| Name | ATPase |
|---|---|
| Synonyms | ATP7A; MK; ATPase; Cation transporting ATPase; ATP7A protein; ATPase Cu(2+) transporting alpha polypeptide; Copper pump 1; Copper transporting ATPase 1… |
| Name | oxamate |
|---|---|
| CAS | hexyl 2-(diethylamino)-2-oxoacetate |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 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. |
81(1,1,1,1) | 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. This indicates that MgATP cleavage by pyruvate carboxylase is entirely dependent on the presence of HCO3- and that there may be a low level of ATPase contamination in the enzyme preparations. |
1(0,0,0,1) | 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. |
31(0,1,1,1) | Details |