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Literature summary for 2.4.1.17 extracted from

  • Hutabarat, R.M.; Yost, G.S.
    Purification and characterization of an ethanol-induced UDP-glucuronosyltransferase (1989), Arch. Biochem. Biophys., 273, 16-25.
    View publication on PubMed
Search for more literature for 2.4.1.17

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0036
-
 UDPglucuronic acid 1.5 mM morphine added, ethanol-induced enzyme Oryctolagus cuniculus
0.0054
-
 UDPglucuronic acid 1.5 mM morphine added, non-induced enzyme Oryctolagus cuniculus
0.0065
-
 UDPglucuronic acid 0.75 mM 1-naphthol added, ethanol-induced enzyme Oryctolagus cuniculus
0.0084
-
 UDPglucuronic acid 0.76 mM 1-naphthol added, non-induced enzyme Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Oryctolagus cuniculus
-
-

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
 rabbit
-

Purification (Commentary)

Purification (Comment) Organism
-
 Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-naphthol + UDP-glucuronate
-
 Oryctolagus cuniculus naphth-1-yl-beta-D-glucuronide + UDP
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 1-naphthol as substrate Oryctolagus cuniculus