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Information on EC 2.1.3.2 - aspartate carbamoyltransferase
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2.1.3.2 aspartate carbamoyltransferaseSpecify your search results
Word Map
- 2.1.3.2
- pyrimidine
- ctp
- n-phosphonacetyl-l-aspartate
- dihydroorotase
- histone
-
homotropic
-
bisubstrate
-
heterotropic
- succinate
- orotate
- ornithine
- uridine
- uracil
- triphosphate
-
r-states
- phosphoribosyltransferase
- cpsase
- cytidine
- orotidine
- carbamylphosphate
-
lipscomb
-
intersubunit
-
glutamine-dependent
- otcase
-
dodecameric
-
pyre
-
syrian
-
high-activity
-
unligated
-
monod
- acivicin
-
changeux
-
cistron
-
trifunctional
-
rudimentary
-
interchain
-
wheat-germ
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
atcase, aspartate transcarbamylase, aspartate transcarbamoylase, l-aspartate transcarbamylase, aspartate carbamyltransferase, carbamoyl-phosphate:l-aspartate carbamoyltransferase, l-aspartate transcarbamoylase, aspartate trans carbamoylase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase
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-
-
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aspartate carbamyltransferase
-
-
-
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aspartate trans carbamoylase
aspartate transcarbamoylase
aspartate transcarbamylase
aspartic acid transcarbamoylase
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-
-
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aspartic carbamyltransferase
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-
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aspartic transcarbamylase
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-
-
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ATC
ATC domain of CAD
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-
-
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ATCase
carbamoylaspartotranskinase
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-
-
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carbamoyltransferase, aspartate
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-
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carbamylaspartotranskinase
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L-aspartate transcarbamoylase
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-
-
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L-aspartate transcarbamylase
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-
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aspartate transcarbamoylase
-
-
-
-
aspartate transcarbamoylase
-
-
aspartate transcarbamylase
-
-
-
-
ATCase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
Pseudomonas vulgaris
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
enzyme exhibits homotropic cooperativity for aspartate, is heterotropically activated by ATP and is heterotropically inhibited by CTP and UTP; reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction proceeds via a nucleophilic attack by the free amino group of L-aspartate on the carbon of carbamoylphosphate
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
kinetic data suggest an ordered bi bi mechanism; reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
enzyme exhibits homotropic cooperativity for aspartate, is heterotropically activated by ATP and is heterotropically inhibited by CTP and UTP
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
significant role of protein-solvent interactions in regulatory conformational changes
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
cooperative mechanism of substrate binding
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
allosteric enzyme, in absence of effectors, two-state, concerted transition model
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
ordered substrate binding with induced fit
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
catalytic and regulatory mechanisms, overview. The enzyme undergoes as it shifts between its low-activity, low-affinity form, T state, to its high-activity, high-affinity form, R state, and allosteric effectors modulate the activity. The ATCase-catalyzed reaction is regulated by nucleotide binding some 60 A from the active site, inducing structural alterations that modulate catalytic activity. The catalytic mechanism is ordered, carbamoyl phosphate binds before aspartate, and carbamoyl aspartate leaves before phosphate. Cooperativity is induced by aspartate binding
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
ATCase follows an ordered Bi Bi reaction mechanism in which carbamoyl phosphate must bind before L-aspartate and the product N-carbamoyl-L-aspartate leaves the active site before inorganic phosphate
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
the catalytic cycle of ATCase leads from the ordered binding of the substrates to the formation and decomposition of the tetrahedral intermediate and to the ordered release of the products from the active site, ordered-binding mechanism, detailed overview
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carbamoyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
carbamoyl-phosphate:L-aspartate carbamoyltransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9012-49-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
carbamoyl phosphate + L-asparagine
phosphate + N-carbamoyl-L-asparagine
-
the enzyme catalyzes the carbamoylation of L-Asn with a Km of 122 mM and a maximal velocity 10fold lower than observed with the natural substrate, L-Asp. As opposed to L-Asp, no cooperativity is observed with respect to L-Asn
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
the enzyme catalyzes the first committed step in pyrimidine biosynthesis
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
substrate binding causes significant conformational changes
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
Arg229, which interacts with the beta-carboxylate of L-Asp, plays a critical role in the orientation of L-Asp in the active site and demonstrates the requirement of the beta-carboxylate of L-Asp in the mechanism of domain closure and the allosteric transition in Escherichia coli ATCase
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
upon substrate binding, allosteric Escherichia coli aspartate transcarbamoylase adopts alternate quaternary structures, stabilized by a set of interdomain and intersubunit interactions, which are readily differentiated by their solution x-ray scattering curves. The cooperative binding of aspartate in aspartate transcarbamoylase appears to result from the combination of the preexisting quaternary structure equilibrium with local changes induced by binding of carbamoyl phosphate
