Ligand Carbamoyl phosphate

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Basic Ligand Information

Molecular Structure
Picture of Carbamoyl phosphate (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
CH4NO5P
Carbamoyl phosphate
FFQKYPRQEYGKAF-UHFFFAOYSA-N
Synonyms:
carbamoyl-phosphate, Carbamoylphosphate, Carbamylphosphate, carbamyl phosphate


Show all pahtways known for Show all BRENDA pathways known for Carbamoyl phosphate

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (86 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
carbamoyl phosphate + N2-succinyl-L-ornithine = phosphate + N-succinyl-L-citrulline
-
show the reaction diagram
carbamoyl phosphate + decarbamoylnovobiocin = phosphate + novobiocin
-
show the reaction diagram
carbamoyl phosphate + oxamate = phosphate + oxalureate
-
show the reaction diagram
carbamoyl phosphate + a 3-hydroxymethyl ceph-3-em-4-carboxylate = phosphate + a 3-carbamoyloxymethylcephem
-
show the reaction diagram
carbamoyl phosphate + H2O = carbamate + phosphate
-
show the reaction diagram
tobramycin + carbamoyl phosphate + ATP + H2O = nebramycin 5' + AMP + diphosphate + phosphate
-

In Vivo Product in Enzyme-catalyzed Reactions (14 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE

Substrate in Enzyme-catalyzed Reactions (164 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
carbamoyl phosphate + oxamate = phosphate + oxalureate
-
show the reaction diagram
carbamoyl phosphate + L-lysine = phosphate + L-homocitrulline
-
show the reaction diagram
D-glucose + carbamoyl phosphate = D-glucose 6-phosphate + carbamate
-
show the reaction diagram
carbamoyl phosphate + inosine = carbamate + IMP
-
show the reaction diagram
carbamoyl phosphate + H2O = carbamate + phosphate
-
show the reaction diagram
carbamoyl phosphate + H2O = carbamate + phosphate
-
show the reaction diagram
tobramycin + carbamoyl phosphate + ATP + H2O = nebramycin 5' + AMP + diphosphate + phosphate
-
show the reaction diagram
ADP + carbamoyl phosphate = ?
-
show the reaction diagram
ADP + carbamoyl phosphate = ATP + carbamate
-
show the reaction diagram
ATP + ribose 5-phosphate + carbamoylphosphate = ADP + phosphate + 5-phosphoribosylamine + formate
-

Product in Enzyme-catalyzed Reactions (39 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
N-carbamoylputrescine + phosphate = putrescine + carbamoyl phosphate
-

Activator in Enzyme-catalyzed Reactions (1 result)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
10 mM, activity is stimulated more than 10fold
-

Inhibitor in Enzyme-catalyzed Reactions (23 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
3 mM, 25% loss of activity
-
competitive
-
erythrocyte enzyme, competitive inhibition, Ki: 6.9 mM
-
non-competitive with respect to L-Glu
-
50% inhibition at 13 mM
-
2 mM: 50% inhibition of ATPase activity. 8 mM: 50% inhibition of carboxylating activity
-

3D Structure of Enzyme-Ligand-Complex (PDB) (116 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (24 results)

COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
aspartate transcarbamoylase activity domain of the multienzyme complex
35.9
-
multienzyme complex
57.4
-
-
47.2
-
wild type enzyme, at pH 8.5 and 20°C
410
-
pH 8.0, 37°C
82
-
mutant enzyme Y229S, at pH 8.5 and 20°C
290
-
mutant enzyme Y229F, at pH 8.5 and 20°C
150
-
mutant enzyme Y160S, at pH 8.5 and 20°C
300
-
mutant enzyme Y160F, at pH 8.5 and 20°C
120
-
mutant enzyme S61A, at pH 8.5 and 20°C
74
-
mutant enzyme R57A, at pH 8.5 and 20°C
7.5
-
mutant enzyme Q104L, at pH 8.5 and 20°C
88
-
mutant enzyme H272N, at pH 8.5 and 20°C
180
-
mutant enzyme H272L, at pH 8.5 and 20°C
4.2
-
mutant enzyme E299Q, at pH 8.5 and 20°C
4.6
-
mutant enzyme E299D, at pH 8.5 and 20°C
120
-
mutant enzyme D231A, at pH 8.5 and 20°C
0.48
-
mutant enzyme D140N, at pH 8.5 and 20°C
360
-
mutant enzyme C273A, at pH 8.5 and 20°C
140
-
pH 7.5, 25°C
319
-
pH 7.8, 30°C, C249A mutant, with acetyl-CoA and K+
0.043
-
pH 7.8, 30°C, C249A mutant, without acetyl-CoA and K+
0.13
-
pH 7.8, 30°C, wild-type Pyc1, with acetyl-CoA and K+
0.11
-
pH 7.8, 30°C, wild-type Pyc1, without acetyl-CoA and K+
0.11
-

KM Value (94 results)

COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
pH 8.5, 22°C
0.0051
-
at 25°C
88
-
at 37°C
162
-
at high salt concentrations
0.2
-
pH 9.4, 37°C
3.93
-
catalytic subunits
0.6
-
mutant enzyme Y197A, at pH 8.3 and 25°C
19.22
-
mutant enzyme H170A/Y197A, at pH 8.3 and 25°C
66.37
-
mutant enzyme H170A, at pH 8.3 and 25°C
38.76
-
mutant enzyme Y197F, at pH 8.3 and 25°C
32.98
-
pH 8.23, 37°C
3.2
-
pH 8.0, 75°C
1.26
-
holoenzyme
0.2
-
in cell extracts
0.61
-
in crude extracts of fibroblasts
0.004
-
in the absence of UMP
0.023
-
pH 8.0, 37°C
0.55
-
multienzyme complex and aspartate transcarbamoylase activity domain of the multienzyme complex alone
0.02
-
pH and temperature not specified in the publication
9.6
-
wild type enzyme, at pH 8.3 and 25°C
13.84
-
recombinant catalytic subunit, at 37°C
0.038
-
30°C
0.34
-
37°C
0.005
-
pH and temperature not specified in the publication
0.7
-
wild-type, pH 7.7, 37°C
0.13
-
mutant enzyme Y229F, at pH 8.5 and 20°C
0.33
-
mutant enzyme Y160F, at pH 8.5 and 20°C
0.53
-
mutant enzyme Y229S, at pH 8.5 and 20°C
0.32
-
mutant enzyme Y160S, at pH 8.5 and 20°C
0.3
-
mutant K88Q, pH 7.7, 37°C
1.24
-
mutant enzyme S61A, at pH 8.5 and 20°C
0.3
-
mutant K88R, pH 7.7, 37°C
0.15
-
pH 8.0, 37°C
pH 8.5, 10 mM fixed substrate
0.625
-
pH 8.5, 37°C
0.09
-
pH 9.0, 20°C
1
-
pH 9.0, 30°C
0.9
-
pH 9.0, 5°C
1.1
-
Q106E
0.06
-
wild type
0.36
-
wild type enzyme, at pH 8.5 and 20°C
0.27
-
mutant enzyme C273A, at pH 8.5 and 20°C
0.26
-
liver enzyme, presence of putrescine, pH 7.0
0.0008
-
liver enzyme, pH 7.0
0.00176
-
37°C, pH 9.0
0.25
-
37°C, pH 8.6
0.033
-
37°C, pH 8.2
0.087
-
mutant enzyme R57A, at pH 8.5 and 20°C
0.28
-
mutant enzyme D140N, at pH 8.5 and 20°C
1.4
-
mutant enzyme D231A, at pH 8.5 and 20°C
0.15
-
mutant enzyme E299D, at pH 8.5 and 20°C
0.22
-
mutant enzyme E299Q, at pH 8.5 and 20°C
0.34
-
mutant enzyme H272L, at pH 8.5 and 20°C
0.93
-
mutant enzyme H272N, at pH 8.5 and 20°C
0.5
-
mutant enzyme Q104L, at pH 8.5 and 20°C
0.4
-
-
0.058
-
pH and temperature not specified in the publication
0.101
-
at pH 7.0
0.17
-
pH 7.5, 25°C
0.085
-
recombinant enzyme, pH 6.5, 37°C
0.65
-
cosubstrate MgADP-, 30°C, pH 5.0
cosubstrate MnADP-, 30°C, pH 5.0
-
0.13
-
enzyme from pancreas
0.6
-
enzyme from brain
2.5
-
enzyme from adrenals
0.8
-
enzyme from testes
1.3
-
erythrocyte enzyme
5.42
-
skeletal muscle enzyme
4.2
-
recombinant enzyme, pH 8.0, 25°C, reaction with ADP
1.17
-
pH 8, 25°C, E211A mutant, ATP synthesis reaction with ADP as cosubstrate
0.51
-
pH 8, 25°C, wild-type enzyme, ATP synthesis reaction with ADP as cosubstrate
4.8
-
pH 8, 25°C, E288A mutant, ATP synthesis reaction with ADP as cosubstrate
2.3
-
pH 8, 25°C, R292A mutant, ATP synthesis reaction with ADP as cosubstrate
2.8
-
pH 8, 25°C, wild-type enzyme, ATP synthesis reaction with ADP as cosubstrate
11.2
-
-
11.9
-
pH 7.8, 30°C, C249A mutant, with acetyl-CoA and K+
1.7
-
pH 7.8, 30°C, C249A mutant, without acetyl-CoA and K+
10.7
-
pH 7.8, 30°C, wild-type Pyc1, with acetyl-CoA and K+
11.3
-
pH 7.8, 30°C, wild-type Pyc1, without acetyl-CoA and K+
12.3
-

Ki Value (5 results)

COMMENTARY
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
LITERATURE
-
0.018
-
at 25°C and pH 8.4
0.012
-
pH 8.5, 37°C
0.151
-
erythrocyte enzyme, competitive inhibition
6.9
-
-
13
-

References & Links

Links to other databases for Carbamoyl phosphate

ChEBI
PubChem
-
PubChem