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Literature summary for 1.13.11.11 extracted from

  • Liu, Y.; Kim, S.M.; Wang, Y.; Karkashon, S.; Lewis-Ballester, A.; Yeh, S.R.; Correia, M.A.
    Characterization of the structural determinants of the ubiquitin-dependent proteasomal degradation of human hepatic tryptophan 2,3-dioxygenase (2021), Biochem. J., 478, 1999-2017 .
    View publication on PubMed
Search for more literature for 1.13.11.11

General Stability

General Stability Organism
one of the most rapidly degraded liver proteins with a half-life (t1/2) of about 2.3 h, relative to an average t1/2 of about 2-3 days for total liver protein Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-tryptophan + O2 Homo sapiens
-
 N-formyl-L-kynurenine
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P48775
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
ubiquitination the enzyme can be recognized and ubiquitinated by two E3 ubiquitin ligases, gp78/AMFR and CHIP, and subsequently degraded via ubiquitin-dependent proteasomal degradation pathway. 15 ubiquitination K-sites are identified. Trp-binding to an exosite impedes its proteolytic degradation Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
Hep-G2 cell
-
 Homo sapiens
-
liver
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tryptophan + O2
-
 Homo sapiens N-formyl-L-kynurenine
-
 ?

Subunits

Subunits Comment Organism
homotetramer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
TDO
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
heme hemoprotein Homo sapiens

General Information

General Information Comment Organism
physiological function tryptophan 2,3-dioxygenase is the rate-limiting enzyme in the kynurenine pathway. It catalyzes the oxidative breakdown of the essential amino acid, L-tryptophan to N-formylkynurenine. This reaction is also carried out by an analogous hemoprotein, indoleamine 2,3-dioxygenase, albeit with a much lower substrate selectivity Homo sapiens