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
the enzyme catalyzes the first step in the pyrimidine biosynthetic pathway
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
the enzyme catalyzes the first step in the pyrimidine biosynthetic pathway
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
Pseudomonas vulgaris
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs. The interaction of carbamoyl-phosphate synthetase/aspartate transcarbamoylase is demonstrated by the unexpectedly weak inhibition of the coupled reaction by the bisubstrate analog, N-(phosphonacetyl)-L-aspartate. In the coupled reaction, the effective concentration of carbamoyl phosphate in the vicinity of the aspartate transcarbamoylase active site is 96fold higher than the concentration in the bulk phase. Channeling probably plays an essential role in protecting this very unstable intermediate of metabolic pathways performing at extreme temperatures
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
specific for L-aspartate
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
second enzyme of pyrimidine synthesis
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
catalyzes the formation of carbamoyl-L-aspartate, the first compound unique to the biosynthetic pathway for pyrimidine nucleotides
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
catalyzes the formation of carbamoyl-L-aspartate, the first compound unique to the biosynthetic pathway for pyrimidine nucleotides
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
Pseudomonas vulgaris
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
carbamoyl phosphate binding structure, in silico docking and electrostatic calculations, overview
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
-
i.e. ureidosuccinic acid
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
ATCase displays ordered substrate binding and product release, remaining in the R state until substrates are exhausted. Wild-type ATCase is in a T-state structure with bound product phosphate
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
additional information
?
-
-
CAD is a rate-limiting enzyme required for the formation of UDP sugar, upstream of two different metabolic pathways; the de novo biosynthesis of pyrimidine and pyrimide-based nucleotides, and the formation of UDP sugar intermediates, required for UDP-dependent glycosylation events
-
-
-
additional information
?
-
-
the allosteric enzyme shows homotropic cooperative interactions between the catalytic sites for the binding of aspartate due to a quarternary structure transition between high aspartate affinity T state and R state
-
-
-
additional information
?
-
-
concerted transition between structural and functional states of either low affinity, low activity or high affinity, high activity for aspartate. Addition of ATP along with the substrates increases the rate of the transition from the T to the R state and also decreases the duration of the R-state steady-state phase. Addition of CTP or the combination of CTP/UTP to the substrates significantly decreases the rate of the T-R transition and causes a shift in the enzyme population towards the T state even at saturating substrate concentrations
-
-
-
additional information
?
-
-
conformational changes due to nucleotide binding, overview
-
-
-
additional information
?
-
-
in the structure of the enzyme trapped in the R state with specific disulfide bonds, two phosphate molecules are bound per active site. The position of the first phosphate corresponds to the position of the phosphate of carbamoyl phosphate and the position of the phosphonate of inhibitor N-phosphonacetyl-L-aspartate. However, the second, more weakly bound phosphate is bound in a positively charged pocket that is more accessible to the surface than the other phosphate. The second phosphate appears to be on the path that phosphate would have to take to exit the active site
-
-
-
additional information
?
-
-
link between enzyme activity and gametogenesis
-
-
-
additional information
?
-
-
ACT-DHOD gene is transcribed to ACT-DHOD mRNA, translated to the single protein, ACT-DHOD, and finally converted to mature independent DHOD and ACT
-
-
-
additional information
?
-
-
direct intermolecular interactions between the enzymes catalyzing the first three reaction steps of the de novo pyrimidine biosynthetic pathway, carbamoylphosphate synthetase II (CPSII), aspartate transcarbamoylase (ATC), and dihydroorotase (DHO), of the parasitic protist Trypanosoma cruzi, interaction analysis, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
P0A786
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
the enzyme catalyzes the first committed step in pyrimidine biosynthesis
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
the enzyme catalyzes the first step in the pyrimidine biosynthetic pathway
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
Q58976
the enzyme catalyzes the first step in the pyrimidine biosynthetic pathway
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs. The interaction of carbamoyl-phosphate synthetase/aspartate transcarbamoylase is demonstrated by the unexpectedly weak inhibition of the coupled reaction by the bisubstrate analog, N-(phosphonacetyl)-L-aspartate. In the coupled reaction, the effective concentration of carbamoyl phosphate in the vicinity of the aspartate transcarbamoylase active site is 96fold higher than the concentration in the bulk phase. Channeling probably plays an essential role in protecting this very unstable intermediate of metabolic pathways performing at extreme temperatures
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
Q5SK66
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q5SK66
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
second enzyme of pyrimidine synthesis
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
P0A786
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
catalyzes the formation of carbamoyl-L-aspartate, the first compound unique to the biosynthetic pathway for pyrimidine nucleotides
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
catalyzes the formation of carbamoyl-L-aspartate, the first compound unique to the biosynthetic pathway for pyrimidine nucleotides
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
Q58976
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
Pseudomonas vulgaris
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
P77918
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
Q55338
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
P05654
-
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
-
i.e. ureidosuccinic acid
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
Q58801, Q58976
-
-
-
?
