Literature summary for 2.1.3.2 extracted from

Ruiz-Ramos, A.; Velazquez-Campoy, A.; Grande-Garcia, A.; Moreno-Morcillo, M.; Ramon-Maiques, S.
Structure and functional characterization of human aspartate transcarbamoylase, the target of the anti-tumoral drug PALA (2016), Structure, 24, 1081-1094 .

Search for more literature for 2.1.3.2

Crystallization (Commentary)

Crystallization (Comment)	Organism
free enzyme and bound to carbamoyl phosphate or N-phosphonacetyl-L-aspartate	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
D1958A	the mutant shows 2.5fold reduced activity compared to the wild type enzyme	Homo sapiens
E1954A	the mutant shows 4fold reduced activity compared to the wild type enzyme	Homo sapiens
R2024Q	the mutation virtually inactivates the enzyme, reducing the activity about 1000fold	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
N-phosphonacetyl-L-aspartate	-	Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P27708	-	-

Purification (Commentary)

Purification (Comment)	Organism
HiTrap heparin column chromatography	Homo sapiens

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
homotrimer	-	Homo sapiens

Synonyms

Synonyms	Comment	Organism
ATCase	-	Homo sapiens
CAD	multienzymatic protein with three functional domains: glutamine-dependent carbamoyl phosphate synthetase, aspartate transcarbamoylase and dihydroorotase	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)