Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

6.4.1.1: pyruvate carboxylase

This is an abbreviated version!
For detailed information about pyruvate carboxylase, go to the full flat file.

Word Map on EC 6.4.1.1

Reaction

ATP
+
pyruvate
+
HCO3-
+
H+
=
ADP
+
phosphate
+
oxaloacetate

Synonyms

Carboxylase, pyruvate, EhPYC1, HpPyc1p, Mfla_1512, MSmeg_2412, PC, Pcase, PCB, PCC, PCx, PYC, Pyc1, Pyc1p, PYC2, pycA, pyruvate carboxylase, pyruvate carboxylase 1, Pyruvic carboxylase, RePC

ECTree

     6 Ligases
         6.4 Forming carbon-carbon bonds
             6.4.1 Ligases that form carbon-carbon bonds (only sub-subclass identified to date)
                6.4.1.1 pyruvate carboxylase

General Stability

General Stability on EC 6.4.1.1 - pyruvate carboxylase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA and sodium pyruvate protects against cold inactivation. L-Asp decreases inactivation, 1 M sucrose gives complete protection
-
acetyl-CoA protects against thermal denaturation
-
acetyl-CoA stabilizes quarternary structure of the enzyme
dilution inactivates the enzyme, inactivation can be prevented at 10 mM Mg2+
-
dilution results in irreversible inactivation, which can be partially avoided by addition of acetyl-CoA. Glycerol stabilizes
-
does not participate directly in the reaction mechanism, but may play a structural role essential to the integrity of the enzymes tetrameric structure
-
freezing and thawing over a 16 h period results in rapid loss of activity
-
inactivated reversibly and converted to protomers by incubation at 0°C in the presence of high concentrations of Cl- salts of monovalent cations. MgCl2 or sucrose prevent inactivation
-
stable to exposure to 6 M urea for up to 2.5 h at 20°C
-
the presence of KCl at 10, 20, 50, and 100 mM potassium phosphate buffer-KCl buffer at 0°C leads to 85%, 44%, 17% and 0% loss of activity
-
upon dilution, there is dissociation of the catalytically active tetrameric enzyme species into inactive dimers. Reactivation of the enzyme results in reassociation of enzymic dimers into tetramers.
-