Information on EC 3.4.19.14 - leukotriene-C4 hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.19.14
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RECOMMENDED NAME
GeneOntology No.
leukotriene-C4 hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
leukotriene C4 + H2O = leukotriene D4 + L-glutamate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arachidonic acid metabolism
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Metabolic pathways
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arachidonic acid metabolism
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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in vivo gamma-glutamyl leukotrienase, and notgamma-glutamyl transpeptidase, is primarily responsible for conversion of leukotriene C4 to leukotriene D4. The enzyme plays an important role in inflammatory processes
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glutathione sulfonic acid + H2O + glycylglycine
? + gamma-glutamyl-glycylglycine
show the reaction diagram
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?
leukotriene C4 + H2O
leukotriene D4 + L-glutamate
show the reaction diagram
oxidized glutathione + H2O + glycylglycine
? + gamma-glutamyl-glycylglycine
show the reaction diagram
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?
reduced glutathione + H2O + glycylglycine
? + gamma-glutamyl-glycylglycine
show the reaction diagram
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?
S-(4-nitro-benzyl)glutathione + H2O + glycylglycine
? + gamma-glutamyl-glycylglycine
show the reaction diagram
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?
S-decyl-GSH + H2O
?
show the reaction diagram
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the substrate has the strongest binding among all of the S-alkyl-GSH analyzed and has binding activity similar to leukotriene C4
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?
S-decylglutathione + H2O
decan-1-ol + glutathione
show the reaction diagram
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the Km for S-decyl glutathione is about 10fold higher than that for leukotriene C4
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?
S-heptylglutathione + H2O
heptan-1-ol + glutathione
show the reaction diagram
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?
S-hexyl glutathione + H2O
?
show the reaction diagram
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?
S-methylglutathione + H2O + glycylglycine
? + gamma-glutamyl-glycylglycine
show the reaction diagram
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?
S-nitrosylglutathione + H2O
nitrous acid + glutathione
show the reaction diagram
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?
S-nonylglutathione + H2O
nonan-1-ol + glutathione
show the reaction diagram
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?
S-octyl glutathione + H2O
?
show the reaction diagram
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?
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acivicin
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serine-borate
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8fold more potent in inhibiting GGT1 than in inhibiting GGT5
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0751
glutathione sulfonic acid
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in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0022 - 0.0102
leukotriene C4
0.426
oxidized glutathione
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in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.105
reduced glutathione
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in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0148
S-(4-nitro-benzyl)glutathione
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in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.03
S-decyl-GSH
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in 0.1 M Tris-HCl buffer, pH 8.0, at 37°C
0.0182
S-Methylglutathione
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in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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the enzyme localizes to capillaries and sinusoids in most organs and in lung to larger vessels as well
Manually annotated by BRENDA team
the enzyme is detected in cerebral, cerebellar, and brain stem neurons but not in glial cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
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1 * 57000 + 1 * 20000, SDS-PAGE
57000
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1 * 57000 + 1 * 20000, SDS-PAGE
63000
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predicted from amino acid sequence
65000
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papain-cleaved enzyme, gel filtration; papain-cleaved enzyme, sedimentation velocity centrifugation
75000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 65000-70000, sucrose velocity sedimentation
heterodimer
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1 * 57000 + 1 * 20000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 60
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at 60°C for 5 min completely inactivates cleavage of LTC4, while at 37°C the enzyme is active for as long as 5 h
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and Sephadex G-150 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in NIH/3T3 cells
expressed in Pichia pastoris
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