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Literature summary for 2.1.3.2 extracted from

  • Liu, L.; Wales, M.E.; Wild, J.R.
    Temperature effects on the allosteric responses of native and chimeric aspartate transcarbamoylases (1998), J. Mol. Biol., 282, 891-901.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
CTP
-
Serratia marcescens

Protein Variants

Protein Variants Comment Organism
additional information chimeric enzyme consisting of E.coli catalytic subunit and Serratia marcescens regulatory subunit Serratia marcescens

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Serratia marcescens
-
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
More
-
Escherichia coli
More dodecameric structure, 2C3:3R2 i.e. 2 trimers of the catalytic subunit and 3 dimers of the regulatory subunit Serratia marcescens