| Name | pyruvate carboxylase |
|---|---|
| Synonyms | PC; PCB; Pyruvate carboxylase; Pyruvic carboxylase; Pyruvate carboxylases; Pyruvic carboxylases; Carboxylase, pyruvate |
| Name | oxamate |
|---|---|
| CAS | hexyl 2-(diethylamino)-2-oxoacetate |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 3963816 | Martin-Requero A, Ayuso MS, Parrilla R: Interaction of oxamate with the gluconeogenic pathway in rat liver. . Arch Biochem Biophys. 1986 Apr;246(1):114-27. The following observations indicate that oxamate inhibits flux through pyruvate carboxylase: accumulation of substrates and decreased concentration of all metabolic intermediates beyond decreased levels of and and enhanced ketone body production, which is a sensitive indicator of decreased mitochondrial free levels. |
163(2,2,2,3) | Details |
| 3814578 | Attwood PV, Cleland WW: Decarboxylation of by pyruvate carboxylase. . Biochemistry. 1986 Dec 16;25(25):8191-6. The decarboxylation of by pyruvate carboxylase in the absence of ADP and Pi is stimulated 400-fold by the presence of oxamate, which is an inhibitory analogue of |
33(0,1,1,3) | Details |
| 19341298 | Zeczycki TN, St Maurice M, Jitrapakdee S, Wallace JC, Attwood PV, Cleland WW: Insight into the carboxyl transferase domain mechanism of pyruvate carboxylase from Rhizobium etli. Biochemistry. 2009 May 26;48(20):4305-13. The effects of mutations in the active site of the carboxyl transferase domain of Rhizobium etli pyruvate carboxylase have been determined for the forward reaction to form the reverse reaction to form MgATP, the oxamate-induced decarboxylation of the phosphorylation of MgADP by and the -dependent ATPase reaction. |
32(0,1,1,2) | Details |
| 20230056 | Duangpan S, Jitrapakdee S, Adina-Zada A, Byrne L, Zeczycki TN, St Maurice M, Cleland WW, Wallace JC, Attwood PV: Probing the Catalytic Roles of Arg548 and Gln552 in the Carboxyl Transferase Domain of the Rhizobium etli Pyruvate Carboxylase by Site-Directed Mutagenesis. Biochemistry. 2010 Mar 25. The effects of oxamate on the catalysis in the biotin carboxylase domain by the R548K and Q552N mutants were similar to those on the catalysis of reactions by the wild-type enzyme. |
3(0,0,0,3) | Details |
| 8512310 | Werneburg BG, Ash DE: Chemical modifications of chicken liver pyruvate carboxylase: evidence for essential - pairs and a reactive sulfhydryl group. Arch Biochem Biophys. 1993 Jun;303(2):214-21. Enzyme modified with 2 equivalents of isoindole retained only 7% of the oxamate-induced, ADP/Pi-independent decarboxylase activity, suggesting that there is at least one essential - ion pair at or near the second subsite. |
3(0,0,0,3) | Details |
| 1445229 | Attwood PV, Graneri BD: -dependent ATP cleavage catalysed by pyruvate carboxylase in the absence of Biochem J. 1992 Nov 1;287 ( Pt 3):1011-7. The HCO3 (-)-dependent MgATP cleavage is also sensitive to inhibition by a pyruvate carboxylase inhibitor, oxamate, and the dependence of the reaction on the free Mg2+ concentration is similar to that of the -carboxylation reaction, whereas the HCO3 (-)-independent MgATP cleavage is not dependent on the concentration of free Mg2+ in the range tested. |
3(0,0,0,3) | Details |
| 7340821 | Goodall GJ, Baldwin GS, Wallace JC, Keech DB: Factors that influence the translocation of the N-carboxybiotin moiety between the two sub-sites of pyruvate carboxylase. Biochem J. 1981 Dec 1;199(3):603-9. At low concentrations induces this movement but does not efficiently act as a carboxy-group acceptor; and oxamate, though not carboxylated, still induce the movement. |
2(0,0,0,2) | Details |
| 15030490 | Sueda S, Islam MN, Kondo H: Protein engineering of pyruvate carboxylase: investigation on the function of and the quaternary structure. Eur J Biochem. 2004 Apr;271(7):1391-400. The two proteins thus formed, PC-(BC) and PC-(CT+BCCP), retained their catalytic activity as assayed by -dependent ATPase and oxamate-dependent decarboxylation, for the former and the latter, respectively. |
2(0,0,0,2) | Details |
| 19683593 | Si Y, Shi H, Lee K: Impact of perturbed pyruvate metabolism on adipocyte triglyceride accumulation. Metab Eng. 2009 Nov;11(6):382-90. Epub 2009 Aug 14. We treated cultured 3T3-L1 adipocytes with chemical inhibitors of lactate dehydrogenase (LDH) and pyruvate carboxylase (PC), and characterized their global effects on intermediary metabolism using metabolic flux and isotopomer analysis. |
1(0,0,0,1) | Details |
| 3028472 | Attwood PV, Tipton PA, Cleland WW: Carbon-13 and deuterium isotope effects on decarboxylation by pyruvate carboxylase. Biochemistry. 1986 Dec 16;25(25):8197-205. The reduction in the magnitude of the 13C isotope effect for the oxamate-dependent decarboxylation of from 1.0238 to 1.0155 when the reaction was performed in D2O (primary deuterum isotope effect = 2.1) clearly indicates that the transfer of the and carboxyl group between and does not occur via a single concerted reaction. |
1(0,0,0,1) | Details |
| 3771515 | Martin-Requero A, Ayuso MS, Parrilla R: Rate-limiting steps for hepatic gluconeogenesis. J Biol Chem. 1986 Oct 25;261(30):13973-8. Mechanism of oxamate inhibition of mitochondrial pyruvate metabolism.. |
0(0,0,0,0) | Details |