additional information
?
-
-
CAD is a rate-limiting enzyme required for the formation of UDP sugar, upstream of two different metabolic pathways; the de novo biosynthesis of pyrimidine and pyrimide-based nucleotides, and the formation of UDP sugar intermediates, required for UDP-dependent glycosylation events
-
-
-
additional information
?
-
-
link between enzyme activity and gametogenesis
-
-
-
additional information
?
-
-
ACT-DHOD gene is transcribed to ACT-DHOD mRNA, translated to the single protein, ACT-DHOD, and finally converted to mature independent DHOD and ACT
-
-
-
additional information
?
-
-
direct intermolecular interactions between the enzymes catalyzing the first three reaction steps of the de novo pyrimidine biosynthetic pathway, carbamoylphosphate synthetase II (CPSII), aspartate transcarbamoylase (ATC), and dihydroorotase (DHO), of the parasitic protist Trypanosoma cruzi, interaction analysis, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-2-(([hydroxy(hydroxymethyl)phosphoryl]acetyl)amino)butanedioic acid
-
competitive
(2S)-2-(([hydroxy(oxido)-lambda5-phosphanyl]acetyl)amino)butanedioic acid
-
competitive
2-(4-hydroxy-2,4-dioxo-4lamdba5-[1,4]azaphosphinan-1-yl)-succinic acid
-
competitive
2-phenyl-1,3-4(H)benzothiazin-4-thione
-
noncompetitive inhibitor towards both aspartate and carbamoyl phosphate
ATP
-
dual regulatory pattern, activating the enzyme at low concentrations and inhibiting it in the mM range
ATP
inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated
carbamoyl aspartate
-
noncompetitive vs. carbamoyl phosphate and aspartate
CTP
-
CTP inhibits ATCase activity. Experimentally driven, statistical modeling approach (high-dimensional model representation, RS-HDMR) to investigate regulation of ATCase in response to varying concentrations of its nucleotide regulators ATP, CTP, GTP, and UTP (at fixed substrate concentrations)
CTP
-
addition of CTP or the combination of CTP/UTP to the substrates significantly decreases the rate of the low activity-high activity T-R transition and causes a shift in the enzymepopulation towards the T state even at saturating substrate concentrations
CTP
-
ATCase is feedback inhibited by CTP and synergistically by the combination of CTP plus UTP
CTP
-
aspartate transcarbamoylase is feedback inhibited by CTP in the presence of CTP. CTP and UTP do not bind competitively, CTP binding structure, overview
CTP
-
demetaled CTP, synergistic inhibition with UTP, while UTP alone has little or no influence on the enzyme activity, mechanism, overview. Binding of UTP can enhance the binding of CTP and presence of a metal ion such as Mg2+ is required for synergistic inhibition. Structure of the ATCase-CTP-UTP-Mg2+ complex
CTP
inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated
GTP
-
GTP inhibits ATCase activity. Experimentally driven, statistical modeling approach (high-dimensional model representation, RS-HDMR) to investigate regulation of ATCase in response to varying concentrations of its nucleotide regulators ATP, CTP, GTP, and UTP (at fixed substrate concentrations)
GTP
inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated
N-(phosphonacetyl)-L-aspartate
-
treatment of seedling with 1 mM, results in delayed germination, inhibition of cotyledon expansion, leaf development and root growth. 2fold increase in enzyme activity and protein level
N-(phosphonacetyl)-L-aspartate
-
there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs. The interaction of carbamoyl-phosphate synthetase/aspartate transcarbamoylase is demonstrated by the unexpectedly weak inhibition of the coupled reaction by the bisubstrate analog, N-(phosphonacetyl)-L-aspartate
N-(Phosphonoacetyl)-L-aspartate
-
0.011 mM, 50% inhibition, low concentrations activate
N-(Phosphonoacetyl)-L-aspartate
-
0.002 mM, 50% inhibition of catalytic subunit
N-(Phosphonoacetyl)-L-aspartate
-
competitive vs. carbamoyl phosphate, noncompetitive vs. aspartate
N-phosphonacetyl-L-aspartate
-
binding of the bisubstrate analogue N-phosphonacetyl-L-aspartate to the aspartate transcarbamoylase subunit inhibits the activity of the distal dihydroorotase subunit
N-phosphonacetyl-L-aspartate
a bisubstrate/transition state analogue, binding structure, in silico docking and electrostatic calculations, overview
N-phosphonacetyl-L-aspartate
-
