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Information on EC 2.1.3.2 - aspartate carbamoyltransferase and Organism(s) Aquifex aeolicus and UniProt Accession O66726

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Aquifex aeolicus
UNIPROT: O66726 not found.
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The taxonomic range for the selected organisms is: Aquifex aeolicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
atcase, aspartate transcarbamylase, aspartate transcarbamoylase, aspartate carbamoyltransferase, l-aspartate transcarbamylase, aspartate carbamyltransferase, carbamoyl-phosphate:l-aspartate carbamoyltransferase, l-aspartate transcarbamoylase, aspartate trans carbamoylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aspartate transcarbamoylase
-
(S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase
-
-
-
-
aspartate carbamyltransferase
-
-
-
-
aspartate transcarbamoylase
aspartate transcarbamylase
-
-
-
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aspartic acid transcarbamoylase
-
-
-
-
aspartic carbamyltransferase
-
-
-
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aspartic transcarbamylase
-
-
-
-
ATC domain of CAD
-
-
-
-
ATCase
-
-
-
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carbamoylaspartotranskinase
-
-
-
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carbamoyltransferase, aspartate
-
-
-
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carbamylaspartotranskinase
-
-
-
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L-aspartate transcarbamoylase
-
-
-
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L-aspartate transcarbamylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carbamoyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
carbamoyl-phosphate:L-aspartate carbamoyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9012-49-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.55 - 1.26
Carbamoyl phosphate
1 - 1.12
L-aspartate
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.6 - 41.7
L-aspartate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000000621
N-phosphonacetyl-L-aspartate
-
pH and temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
aspartate transcarbamoylase and dihydroorotase, enzymes that catalyze the second and third step in de novo pyrimidine biosynthesis, are associated in dodecameric complexes in Aquifex aeolicus and many other organisms, intersubunit communication in the dihydroorotase-aspartate transcarbamoylase complex of Aquifex aeolicus, overview. The architecture of the dodecamer is ideally suited to channel the intermediate, carbamoyl aspartate from its site of synthesis on the ATC subunit to the active site of dihydroorotase, which catalyzes the next step in the pathway, because both reactions occur within a large, internal solvent-filled cavity. The apparent second-order rate constant (kcat/Km) of ATC is 7.0fold greater than that of dihydroorotase
additional information
-
the dihydroorotase loop A that binds between the two ATC domains is an allosteric or noncompletive ATC inhibitor with Ki 5 of 0.022 mM, loop A is an important component of the functional linkage between the enzymes. modeling, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
112800
-
gel filtration
33557
-
3 * 37000, SDS-PAGE, recombinant enzyme with His-tag, 3 * 33557, calculated
37000
-
3 * 37000, SDS-PAGE, recombinant enzyme with His-tag, 3 * 33557, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
noncovalent association with dihydroorotase
dodecamer
-
CAD enzyme complex including the aspartate transcarbamoylase. The Aquifex aeolicus DHO-ATC dodecameric complex consists of two trimeric ATC subunits and three DHO dimers. ATC is a trimer consisting of a carbamoyl phosphate binding domain and an aspartate binding domain
trimer
-
3 * 37000, SDS-PAGE, recombinant enzyme with His-tag, 3 * 33557, calculated
additional information
-
channeling and transient complex formation between enzyme and carbamoyl phosphate synthetase
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complex of aspartate transcarbamoylase and dihydroorotase
noncovalent hexamer of dihydroorotase and ATCase, to 2.3 A resolution. The structure has citrate, bound to the active sites of both enzymes.Six DHO and six ATC chains form a hollow dodecamer, in which the 12 active sites face an internal reaction chamber that is approximately 60 A in diameter and connected to the cytosol by narrow tunnels. The entrances and the interior of the chamber are both electropositive, which suggests that the architecture of this nanoreactor modifies the kinetics of the bisynthase, not only by steric channeling but also by preferential escape of the product, dihydroorotase
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
-
stable up to
87
-
5 min, 50% inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain BL21
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Purcarea, C.; Ahuja, A.; Lu, T.; Kovari, L.; Guy, H.I.; Evans, D.R.
Aquifex aeolicus aspartate transcarbamoylase, an enzyme specialized for the efficient utilization of unstable carbamoyl phosphate at elevated temperature
J. Biol. Chem.
278
52924-52934
2003
Aquifex aeolicus
Manually annotated by BRENDA team
Zhang, P.; Martin, P.D.; Purcarea, C.; Vaishnav, A.; Brunzelle, J.S.; Fernando, R.; Guy-Evans, H.I.; Evans, D.R.; Edwards, B.F.
Dihydroorotase from the hyperthermophile Aquifex aeolicus is activated by stoichiometric association with aspartate transcarbamoylase and forms a one-pot reactor for pyrimidine biosynthesis
Biochemistry
48
766-778
2009
Aquifex aeolicus (O66726), Aquifex aeolicus
Manually annotated by BRENDA team
Evans, H.G.; Fernando, R.; Vaishnav, A.; Kotichukkala, M.; Heyl, D.; Hachem, F.; Brunzelle, J.S.; Edwards, B.F.; Evans, D.R.
Intersubunit communication in the dihydroorotase-aspartate transcarbamoylase complex of Aquifex aeolicus
Protein Sci.
23
100-109
2014
Aquifex aeolicus
Manually annotated by BRENDA team