Ligand Glutarate

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

Basic Ligand Information

Molecular Structure
Picture of Glutarate (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C5H8O4
Glutarate
JFCQEDHGNNZCLN-UHFFFAOYSA-N
Synonyms:
Glutaric acid, L-glutarate, pentan-1,5-dioic acid, pentanedioate, pentanedioic acid


Show all pahtways known for Show all BRENDA pathways known for Glutarate

Roles as Enzyme Ligand

In Vivo Product in Enzyme-catalyzed Reactions (7 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
L-Gln + H2O + O2 = glutarate + NH3 + H2O2
-
show the reaction diagram
glutaramic acid + H2O = glutaric acid + NH3
-

Substrate in Enzyme-catalyzed Reactions (22 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
glutarate + 2-oxoglutarate + O2 = (S)-2-hydroxyglutarate + succinate + CO2
-
show the reaction diagram
L-glutarate + 2-oxobutanoate = 2-oxoglutarate + 2-aminobutanoate
-
show the reaction diagram
ATP + glutaric acid = ?
-
show the reaction diagram
glutaconyl-CoA + glutarate = glutaconate + glutaryl-CoA
-
show the reaction diagram
succinyl-CoA + glutarate = glutaryl-CoA + succinate
-
show the reaction diagram
glutarate + succinyl-CoA = ? + succinate
-
show the reaction diagram
glutarate + H+ = butanoate + CO2
-
show the reaction diagram
ATP + glutarate + CoA = AMP + diphosphate + glutaryl-CoA
-
show the reaction diagram
ATP + pentanedioic acid + CoA = AMP + diphosphate + pentanedioyl-CoA
-
show the reaction diagram
ATP + glutarate + CoA = AMP + diphosphate + glutaryl-CoA
-
show the reaction diagram
ATP + glutarate + CoA = ADP + phosphate + glutaryl-CoA
-
show the reaction diagram
ATP + pentanedioate + NH4+ = ADP + phosphate + ?
-

Product in Enzyme-catalyzed Reactions (89 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
taurine + alpha-ketoadipate + O2 = sulfite + aminoacetaldehyde + pentan-1,5-dioic acid + CO2
-
show the reaction diagram
naringenin + 2-oxoadipate + O2 = dihydrokaempferol + pentanedioate + CO2
-
-
show the reaction diagram
2-oxoadipate + L-arginine + O2 = glutarate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
-
show the reaction diagram
glutaraldehyde + NAD+ + H2O = glutarate + NADH
-
-
show the reaction diagram
glutaraldehyde + NADP+ + H2O = glutarate + NADPH + H+
-
show the reaction diagram
glutaraldehyde + NAD+ = glutaric acid + NADH
-
-
show the reaction diagram
glutaraldehyde + NAD+ = glutarate + NADH
-
-
show the reaction diagram
glutaraldehyde + H2O + oxidized methyl viologen = glutarate + H+ + reduced methyl viologen
-
-
show the reaction diagram
glutaraldehyde + H2O + benzylviologen = glutarate + reduced benzylviologen
-
-
show the reaction diagram
L-Gln + H2O + O2 = glutarate + NH3 + H2O2
-
show the reaction diagram
glutaryl-CoA + acetate = glutarate + acetyl-CoA
-
-
show the reaction diagram
glutaryl-CoA = glutarate + CoA
-
-
show the reaction diagram
glutaryl-CoA + H2O = CoA + glutarate
-
-
show the reaction diagram
glutaryl-CoA + H2O = CoA + glutarate
-
-
show the reaction diagram
succinamic acid + H2O = pentanedioic acid + NH3
-
-
show the reaction diagram
glutaryl-7-aminocephalosporanic acid + H2O = glutarate + 7-aminocephalosporanic acid
-
-
show the reaction diagram
glutaramate + H2O = glutarate + NH3
-
-
show the reaction diagram
glutaronitrile + H2O = glutaric acid + NH3
-

Activator in Enzyme-catalyzed Reactions (4 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (41 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
inhibits at 10 mM
-
57% inhibition at 5 mM
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
-
most potent competitive inhibitor
-
competitive inhibitor
-
uncompetitive versus L-glutamate, competitive versus NAD+
-
shows no affinity for N6-linked NAD+ but is biospecifically adsorbed to S6-linked NAD+ derivatives in the presence of its soluble kinetic-based enzyme capture ligand glutarate
-
at 20 mM, 25% inhibition
-
at 6.67 mM 62% inhibition
-
competitive inhibitor
-
competitive inhibition of 15%
-
isozyme AAT1: competitive
about 70% inhibition, both isoforms
-
2.5 mM, 69% inhibition
-
10 mM, 94% inhibition
-
63% inhibition at 0.5 mM
-
6 mM, 5% inhibition
-
weak
-
0.1 M, weak
-
competitive inhibition
-
competitive
-
20 mM, 28% loss of activity
-
inhibits 42% at 1 mM

3D Structure of Enzyme-Ligand-Complex (PDB) (22 results)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (1 result)

COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
pH and temperature not specified in the publication
0.0051
-

KM Value (8 results)

COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
pH 7.2, 30°C
0.65
-
cosubstrate glutaconyl-CoA
0.7
-
pH 7.8, 30°C, cosubstrate 3-hydroxy-3-methylglutaryl-CoA
0.5
-
pH 7.8, 30°C, cosubstrate adipylCoA
0.18
-
pH 7.8, 30°C, cosubstrate malonylCoA
0.26
-
pH 7.8, 30°C, cosubstrate methylmalonylCoA
0.84
-
pH 7.8, 30°C, cosubstrate succinylCoA
0.45
-
37°C, pH 7.8
40.9
-

Ki Value (19 results)

COMMENTARY
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
LITERATURE
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
3.6
-
pH 7.0, 20°C
30
-
-
0.35
-
pH 8.0, 40°C, Ki(intercept), at 120 mM L-glutamate
53
-
pH 8.0, 40°C, Ki(slope), at 2.5 mM NAD+
3
-
at pH 7.4
0.09
-
at pH 8.5
0.07
-
at pH 7.0
1
-
pH 7.2
26
-
isozyme AAT1, 25°C, versus 2-oxoglutarate
15.05
-
isozyme AAT1, 25°C, versus L-aspartate
26.55
-
mutant I50Q, pH 7.8, 25°C
233
-
mutant V241A, pH 7.8, 25°C
140
-
wild-type, pH 7.8, 25°C
19
-

References & Links

Links to other databases for Glutarate

ChEBI
PubChem
-
PubChem