PALA, a bisubstrate transition state analogue, and shows also ability of PALA to enhance the activity of ATCase at low concentrations of aspartate, in the presence of a saturating concentration of carbamoyl phosphat. Interactions between the side chain of Gln137 and the backbone carbonyl oxygen of Pro266 to the amino group on the tetrahedral carbon and the side chain of Arg54 with the ester oxygen between the phosphorus and the tetrahedral carbone
N-phosphonacetyl-L-aspartate
-
i.e. PALA, a bisubstrate analogue, the binding of PALA is able to stabilize the enzyme in the high-activity, high-affinity R state because its structure mimics the reaction's transition state structure. The concerted transition to the R state allows a majority of active sites free to react with substrates and release products while a minority of active sites bound with PALA are inactive but stabilize the enzyme in the R state. Therefore, at low concentrations of PALA the activity increases; however, as the concentration of PALA is increased more and more of the active sites are filled by the non-hydrolyzable bisubstrate analog and the activity drops. At high concentrations of Asp and a saturating concentration of carbamoyl phosphate, no PALA activation is observed. In the absence of allosteric effectors the average KD of PALA is 110 nM, decreasing to 65 nM in the presence of ATP and increasing to 266 nM in the presence of CTP
N-phosphonoacetyl-L-aspartate
-
after addition of N-phosphonacetyl-L-aspartate to the enzyme, the transition rate is more than 1 order of magnitude slower than with the natural substrates
phosphate
-
competitive vs. carbamoyl phosphate, noncompetitive vs. aspartate
succinate
-
activator at low concentrations of both succinate and aspartate, inhibitor at high succinate concentrations and at high aspartate concentrations
UMP
-
0.1 mM, 25% inhibition, inhibition increases to 80% and 90% in the presence of 0.2 mM and 0.6 mM deoxycholate respectively
UMP
-
fatty acids with chains of C8 or longer, dodecylsulfate and decylsulfonate potentiate inhibition
UTP
-
synergistic inhibition by CTP and UTP, no inhibition unless CTP is present
UTP
-
UTP inhibits ATCase activity. Experimentally driven, statistical modeling approach (high-dimensional model representation, RS-HDMR) to investigate regulation of ATCase in response to varying concentrations of its nucleotide regulators ATP, CTP, GTP, and UTP (at fixed substrate concentrations)
UTP
-
addition of CTP or the combination of CTP/UTP to the substrates significantly decreases the rate of the low activity-high activity T-R transition and causes a shift in the enzymepopulation towards the T state even at saturating substrate concentrations
UTP
-
aspartate transcarbamoylase is feedback inhibited by UTP in the presence of CTP. UTP binds to a unique site on each regulatory chain of the enzyme that is near but not overlapping with the known CTP site. CTP and UTP do not bind competitively, UTP binds to the r6 regulatory chain of ATCase, UTP binding structure, overview
UTP
-
inhibition with CTP, while UTP alone has little or no influence on the enzyme activity, mechanism, overview. UTP, in the presence of dCTP or CTP, binds at a site on a regulatory side chain that does not overlap the CTP/dCTP site, and the triphosphates of the two nucleotides are parallel to each other with a metal ion, in this case Mg2+, coordinated between the beta- and gamma-phosphates of the two nucleotides. UTP binds more tightly in the presence of CTP. Structure of the ATCase-CTP-UTP-Mg2+ complex
UTP
UTP is able to synergistically inhibit ATCase in the presence of CTP, but UTP alone has little or no influence on activity
UTP
inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated
additional information
-
conformational changes due to nucleotide binding, overview
-
additional information
CTP and dCTP bind in a very similar fashion, UTP, in the presence of dCTP or CTP, binds at a site that does not overlap the CTP/dCTP site, and the triphosphates of the two nucleotides are parallel to each other with a metal ion, in this case Mg2+, coordinated between the beta- and gamma-phosphates of the two nucleotides, synergistic Inhibition of ATCase by CTP and UTP is metal-dependent, Mg2+ and Mn2+ act best, binding structures, overview
-
additional information
-
50% inhibition at 80 MPa; not inhibited by phosphonoacetate, diphosphate or phosphate
-
additional information
-
kinetic analysis of properties of allosteric effectors alone and in combination with each other
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-malate
-
