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4.1.1.32: phosphoenolpyruvate carboxykinase (GTP)

This is an abbreviated version!
For detailed information about phosphoenolpyruvate carboxykinase (GTP), go to the full flat file.

Word Map on EC 4.1.1.32

Reaction

GTP
+
oxaloacetate
=
GDP
 +
phosphoenolpyruvate
 +
CO2

Synonyms

C4 phosphoenolpyruvate carboxykinase, carboxykinase, phosphopyruvate (guanosine triphosphate), CGI_10014916, CgPCK, GDP-linked PEP carboxykinase, GTP-dependent PEPCK-C, GTP-PEPCK, GTP/ITP: oxaloacetate carboxylase (transphosphorylating), GTP/ITP:oxaloacetate carboxylyase (transphosphorylating), GTP/ITP:oxaloacetatecarboxylase (transphosphorylating), GTP:oxaloacetate carboxy-lyase, oxaloacetate kinase (decarboxylating, GDP), P-enolpyruvate carboxykinase, PCK, PCK2, PDC-E2, PEP carboxykinase, PEP carboxylase, PEP-carboxykinase, PEPC, PEPCK, PEPCK-C, PEPCK-M, phosphoenolpyruvate carboxykinase, phosphoenolpyruvate carboxykinase (GTP), phosphoenolpyruvate carboxykinase, GTP-dependent, Phosphoenolpyruvate carboxylase, phosphoenolpyruvate carboxylase (GTP), phosphoenolpyruvic carboxykinase, phosphoenolpyruvic carboxykinase (GTP), phosphoenolpyruvic carboxykinase (inosine triphosphate), Phosphoenolpyruvic carboxylase, phosphoenolpyruvic carboxylase (GTP), phosphoenolpyruvic carboxylase (inosine triphosphate), phosphopyruvate carboxykinase, phosphopyruvate carboxylase, phosphopyruvate carboxylase (GTP)

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.32 phosphoenolpyruvate carboxykinase (GTP)

Engineering

Engineering on EC 4.1.1.32 - phosphoenolpyruvate carboxykinase (GTP)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D262N
-
active site mutant, 5times higher catalytic efficiency than wild-type enzyme
D263N
-
increased Km-value for Mn2+ and phosphoenolpyruvate
H225Q
-
active site mutant, increased Km-value for Mn2+ and phosphoenolpyruvate
T249N
-
active site mutant
C306A
-
catalytically active mutant, kinetics
C306S
-
catalytically active mutant, kinetics
Y235A
site-directed mutagenesis
Y235F
site-directed mutagenesis
Y235S
site-directed mutagenesis
D75A
75% reduced activity
D75N
reduced activity
D75Q
reduced activity
D75S
reduced activity
D78A
severely reduced activity
E83A
severely reduced activity
A467G
PEPCK has a 14fold higher Km value for oxaloacetate than wild type, coupled with a reduction in kcat (26% of wild type), resulting in a reduction in catalytic efficiency by nearly two orders of magnitude (1.9% of wild type). There is little change in the Km for GTP (factor of 1.4), resulting in the catalytic efficiency for GTP decreasing by less than a factor of three. In the reverse reaction, the mutant shows a decrease in the Km value for phosphoenolpyruvate (21% of wild type), a kcat reduced to 5% of the wild type value, and a factor of four reduction in the catalytic efficiency relative to wild type
S252A
side directed mutagenesis
M139L
-
natural variant, leading to different kinetic properties
additional information