2.1.3.2: aspartate carbamoyltransferase

This is an abbreviated version!
For detailed information about aspartate carbamoyltransferase, go to the full flat file.

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

ECTree

     2 Transferases

         2.1 Transferring one-carbon groups

             2.1.3 Carboxy- and carbamoyltransferases

                2.1.3.2 aspartate carbamoyltransferase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
60	Activating Compound
42879	AA Sequence
1	CAS Registry Number
28	Cloned(Commentary)
4	Cofactor
41	Crystallization (Commentary)
125	Disease/ Diagnostics
33	General Information
13	General Stability
18	IC50 Value
253	Inhibitors
66	Ki Value [mM]
77	KM Value [mM]
4	Localization
5	Metals/Ions
61	Molecular Weight [Da]
113	Natural Substrates/ Products (Substrates)
162	Organism
8	Pathway
316	PDB ID
24	pH Optimum
2	pH Range
3	pH Stability
1	Posttranslational Modification
61	Protein Variants
46	Purification (Commentary)
38	Reaction
2	Reaction Type
161	Reference
3	Renatured (Commentary)
36	Source Tissue
40	Specific Activity [micromol/min/mg]
9	Storage Stability
224	Substrates and Products (Substrate)
49	Subunits
104	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
3	Temperature Range [°C]
29	Temperature Stability [°C]
8	Turnover Number [1/s]

Reaction

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Reaction on EC 2.1.3.2 - aspartate carbamoyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide show all columns Go to Reaction Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

31 entries

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Salmonella enterica subsp. enterica serovar Typhimurium

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Vigna radiata var. radiata

-

485837, 485856, 485863

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Bacillus subtilis

-

485837, 485857

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Mus musculus

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Escherichia coli

-

485837, 485838

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Rattus norvegicus

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Saccharomyces cerevisiae

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Triticum aestivum

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Oryctolagus cuniculus

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Neurospora crassa

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Pseudomonas fluorescens

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Klebsiella aerogenes

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Pseudomonas aeruginosa

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Halobacterium salinarum

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Serratia marcescens

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Enterococcus faecalis

-

485837, 485858, 485861

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Azotobacter vinelandii

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Lactuca sativa

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Citrobacter freundii

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction mechanism

Pseudomonas vulgaris

-

485837

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

reaction proceeds via a nucleophilic attack by the free amino group of L-aspartate on the carbon of carbamoylphosphate

Escherichia coli

-

485843

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

kinetic data suggest an ordered bi bi mechanism

Vigna radiata var. radiata

-

485863

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

enzyme exhibits homotropic cooperativity for aspartate, is heterotropically activated by ATP and is heterotropically inhibited by CTP and UTP

Escherichia coli

-

485838, 485872

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

allosteric enzyme, in absence of effectors, two-state, concerted transition model

Escherichia coli

-

662646

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

cooperative mechanism of substrate binding

Pyrococcus abyssi

-

661693

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

ordered substrate binding with induced fit

Escherichia coli

-

663253

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

significant role of protein-solvent interactions in regulatory conformational changes

Escherichia coli

-

661450

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

ATCase follows an ordered Bi Bi reaction mechanism in which carbamoyl phosphate must bind before L-aspartate and the product N-carbamoyl-L-aspartate leaves the active site before inorganic phosphate

Escherichia coli

-

718699

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

catalytic and regulatory mechanisms, overview. The enzyme undergoes as it shifts between its low-activity, low-affinity form, T state, to its high-activity, high-affinity form, R state, and allosteric effectors modulate the activity. The ATCase-catalyzed reaction is regulated by nucleotide binding some 60 A from the active site, inducing structural alterations that modulate catalytic activity. The catalytic mechanism is ordered, carbamoyl phosphate binds before aspartate, and carbamoyl aspartate leaves before phosphate. Cooperativity is induced by aspartate binding

Escherichia coli

-

718458

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

the catalytic cycle of ATCase leads from the ordered binding of the substrates to the formation and decomposition of the tetrahedral intermediate and to the ordered release of the products from the active site, ordered-binding mechanism, detailed overview

Bacillus subtilis

P05654

720257

carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

-

-

-

-