activation in presence of excess carbamoyl phosphate and limiting L-aspartate
mesotartrate
-
activation in presence of excess carbamoyl phosphate and limiting L-aspartate
ATP
-
allosteric effector, increases the apparent rate of unliganded T-state to substrate-bound R-state
ATP
-
ATP enhances ATCase activity. Experimentally driven, statistical modeling approach (high-dimensional model representation, RS-HDMR) to investigate regulation of ATCase in response to varying concentrations of its nucleotide regulators ATP, CTP, GTP, and UTP (at fixed substrate concentrations)
ATP
-
addition of ATP along with the substrates increases the rate of the transition from the low activity T to the high activity R state and also decreases the duration of the R-state steady-state phase
ATP
-
the effects of binding of nucleotides are monitored in a series of 1H-13C methyl TROSY spectroscopy spectra recorded on the 300 kDa aspartate transcarbamoylase holoenzyme in both the absence and the presence of saturating amounts of ATP or CTP. No changes in shifts of methyl probes of the catalytic chains that include the active sites are observed, consistent with a lack of structural changes. Results indicate that the mechanism of action of ATP and CTP can be explained fully by the Monod-Wyman-Changeux model
ATP
-
dual regulatory pattern, activating the enzyme at low concentrations and inhibiting it in the mM range
CTP
-
allosteric effector, slightly shifts the dynamical equilibrium during steady state toward unliganded T-state
CTP
-
the effects of binding of nucleotides are monitored in a series of 1H-13C methyl TROSY spectroscopy spectra recorded on the 300 kDa aspartate transcarbamoylase holoenzyme in both the absence and the presence of saturating amounts of ATP or CTP. No changes in shifts of methyl probes of the catalytic chains that include the active sites are observed, consistent with a lack of structural changes. Results indicate that the mechanism of action of ATP and CTP can be explained fully by the Monod-Wyman-Changeux model
N-(Phosphonoacetyl)-L-aspartate
-
at concentrations below 0.000002 mM, inhibition above
N-phosphonacetyl-L-aspartate
-
PALA, a bisubstrate transition state analogue, and shows also ability of PALA to enhance the activity of ATCase at low concentrations of aspartate, in the presence of a saturating concentration of carbamoyl phosphate. Interactions between the side chain of Gln137 and the backbone carbonyl oxygen of Pro266 to the amino group on the tetrahedral carbon and the side chain of Arg54 with the ester oxygen between the phosphorus and the tetrahedral carbon
N-phosphonacetyl-L-aspartate
-
i.e. PALA, a bisubstrate analogue, the binding of PALA is able to stabilize the enzyme in the high-activity, high-affinity R state because its structure mimics the reaction's transition state structure. The concerted transition to the R state allows a majority of active sites free to react with substrates and release products while a minority of active sites bound with PALA are inactive but stabilize the enzyme in the R state. Therefore, at low concentrations of PALA the activity increases; however, as the concentration of PALA is increased more and more of the active sites are filled by the non-hydrolyzable bisubstrate analog and the activity drops. At high concentrations of Asp and a saturating concentration of carbamoyl phosphate, no PALA activation is observed
succinate
-
activation in presence of excess carbamoyl phosphate and limiting L-aspartate
succinate
-
low concentrations, 35% activation in the presence of 2 mM aspartate
additional information
-
activity is not regulated by nucleotide triphosphates
-
additional information
-
every type of anion tested, including ATP and CTP can stimulate the reaction to a certain extent
-
additional information
-
at high aspartate levels addition of an activator has no effect
-
additional information
-
kinetic analysis of properties of allosteric effectors alone and in combination with each other
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alzheimer Disease
Increasing Tip60 HAT levels rescues axonal transport defects and associated behavioral phenotypes in a Drosophila Alzheimer's disease model.
Alzheimer Disease
Tip60 HAT Activity Mediates APP Induced Lethality and Apoptotic Cell Death in the CNS of a Drosophila Alzheimer's Disease Model.
Anemia, Hypochromic
Mode of Action of the Toxin from Pseudomonas phaseolicola: I. Toxin Specificity, Chlorosis, and Ornithine Accumulation.
