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2.1.3.2: aspartate carbamoyltransferase

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

Word Map on EC 2.1.3.2

Reaction

Carbamoyl phosphate
+
L-aspartate
=
phosphate
 +
N-carbamoyl-L-aspartate

Synonyms

(S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase, ACT, aspartate carbamoyltransferase, aspartate carbamyltransferase, aspartate trans carbamoylase, aspartate transcarbamoylase, aspartate transcarbamylase, aspartic acid transcarbamoylase, aspartic carbamyltransferase, aspartic transcarbamylase, ATC, ATC domain of CAD, ATCase, CAD, carbamoylaspartotranskinase, carbamoyltransferase, aspartate, carbamylaspartotranskinase, L-aspartate transcarbamoylase, L-aspartate transcarbamylase, MJ1581, PYRB

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.3 Carboxy- and carbamoyltransferases
                2.1.3.2 aspartate carbamoyltransferase

Engineering

Engineering on EC 2.1.3.2 - aspartate carbamoyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A241C
-
reduced affinity for aspartate, hyperbolic aspartate saturation curve
C47A
-
Hill coefficient 1.3 as compared to 2.4 for wild-type
C47A/A241C
D162A
-
7700fold reduction in specific activity, 2fold decrease in affinity for aspartate, loss of homotropic cooperativity and decreased activation by ATP
D236A
E239Q
-
mutation in the catalytic subunit, the mutation substantially destabilize the T state of the enzyme
G128A
the mutation completely abolishes enzyme activity
G128A/G130A
the mutation completely abolishes enzyme activity
G166A
the mutant retains some activity
G166P
the mutant loses almost all activity
H107A
the mutant shows reduced activity compared to the wild type enzyme
H107A/Y197A
the mutant shows reduced activity compared to the wild type enzyme
K143A
-
mutation in the regulatory subunit, the mutation substantially destabilize the T state of the enzyme
K164E/E239K
site-directed mutagenesis, a mutant aspartate transcarbamoylase exists in an intermediate quaternary structure between the canonical T and R structures, crystal structure and quaternary conformation analysis, detailed overview. pH-Dependent structural alteration consistent with either a pH-induced conformational change or a pH-induced alteration in the T to R equilibrium
K244A
-
dramatic reduction in homotropic cooperativity and the ability of heterotropic effectors to modulate activity
K244N
-
dramatic reduction in homotropic cooperativity and the ability of heterotropic effectors to modulate activity
K60A
a regulatory mutant, which does not exhibit UTP synergistic inhibition
K6A
a regulatory mutant, which does not exhibit UTP synergistic inhibition
L151Q
-
strongly reduced stimulation by ATP, synergistic inhibition by UTP is decreased
L151V
-
stimulation by ATP is reduced by 50%
L32A
-
stimulation by ATP is reduced by 25%
L76A
-
synergistic inhibition by UTP is decreased
L7A
a regulatory mutant, which does not exhibit UTP synergistic inhibition
N111A
-
mutation in the regulatory subunit, the mutation substantially destabilize the T state of the enzyme
P268A
-
40fold reduction in activity, concentration of N-(phosphonoacetyl)-L-aspartate for maximal activation is increased 233fold as compared to the wild-type, less activation by ATP, stronger inhibition by CTP
Q137A
Q73E
-
stimulation by ATP is reduced by 80%
R105A
catalytic trimer mutant
R167A
V106A
-
synergistic inhibition by UTP is decreased
V106W
-
strongly reduced stimulation by ATP
V106W/Y77F
-
strongly reduced stimulation by ATP
Y165F
-
mutant enzyme shows greatly reduced affinity for aspartate and activity
Y197A
the mutant shows reduced activity compared to the wild type enzyme
Y197F
the mutant shows reduced activity compared to the wild type enzyme
Y240F
-
mutant enzyme shows higher affinity for aspartate and increased activity
Y77F
-
synergistic inhibition by UTP is decreased
D1958A
the mutant shows 2.5fold reduced activity compared to the wild type enzyme
E1954A
the mutant shows 4fold reduced activity compared to the wild type enzyme
G128A/G130A
-
the mutant loses almost all activity
G130A
-
the mutant retains some activity
G132A
-
the mutation completely abolishes enzyme activity
G166A
-
the mutant retains some activity
G166P
-
the mutant loses almost all activity
R2024Q
the mutation virtually inactivates the enzyme, reducing the activity about 1000fold
R109A/K138A
the mutant shows significantly lower activity compared to the wild type enzyme
additional information