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Literature summary for 2.1.3.2 extracted from

  • Mendes, K.R.; Kantrowitz, E.R.
    The pathway of product release from the R state of aspartate transcarbamoylase (2010), J. Mol. Biol., 401, 940-948.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.3.2

Crystallization (Commentary)

Crystallization (Comment) Organism
ATCase locked in the R quaternary structure by specific introduction of disulfide bonds bound to the final product molecule phosphate, 10 mg/ml protein solution is dialyzed against a solution of 100 mM potassium dihydrogen phosphate and 3 mM sodium azide, pH 5.9, 1 week, X-ray diffraction structure determination and analysis at 2.85 A resolution, molecular replacement Escherichia coli

Protein Variants

Protein Variants Comment Organism
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 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
N-phosphonacetyl-L-aspartate
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate + carbamoyl phosphate Escherichia coli
-
 phosphate + N-carbamoyl-L-aspartate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + carbamoyl phosphate
-
 Escherichia coli phosphate + N-carbamoyl-L-aspartate
-
 ?
L-aspartate + carbamoyl phosphate 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 Escherichia coli phosphate + N-carbamoyl-L-aspartate
-
 ?
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 Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
aspartate transcarbamoylase
-
 Escherichia coli
ATCase
-
 Escherichia coli

General Information

General Information Comment Organism
metabolism ATCase is an allosteric enzyme that catalyzes the committed step of pyrimidine nucleotide biosynthesis Escherichia coli
additional information allosteric and kinetic structures, overview Escherichia coli
physiological function allosteric transition of ATCase, R-state stabilization by disulfide linkages, overview. Wild-type ATCase displays homotropic cooperativity with respect to the second substrate Asp due a shift from the low-activity, low-affinity T state to the high-activity, high-affinity R state Escherichia coli