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
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2.1.3.2
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pyrimidine
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dihydroorotase
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ctp
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n-phosphonacetyl-l-aspartate
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trimer
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homotropic
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bisubstrate
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heterotropic
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holoenzyme
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succinate
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orotate
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uridine
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ornithine
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hamster
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uracil
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r-states
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cpsase
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phosphoribosyltransferase
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glutamine-dependent
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carbamylphosphate
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dhoase
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cytidine
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orotidine
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lipscomb
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intersubunit
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changeux
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pyre
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otcase
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syrian
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acivicin
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high-activity
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wheat-germ
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cistron
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unligated
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monod
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trifunctional
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interchain
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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
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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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Subunits
Subunits on EC 2.1.3.2 - aspartate carbamoyltransferase
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dimer
dodecamer
hexamer
homotrimer
tetramer
trimer
additional information
x * 37000 + x * 17000, most probably a dodecamer, SDS-PAGE
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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
dodecamer
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quaternary structural changes during the allosteric transition, overview
dodecamer
the Escherichia coli ATCase holoenzyme is a dodecamer composed of six regulatory chains and six catalytic chains arranged into three regulatory dimers and two catalytic trimers
dodecamer
composed of two catalytic trimers and three regulatory dimers
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3 * 37000, SDS-PAGE, recombinant enzyme with His-tag, 3 * 33557, calculated
trimer
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3 * 33500, SDS-PAGE, sedimemtation equilibrium analysis of protein dissolved in 6 M guanidine hydrochloride
trimer
crystals of the catalytic subunit in an orthorhombic crystal form contain four crystallographically independent trimers which associate in pairs to form stable staggered complexes. Each subunit has a sulfate in the central channel. The catalytic subunits in these complexes show flexibility, with the elbow angles of the monomers differing by up to 7.4° between crystal forms. There is also flexibility in the relative orientation of the trimers around their threefold axis in the complexes, with a difference of 4° between crystal forms
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channeling and transient complex formation between enzyme and carbamoyl phosphate synthetase
additional information
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ATCase and dihydroorotase form a non-covalently bonded complex which probably consists of six polypeptide chains of dihydroorotase and six of ATCase. All the ATCase and dihydroorotase activity in Deinococcus radiophilus occurs in the form of this complex
additional information
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ATCase and dihydroorotase form a non-covalently bonded complex which probably consists of six polypeptide chains of dihydroorotase and six of ATCase. All the ATCase and dihydroorotase activity in Deinococcus radiophilus occurs in the form of this complex
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additional information
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holoenzyme is a dodecamer composed of 2 catalytic trimers and 3 regulatory dimers, the catalytic chain is composed of 2 structural domains, the aspartate domain and the carbamoylphosphate domain which are involved in the binding of aspartate and carbamoylphosphate respectively, the regulatory chain is also composed of 2 domains, the allosteric and the zinc domains, which are involved in the binding of allosteric effectors and zinc
additional information
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characterization of a complex between catalytical and regulatory subunit
additional information
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2 distinct kinds of separable subunits, a catalytically active C subunit of 33000 Da and a regulatory R subunit of 17000 Da, native structure: (C3)2(R2)3 i.e. a dimer of C subunits and a trimer of R subunits
additional information
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quarternary structure and substrate binding-mediated conformational changes analyzed by inelastic neuron scattering using bisubstrate analogue N-(phosphonacetyl)-L-aspartate binding, protein dynamics, overview
additional information
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the larger subunit retains catalytic activity while the smaller subunit exhibits no activity but it contains the nucleotide binding regulatory sites, and three-dimensional and quaternary structure of ATCase, and secondary structure of a regulatory chain and a catalytic chain of ATCase, detailed overview
additional information
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hamster aspartate carbamoyltransferase domain is an oligomer consisting of 2 or 3 identical copies of the 40000 Da proteolytic fragment of CAD, 2 or 3 * 40000, SDS-PAGE
additional information
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dodecameric structure, 2C3:3R2 i.e. 2 trimers of the catalytic subunit and 3 dimers of the regulatory subunit