Anemia, Hypoplastic, Congenital
Elevation of pyrimidine enzyme activities in the RBC of patients with congenital hypoplastic anaemia and their parents.
Brain Neoplasms
Pyrimidine pathways enzymes in human tumors of brain and associated tissues: potentialities for the therapeutic use of N-(phosphonacetyl-L-aspartate and 1-beta-D-arabinofuranosylcytosine.
Breast Neoplasms
Fe65 Suppresses Breast Cancer Cell Migration and Invasion through Tip60 Mediated Cortactin Acetylation.
Breast Neoplasms
TIP60 Histone Acetyltransferase in Adipose Tissue: Possible Linkages with Breast Cancer Development?
Breast Neoplasms
TIP60: an actor in acetylation of H3K4 and tumor development in breast cancer.
Carcinogenesis
Exciting History of Tip60 and Its Companions in Carcinogenesis Across the Heterochromatin Landscapes.
Carcinogenesis
The acetyltransferase Tip60 contributes to mammary tumorigenesis by modulating DNA repair.
Carcinoma
The effects of pH and inhibitors upon the catalytic activity of the dihydroorotase of multienzymatic protein pyr1-3 from mouse Ehrlich ascites carcinoma.
Carcinoma, Ehrlich Tumor
Binding of radiolabeled N-(phosphonacetyl)-L-aspartate to aspartate transcarbamylase from Ehrlich ascites tumor cells.
Carcinoma, Hepatocellular
A multienzyme complex of carbamoyl-phosphate synthase (glutamine): aspartate carbamoyltransferase: dihydoorotase (rat ascites hepatoma cells and rat liver).
Carcinoma, Hepatocellular
Aspartate carbamoyltransferase inhibition and uridylate trapping result in a synergistic depression of uridine triphosphate in hepatoma cells.
Carcinoma, Hepatocellular
Feedback inhibition of aspartate transcarbamylase in liver and in hepatoma.
Carcinoma, Hepatocellular
Phosphorylation and dephosphorylation of carbamoyl-phosphate synthetase II complex of rat ascites hepatoma cells.
Carcinoma, Hepatocellular
Purification of homogeneous glutamine-dependent carbamyl phosphate synthetase from ascites hepatoma cells as a complex with aspartate transcarbamylase and dihydroorotase.
Cholangiocarcinoma
Tip60 Suppresses Cholangiocarcinoma Proliferation and Metastasis via PI3k-AKT.
Colonic Neoplasms
Phase II trial of N-(phosphonacetyl)-L-aspartate (PALA), 5-fluorouracil and recombinant interferon-alpha-2b in patients with advanced gastric carcinoma.
Colorectal Neoplasms
Down-regulation of Tip60 gene as a potential marker for the malignancy of colorectal cancer.
Fanconi Anemia
Tip60 Is Required for DNA Interstrand Cross-link Repair in the Fanconi Anemia Pathway.
Glioblastoma
Tip60 regulates MT1-MMP transcription and invasion of glioblastoma cells through NF-?B pathway.
Herpes Simplex
A continuous spectrophotometric assay for aspartate transcarbamylase and ATPases.
Hypothyroidism
Effect of hypothyroidism on aspartate transcarbamylase, uridine kinase, and DNA biosynthesis during cerebellar development in the rat.
hypoxanthine phosphoribosyltransferase deficiency
Elevated aspartate transcarbamylase and dihydroorotase activities in erythrocytes from patients with hypoxanthine guanine phosphoribosyltransferase deficiency.
Infection
Activity of some hepatic enzymes in schistosomiasis and concomitant alteration of arylsulfatase B.
Influenza, Human
Histone acetyl transferase TIP60 inhibits the replication of influenza a virus by activation the TBK1-IRF3 pathway.
Lesch-Nyhan Syndrome
Elevated aspartate transcarbamylase and dihydroorotase activities in erythrocytes from patients with hypoxanthine guanine phosphoribosyltransferase deficiency.
Leukemia
Inhibition of cell growth by N-(phosphonacetyl)-L-aspartate in human and murine cells in vitro.
Liver Neoplasms
Acetylation of TIP60 at K104 is essential for metabolic stress-induced apoptosis in cells of hepatocellular cancer.
Melanoma
Inhibition of cell growth by N-(phosphonacetyl)-L-aspartate in human and murine cells in vitro.
Melanoma
Kinetic parameters of aspartate transcarbamylase in human normal and tumoral cell lines.
