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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

Engineering

Engineering on EC 6.4.1.3 - propionyl-CoA carboxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A487V
-
no effect on activity
A497V
A513_R514insP
D178H
increased alpha/beta subunit ratio, very low activity
DELTA408
catalytically inactive
DELTA499
DELTA514
DELTA531
E168K
G131R
G198D
G246V
-
activity of the mutant enzyme is 12% of the wild-type activity
L519P
M442T
catalytically inactive
N536D
P228L
increased alpha/beta subunit ratio, very low activity
R165Q
-
beta subunit, no effect on subunit interactions and activity
R165W
R410W
R44P
catalytically inactive
R512C
R67S
-
beta subunit, no effect on subunit interactions only when expressed at low temperature (27°C), reduced activity at 37°C
S106R
V205D
W531X
-
activity of the mutant enzyme is less than 1% of the wild-type activity
A431C
-
kcat (propionyl-CoA) decreased compared to wild-type, Km (propionyl-CoA) increased compared to wild-type. kcat (acetyl-CoA) increased compared to wild-type, Km (propionyl-CoA) similar to wild-type
A431D
-
mutant enzyme shows no activity
A431I
-
kcat (propionyl-CoA) decreased compared to wild-type, Km (propionyl-CoA) increased compared to wild-type. kcat (acetyl-CoA) increased compared to wild-type, Km (propionyl-CoA) similar to wild-type
A431L
-
mutant enzyme shows no activity
Y430H/A431I
-
mutant enzyme shows no activity
D440I
the mutation does not change the substrate preference of the enzyme
G668R
the mutation in the biotin carboxyl carrier protein domain abolishes biotinylation
R165Q
the mutation disturbs the recognition of the adenine base of CoA
R165W
the mutation disturbs the recognition of the adenine base of CoA
R399Q
the mutation leads to a large loss in activity
D422A
mutant of the PccB subunit, shows strong preference for butyryl-CoA as substrate
D422C
mutant of the PccB subunit, shows strong preference for butyryl-CoA as substrate
D422I
mutant of the PccB subunit, accepts acetyl-CoA, propionyl-CoA, and butyrl-CoA as substrates, the latter two with lower Vmax/Km values as compared to the wild type enzyme
D422L
mutant of the PccB subunit, the mutants has narrowed down their substrate specificity, accepting only propionyl-CoA as its substrate
D422N
mutant of the PccB subunit, the mutants has narrowed down their substrate specificity, accepting only propionyl-CoA as its substrate
D422V
mutant of the PccB subunit, accepts both propionyl-CoA and butyrl-CoA as substrates but with lower Vmax/Km values as compared to the wild type enzyme
additional information