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Literature summary for 1.14.11.1 extracted from

  • Lin, X.; Lyvers Peffer, P.A.; Woodworth, J.; Odle, J.
    Ontogeny of carnitine biosynthesis in Sus scrofa domesticus, inferred from gamma-butyrobetaine hydroxylase (dioxygenase) activity and substrate inhibition (2020), Am. J. Physiol. Regul. Integr. Comp. Physiol., 319, R43-R49 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
4-Trimethylammoniobutanoate substrate inhibition associated with age is observed at concentrations above 0.6 mM Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.013
-
4-Trimethylammoniobutanoate apparent kinetic constant (Km), in liver of 1-day-old domestic pig, pH 7.4, 37°C Sus scrofa
0.025
-
4-Trimethylammoniobutanoate apparent kinetic constant (Km), in liver of 7-day-old domestic pig, pH 7.4, 37°C Sus scrofa
0.026
-
4-Trimethylammoniobutanoate apparent kinetic constant (Km), in liver of 56-day-old domestic pig, pH 7.4, 37°C Sus scrofa
0.032
-
4-Trimethylammoniobutanoate apparent kinetic constant (Km), in kidney of 1-day-old domestic pig, pH 7.4, 37°C Sus scrofa
0.037
-
4-Trimethylammoniobutanoate apparent kinetic constant (Km), in kidney of 56-day-old domestic pig, pH 7.4, 37°C Sus scrofa
0.038
-
4-Trimethylammoniobutanoate apparent kinetic constant (Km), in liver of 21-day-old domestic pig, pH 7.4, 37°C Sus scrofa
0.041
-
4-Trimethylammoniobutanoate apparent kinetic constant (Km), in liver of 35-day-old domestic pig, pH 7.4, 37°C Sus scrofa
0.053
-
4-Trimethylammoniobutanoate apparent kinetic constant (Km), in liver of newborn domestic pig, pH 7.4, 37°C Sus scrofa
0.06
-
4-Trimethylammoniobutanoate apparent kinetic constant (Km), in liver of 210-day-old domestic pig, pH 7.4, 37°C Sus scrofa
0.061
-
4-Trimethylammoniobutanoate apparent kinetic constant (Km), in kidney of 7-day-old domestic pig, pH 7.4, 37°C Sus scrofa
0.063
-
4-Trimethylammoniobutanoate apparent kinetic constant (Km), in kidney of 21-day-old domestic pig, pH 7.4, 37°C Sus scrofa
0.074
-
4-Trimethylammoniobutanoate apparent kinetic constant (Km), in kidney of 210-day-old domestic pig, pH 7.4, 37°C Sus scrofa
0.086
-
4-Trimethylammoniobutanoate apparent kinetic constant (Km), in kidney of 35-day-old domestic pig, pH 7.4, 37°C Sus scrofa
0.119
-
4-Trimethylammoniobutanoate apparent kinetic constant (Km), in kidney of newborn domestic pig, pH 7.4, 37°C Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-trimethylammoniobutanoate + 2-oxoglutarate + O2 Sus scrofa
-
3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Sus scrofa F1SGL4
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney from newborn and 1-, 7-, 21-, 35-, 56-, and 210-day-old domestic pigs. The predominant organ for carnitine synthesis is likely the kidney at birth. The liver appears to predominate after the pig exceeds 7 days of age Sus scrofa
-
liver from newborn and 1-, 7-, 21-, 35-, 56-, and 210-day-old domestic pigs. The predominant organ for carnitine synthesis is likely the kidney at birth. The liver appears to predominate after the pig exceeds 7 days of age Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-trimethylammoniobutanoate + 2-oxoglutarate + O2
-
Sus scrofa 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2
-
?

Synonyms

Synonyms Comment Organism
gamma-BBH
-
Sus scrofa
gamma-butyrobetaine hydroxylase
-
Sus scrofa

Expression

Organism Comment Expression
Sus scrofa hepatic activity is low at birth but increases after 1 day. By 21 days, the activity rises by 6.6fold and remains constant after 56 days. Renal activity is higher than in liver at birth but remains constant through 35 days. By 56 days, the velocity increases by 44% over the activity at birth up

General Information

General Information Comment Organism
metabolism last limiting enzyme of the L-carnitine biosynthesis pathway and plays an important role in catalyzing the hydroxylation of gamma-butyrobetaine to L-carnitine Sus scrofa