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6.4.1.3: propionyl-CoA carboxylase

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

Word Map on EC 6.4.1.3

Reaction

ATP
+
propanoyl-CoA
 +
HCO3-
 +
H+
=
ADP
 +
phosphate
 +
(S)-methylmalonyl-CoA

Synonyms

AccA3-PccB complex, acetyl-CoA/propionyl-CoA carboxylase, Carboxylase, propional coenzyme A (adenosine triphosphate-hydrolyzing), LA_2736-LA_2735, Pcase, PCC, PccA, PccA-1, PCCase, PccB, PccB-1, pccBC, PccE, Propanoyl-CoA:carbon dioxide ligase, Propionyl coenzyme A carboxylase, Propionyl coenzyme A carboxylase (adenosine triphosphate-hydrolyzing), Propionyl coenzyme A carboxylase (ATP-hydrolyzing), Propionyl-CoA carboxylase, propionyl-coenzyme A carboxylase

ECTree

     6 Ligases
         6.4 Forming carbon-carbon bonds
             6.4.1 Ligases that form carbon-carbon bonds (only sub-subclass identified to date)
                6.4.1.3 propionyl-CoA carboxylase

Temperature Stability

Temperature Stability on EC 6.4.1.3 - propionyl-CoA carboxylase

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-50 - 37
-
stable
0 - 40
-
maximal stability
47
-
30 min, wild-type enzyme is stable, mutant enzyme A497V loses 40% of its activity mutant enzymes R165W, E168K and R410W lose 85% of their activity
50
Q877I4; Q877I3; Q877I5
2 h, 40% loss of activity
58
-
the wild-type enzyme undergoes a cooperative two-state transition between the native and denatured states with a Tm of 57.6°C
60
Q877I4; Q877I3; Q877I5
30 min, 50% loss of activity
70
Q877I4; Q877I3; Q877I5
30 min, 90% loss of activity
80
Q877I4; Q877I3; Q877I5
30 min, 95% loss of activity
90
Q877I4; Q877I3; Q877I5
10 min, complete loss of activity
additional information
-
thermal denaturation is irreversible