Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.1.3.2 - aspartate carbamoyltransferase and Organism(s) Homo sapiens and UniProt Accession P27708

for references in articles please use BRENDA:EC2.1.3.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P27708 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Homo sapiens
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, aspartate trans carbamoylase, l-aspartate transcarbamoylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aspartate transcarbamoylase
-
CAD
multienzymatic protein with three functional domains: glutamine-dependent carbamoyl phosphate synthetase, aspartate transcarbamoylase and dihydroorotase
(S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase
-
-
-
-
aspartate carbamyltransferase
-
-
-
-
aspartate transcarbamoylase
aspartate transcarbamylase
-
-
-
-
aspartic acid transcarbamoylase
-
-
-
-
aspartic carbamyltransferase
-
-
-
-
aspartic transcarbamylase
-
-
-
-
ATC domain of CAD
-
-
-
-
ATCase
carbamoylaspartotranskinase
-
-
-
-
carbamoyltransferase, aspartate
-
-
-
-
carbamylaspartotranskinase
-
-
-
-
L-aspartate transcarbamoylase
-
-
-
-
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
-
-
-
?
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
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-phosphonacetyl-L-aspartate
-
N-phosphonoacetyl-L-aspartate
binding structure, overview
4-(3-methyl-2,4,6-trioxo-2,3,4,5,6,11-hexahydro-1H-indeno[2',1':5,6]pyrido[2,3-d]pyrimidin-5-yl)phenyl 2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propanoate
-
-
5-([6-[(2E)-2-([2-[(2,4-dichlorophenyl)methoxy]phenyl]methylidene)hydrazinyl][1,2,5]oxadiazolo[3,4-b]pyrazin-5-yl]amino)-1,3-dihydro-2H-benzimidazol-2-one
-
-
YD19
-
-
YD21
-
-
additional information
-
not inhibited by fluorouracil
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7
Carbamoyl phosphate
-
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0154
4-(3-methyl-2,4,6-trioxo-2,3,4,5,6,11-hexahydro-1H-indeno[2',1':5,6]pyrido[2,3-d]pyrimidin-5-yl)phenyl 2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propanoate
Homo sapiens
-
pH and temperature not specified in the publication
0.0041
5-([6-[(2E)-2-([2-[(2,4-dichlorophenyl)methoxy]phenyl]methylidene)hydrazinyl][1,2,5]oxadiazolo[3,4-b]pyrazin-5-yl]amino)-1,3-dihydro-2H-benzimidazol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
in animals, CPSase, ATCase and DHOase are part of a 243 kDa multifunctional polypeptide named CAD
physiological function
upregulation of CAD, comprising CPSase, ATCase and DHOase activities, is essential for normal and tumour cell proliferation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PYR1_HUMAN
2225
0
242984
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
102000
detagged isolated recombinant enzyme, gel filtration
34800
3 * 34800, detagged isolated recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
free enzyme and bound to carbamoyl phosphate or N-phosphonacetyl-L-aspartate
purified detagged isolated recombinant huATCase, free or in complex with inhibitor N-phosphonoacetyl-L-aspartate, 1.5 mg/ml protein, 0.1 M Tris pH 8.5, 6% PEG 8000, and 9% ethylene glycol is mixed with 0.1 M CAPS pH 10, 150 mM NaCl or 1.5 mg ml1 and 10 mM ZnCl2, 15% PEG 6000, 50 mM sodium acetate pH 4.8, and 0.5 mM inhibitor, X-ray diffraction structure determination and analysis at 2.1 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D1958A
the mutant shows 2.5fold reduced activity compared to the wild type enzyme
E1954A
the mutant shows 4fold reduced activity compared to the wild type enzyme
R2024Q
the mutation virtually inactivates the enzyme, reducing the activity about 1000fold
G128A/G130A
-
the mutant loses almost all activity
G130A
-
the mutant retains some activity
G132A
-
the mutation completely abolishes enzyme activity
G166A
-
the mutant retains some activity
G166P
-
the mutant loses almost all activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap heparin column chromatography
recombinant enzyme from the N-terminal His6-tagged maltose-binding fusion protein CAD complex from Escherichia coli strain BL21(DE3) pLysS cells by ncikel affinity chromatography, ion-exchange chromatography, tag cleavage, and gel filtration. Three extra residues are left at the N-terminus of huATCase (GPM1915SP) after removal of the tag
Ni-NTA column chromatography and Superdex 200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of the enzyme as part of the N-terminal His6-tagged maltose-binding fusion protein CAD complex in Escherichia coli strain BL21(DE3) pLysS cells
expressed in Escherichia coli BL21(DE3) cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ruiz-Ramos, A.; Lallous, N.; Grande-Garcia, A.; Ramon-Maiques, S.
Expression, purification, crystallization and preliminary X-ray diffraction analysis of the aspartate transcarbamoylase domain of human CAD
Acta Crystallogr. Sect. F
69
1425-1430
2013
Homo sapiens (P27708), Homo sapiens
Manually annotated by BRENDA team
Lei, Z.; Wang, B.; Lu, Z.; Wang, N.; Tan, H.; Zheng, J.; Jia, Z.
New regulatory mechanism-based inhibitors of aspartate transcarbamoylase for potential anticancer drug development
FEBS J.
287
3579-3599
2020
Homo sapiens, Escherichia coli (P0A786)
Manually annotated by BRENDA team
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
Structure
24
1081-1094
2016
Homo sapiens (P27708), Homo sapiens
Manually annotated by BRENDA team