Melanoma, Experimental
Inhibition of cell growth by N-(phosphonacetyl)-L-aspartate in human and murine cells in vitro.
Mycoses
The Asc locus for resistance to Alternaria stem canker in tomato does not encode the enzyme aspartate carbamoyltransferase.
Myocardial Infarction
Further heterogeneity demonstrated for serum creatine kinase isoenzyme MM.
Neoplasm Metastasis
Role of Tip60 in Human Melanoma Cell Migration, Metastasis, and Patient Survival.
Neoplasm Metastasis
TIP60 inhibits metastasis by ablating DNMT1-SNAIL2-driven epithelial-mesenchymal transition program.
Neoplasm Metastasis
Tip60 Suppresses Cholangiocarcinoma Proliferation and Metastasis via PI3k-AKT.
Neoplasm Metastasis
Transcriptional regulation of a metastasis suppressor gene by Tip60 and beta-catenin complexes.
Neoplasms
Activity of aspartate transcarbamylase in mammary tumours induced by 7,12-dimethyl-benzanthracene in the rat.
Neoplasms
Binding of radiolabeled N-(phosphonacetyl)-L-aspartate to aspartate transcarbamylase from Ehrlich ascites tumor cells.
Neoplasms
Diversion of aspartate in ASS1-deficient tumours fosters de novo pyrimidine synthesis.
Neoplasms
Down-regulation of Tip60 gene as a potential marker for the malignancy of colorectal cancer.
Neoplasms
E3 ligase EDD1/UBR5 is utilized by the HPV E6 oncogene to destabilize tumor suppressor TIP60.
Neoplasms
Effects of N-(phosphonacetyl)-L-aspartate on murine tumors and normal tissues in vivo and in vitro and the relationship of sensitivity to rate of proliferation and level of aspartate transcarbamylase.
Neoplasms
Flux through the de novo pyrimidine pathway in vivo. Effect of N-phosphonacetyl-L-aspartate, a potent inhibitor of aspartate transcarbamylase.
Neoplasms
Histone H3 methylation links DNA damage detection to activation of the tumour suppressor Tip60.
Neoplasms
Increased incidence of CAD gene amplification in tumorigenic rat lines as an indicator of genomic instability of neoplastic cells.
Neoplasms
Inhibition of Tip60 Reduces Lytic and Latent Gene Expression of Kaposi's Sarcoma-Associated Herpes Virus (KSHV) and Proliferation of KSHV-Infected Tumor Cells.
Neoplasms
Mechanisms of sensitivity or resistance of murine tumors to N-(phosphonacetyl)-L-aspartate (PALA).
Neoplasms
N-(Phosphonacetyl)-L-aspartate inhibition of the enzyme complex of pyrimidine biosynthesis.
Neoplasms
Pyrimidine pathways enzymes in human tumors of brain and associated tissues: potentialities for the therapeutic use of N-(phosphonacetyl-L-aspartate and 1-beta-D-arabinofuranosylcytosine.
Neoplasms
Tip60 is a haplo-insufficient tumour suppressor required for an oncogene-induced DNA damage response.
Neoplasms
Tip60 Protein Isoforms and Altered Function in Skin and Tumors that Overexpress Ornithine Decarboxylase.
Neoplasms
Urea Cycle Dysregulation Generates Clinically Relevant Genomic and Biochemical Signatures.
ornithine carbamoyltransferase deficiency
Expression, purification and kinetic characterization of wild-type human ornithine transcarbamylase and a recurrent mutant that produces 'late onset' hyperammonaemia.
Ornithine Carbamoyltransferase Deficiency Disease
Expression, purification and kinetic characterization of wild-type human ornithine transcarbamylase and a recurrent mutant that produces 'late onset' hyperammonaemia.
Pre-Eclampsia
Insulin-like growth factor binding protein-1 at the maternal-fetal interface and insulin-like growth factor-I, insulin-like growth factor-II, and insulin-like growth factor binding protein-1 in the circulation of women with severe preeclampsia.
Prostatic Neoplasms
Characterisation of a Tip60 specific inhibitor, NU9056, in prostate cancer.
Prostatic Neoplasms
Expression of Tip60, an androgen receptor coactivator, and its role in prostate cancer development.
Prostatic Neoplasms
Tip60 is associated with resistance to X-ray irradiation in prostate cancer.
Prostatic Neoplasms
Tip60 promotes prostate cancer cell proliferation by translocation of androgen receptor into the nucleus.
Sarcoma, Yoshida
Intracellular distribution of various enzymes concerned with DNA synthesis from normal and regenerating rat liver, and Yoshida sarcoma.
