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
-
2.1.3.2
-
pyrimidine
-
dihydroorotase
-
ctp
-
n-phosphonacetyl-l-aspartate
-
trimer
-
homotropic
-
bisubstrate
-
heterotropic
-
holoenzyme
-
succinate
-
orotate
-
uridine
-
ornithine
-
hamster
-
uracil
-
r-states
-
cpsase
-
phosphoribosyltransferase
-
glutamine-dependent
-
carbamylphosphate
-
dhoase
-
cytidine
-
orotidine
-
lipscomb
-
intersubunit
-
changeux
-
pyre
-
otcase
-
syrian
-
acivicin
-
high-activity
-
wheat-germ
-
cistron
-
unligated
-
monod
-
trifunctional
-
interchain
-
dodecameric
- 2.1.3.2
- pyrimidine
- dihydroorotase
- ctp
- n-phosphonacetyl-l-aspartate
- trimer
-
homotropic
-
bisubstrate
-
heterotropic
-
holoenzyme
- succinate
- orotate
- uridine
- ornithine
- hamster
- uracil
-
r-states
- cpsase
- phosphoribosyltransferase
-
glutamine-dependent
- carbamylphosphate
- dhoase
- cytidine
- orotidine
-
lipscomb
-
intersubunit
-
changeux
-
pyre
- otcase
-
syrian
- acivicin
-
high-activity
-
wheat-germ
-
cistron
-
unligated
-
monod
-
trifunctional
-
interchain
-
dodecameric
Reaction
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
Advanced search results
Engineering
Engineering on EC 2.1.3.2 - aspartate carbamoyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
A241C
-
reduced affinity for aspartate, hyperbolic aspartate saturation curve
C47A/A241C
D162A
-
7700fold reduction in specific activity, 2fold decrease in affinity for aspartate, loss of homotropic cooperativity and decreased activation by ATP
D19A
D236A
E239Q
-
mutation in the catalytic subunit, the mutation substantially destabilize the T state of the enzyme
E50A
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
H20A
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
K56A
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
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
R167A
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
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
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
-
non-reducing conditions, reduced affinity for aspartate, hyperbolic aspartate saturation curve
C47A/A241C
-
the mutant holoenzyme with disulfides intact displays a hyperbolic Asp saturation curve confirming the loss of homotropic cooperativity, phosphate binding structure of the mutant, overview
D19A
a regulatory mutant, which does not exhibit UTP synergistic inhibition
-
the small-angle x-ray scattering pattern of unliganded D236A ATCase differs from the scattering pattern of the wild-type enzyme
D236A
-
mutation in the catalytic subunit, the mutation substantially destabilize the T state of the enzyme
D236A
site-directed mutagenesis, the wild-type enzyme shows o change in structure by SAXS through the temperature range of 4°C to 55°C, whereas the D236A ATCase exhibits a large shift toward the T state between 4°C and 30°C, with a minor shift back toward the R state between 30°C and 45°C
-
mutant enzyme shows a low activity, low affinity state, only 2fold activation with N-(phosphonoacetyl)-L-aspartate, kinetic mechanism is changed
E50A
-
shift of equilibrium toward unliganded T-state, crystallization analysis
a regulatory mutant, which does not exhibit UTP synergistic inhibition
H20A
the mutation results in the complete loss of synergistic inhibition by UTP
a regulatory mutant, which does not exhibit UTP synergistic inhibition
K56A
the mutation results in the complete loss of synergistic inhibition by UTP
-
no induction of induced fit by substrates, enzyme is lockd in the low-activity, low affinity T-state
Q137A
-
the concentration of carbamoyl phosphate required to attain one half of the maximal activity increases by 210fold, the corresponding value for aspartate increases by 76fold, extremely reduced affinity for carbamoyl phosphate and near abolition of aspartate binding compared to the wild-type enzyme
in noncovalent association with dihydroorotase, possible model for mammalian polypeptide chain CPSase/ATCase/DHOase during pyrimidine biosynthesis
additional information
-
in noncovalent association with dihydroorotase, possible model for mammalian polypeptide chain CPSase/ATCase/DHOase during pyrimidine biosynthesis
additional information
-
chimeric enzyme consisting of E.coli catalytic subunit and Serratia marcescens regulatory subunit