S.R.
    Human indoleamine 2,3-dioxygenase is a catalyst of physiological heme peroxidase reactions: implications for the inhibition of dioxygenase activity by hydrogen peroxide (2013), J. Biol. Chem., 288, 1548-1567.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.13.11.52

Activating Compound

Activating Compound Comment Organism Structure
ascorbate promotes IDO peroxidase turnover by reducing Compound II Homo sapiens
hydrogen peroxide activates the peroxidase function of IDO to induce protein oxidation and inhibit dioxygenase activity Homo sapiens
additional information L-Trp is a poor reductant of IDO compound II Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
cyanide inhibits the dioxygenase activity Homo sapiens
H2O2 inhibits the dioxygenase activity in a manner abrogated by L-Trp. Physiological peroxidase substrates, ascorbate or tyrosine, enhanced rIDO-mediated H2O2 consumption and attenuated H2O2-induced protein oxidation and dioxygenase inhibition. H2O2 alters the heme active site of recombinant IDO Homo sapiens
additional information the dioxygenase enzyme activity is inhibited by free radical scavengers. Protection of the dioxygenase enzyme function by L-Trp coincides with its oxidation into oxindolylalanine and kynurenine and the formation of a compound II-type ferryl-oxo heme Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ heme-containing enzyme, reduction of heme from the ferric (FeIII) to the ferrous (FeII) form facilitates binding of O2 and L-Trp to form the active ternary complex Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens the enzyme acts as a heme peroxidase that, in the absence of substrates, self-inactivates dioxygenase activity via compound I-initiated protein oxidation. L-Trp protects against dioxygenase inactivation by reacting with compound I and retarding compound II reduction to suppress peroxidase turnover. Catalytic cycle of hemeperoxidase enzymes, and enzyme peroxidase mechanism, overview ?
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 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme acts as a heme peroxidase that, in the absence of substrates, self-inactivates dioxygenase activity via compound I-initiated protein oxidation. L-Trp protects against dioxygenase inactivation by reacting with compound I and retarding compound II reduction to suppress peroxidase turnover. Catalytic cycle of hemeperoxidase enzymes, and enzyme peroxidase mechanism, overview Homo sapiens ?
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 ?

Synonyms

Synonyms Comment Organism
IDO
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 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
heme the active-site heme is essential for IDO dioxygenase activity, reduction of heme from the ferric (FeIII) to the ferrous (FeII) form facilitates binding of O2 and L-Trp to form the active ternary complex Homo sapiens

General Information

General Information Comment Organism
additional information H2O2 activates the peroxidase function to induce protein oxidation and inhibit dioxygenase activity, overview. Dioxygenase inhibition correlated with IDO-catalyzed H2O2 consumption, compound I-mediated formation of protein-centered radicals, altered protein secondary structure, and opening of the distal heme pocket to promote nonproductive substrate binding, inhibited by L-Trp, the heme ligand cyanide, or free radical scavengers Homo sapiens
physiological function heme enzyme indoleamine 2,3-dioxygenase is a key regulator of immune responses through catalyzing L-tryptophan oxidation. Peroxidase-mediated dioxygenase inactivation, NO consumption, or protein nitration may modulate the biological actions of IDO expressed in inflammatory tissues where the levels of H2O2 and NO are elevated and L-Trp is low Homo sapiens