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
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Metals Ions
Metals Ions on EC 2.1.3.2 - aspartate carbamoyltransferase
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Mg2+
required for synergistic inhibition of the enzyme by CTP and UTP, metal binding site in the allosteric regulatory site of ATCase, overview
Zn2+
Zn2+
-
regulatory subunit contains 6 Zn2+ per 300000 Da protein, Zn2+ may be replaced by Hg2+ or Cd2+
Zn2+
-
the Zn domain, primarily involved in the binding of the zinc cofactor, of the regulatory chain is classified as rubredoxin-like with a metal (zinc or iron) bound that contains usually two CX(n)C motifs