Spinocerebellar Ataxias
Partial Loss of Tip60 Slows Midstage Neurodegeneration in a Spinocerebellar Ataxia Type 1 (SCA1) Mouse Model.
Starvation
19F nuclear magnetic resonance studies of fluorotyrosine-labeled aspartate transcarbamoylase. Properties of the enzyme and its catalytic and regulatory subunits.
Starvation
Characterization of a Salmonella typhimurium mutant defective in phosphoribosylpyrophosphate synthetase.
Starvation
Effects of phosphate limitation on expression of genes involved in pyrimidine synthesis and salvaging in Arabidopsis.
Starvation
The Escherichia coli K-12 "wild types" W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels.
Urinary Bladder Neoplasms
Expression of TIP60 (tat-interactive protein) and MRE11 (meiotic recombination 11 homolog) predict treatment-specific outcome of localised invasive bladder cancer.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
Carbamoyl phosphate
-
multienzyme complex and aspartate transcarbamoylase activity domain of the multienzyme complex alone
0.021
L-aspartate
-
aspartate transcarbamoylase activity domain of the multienzyme complex alone
additional information
additional information
-
sigmoidal saturation curve for carbamoylphosphate and aspartate
-
additional information
additional information
-
enzyme exhibits Michaelis-Menten kinetics for both of its substrates
-
additional information
additional information
sigmoidal saturation curve for aspartate
-
additional information
additional information
-
sigmoidal saturation curve for aspartate
-
additional information
additional information
-
study of enzyme kinetics under high pressure, in presence of low concentration of L-aspartate, pressure promotes the transition to R-state
-
additional information
additional information
-
the allosteric enzyme shows homotropic cooperative interactions between the catalytic sites for the binding of aspartate, neuron scattering, protein dynamics, overview
-
additional information
additional information
-
the saturation curve is cooperative exhibiting a pH dependent Hill coefficient, cooperative kinetics, modeling with the enzyme being in a dynamic equilibrium between a low-activity, low-affinity T state and a high-activity, high-affinity R state
-
additional information
additional information
-
aspartate transcarbamoylase is an allosteric enzyme, quaternary structural changes during the allosteric transition, and kinetics of the allosteric transition, overview
-
additional information
additional information
-
allosteric mechanism with metal ion involvement, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
79.7
aspartate
-
aspartate transcarbamoylase activity domain of the multienzyme complex
35.9
Carbamoyl phosphate
-
aspartate transcarbamoylase activity domain of the multienzyme complex
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000193
(2S)-2-(([hydroxy(hydroxymethyl)phosphoryl]acetyl)amino)butanedioic acid
-
-
0.000417
(2S)-2-(([hydroxy(oxido)-lambda5-phosphanyl]acetyl)amino)butanedioic acid
-
-
0.001
2-(4-hydroxy-2,4-dioxo-4lamdba5-[1,4]azaphosphinan-1-yl)-succinic acid
-
catalytic subunit of aspartate transcarbamoylase
0.00021
N-(2-hydroxy-acetyl)-L-aspartic acid-phosphate
-
catalytic subunit of aspartate transcarbamoylase
0.000000621
N-phosphonacetyl-L-aspartate
-
pH and temperature not specified in the publication
additional information
additional information
-
Ki-values at varying concentrations of Asp and carbamoyl phosphate
-
4.59
L-aspartate
-
aspartate transcarbamoylase activity domain of the multienzyme complex
7.9
L-aspartate
-
substrate inhibition, complex of catalytic and regulatory subunits, C3R6
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
specific activity of the catalytic subunit alone is about 50% higher than that of the holoenzyme
additional information
-
highest activity in Tris-HCl buffer, followed by Tris-acetate EDTA, glycine sodium and cacodylate buffer
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.5
10.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 75
-
approx. 70% of maximal activity at 30°C, approx. 30% of maximal activity at 75°C
additional information
-
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
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; in noncovalent association with dihydroorotase, possible model for the mammalian polypeptide chain CPSase/ATCase/DHOase during pyrimidine biosynthesis
UniProt
brenda
-
485835, 485837, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485845, 485846, 485853, 485870, 485871, 485872, 485874, 485877, 485881, 485882, 485884, 485885, 661140, 661272, 661450, 662222, 662627, 662646, 662651, 672392, 684138, 685252, 685568, 688367, 689777, 689963, 689977, 696699, 696763, 698488, 699559, 699578, 700959, 718458, 718699, 720245
-
-
brenda