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Information on EC 3.4.19.14 - leukotriene-C4 hydrolase and Organism(s) Mus musculus and UniProt Accession Q9Z2A9

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.19 Omega peptidases
                3.4.19.14 leukotriene-C4 hydrolase
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This record set is specific for:
Mus musculus
UNIPROT: Q9Z2A9 not found.
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
gamma-glutamyl leukotrienase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
gamma-glutamyl leukotrienase
-
gamma-glutamyl leukotrienase
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
leukotriene C4 + H2O
leukotriene D4 + L-glutamate
show the reaction diagram
-
-
-
?
leukotriene C4 + H2O
leukotriene D4 + L-glutamate
show the reaction diagram
S-decyl-GSH + H2O
?
show the reaction diagram
-
the substrate has the strongest binding among all of the S-alkyl-GSH analyzed and has binding activity similar to leukotriene C4
-
-
?
S-decylglutathione + H2O
decan-1-ol + glutathione
show the reaction diagram
-
the Km for S-decyl glutathione is about 10fold higher than that for leukotriene C4
-
-
?
S-heptylglutathione + H2O
heptan-1-ol + glutathione
show the reaction diagram
-
-
-
-
?
S-hexyl glutathione + H2O
?
show the reaction diagram
-
-
-
-
?
S-nitrosylglutathione + H2O
nitrous acid + glutathione
show the reaction diagram
-
-
-
-
?
S-nonylglutathione + H2O
nonan-1-ol + glutathione
show the reaction diagram
-
-
-
-
?
S-octyl glutathione + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acivicin
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0022
leukotriene C4
0.03
S-decyl-GSH
-
in 0.1 M Tris-HCl buffer, pH 8.0, at 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
pulmonary interstitial cell
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
crypt cells of the small intestine
Manually annotated by BRENDA team
the enzyme is primarily expressed in spleen
Manually annotated by BRENDA team
-
the enzyme localizes to capillaries and sinusoids in most organs and in lung to larger vessels as well
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GGT5_MOUSE
573
1
61674
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
-
1 * 57000 + 1 * 20000, SDS-PAGE
57000
-
1 * 57000 + 1 * 20000, SDS-PAGE
63000
-
predicted from amino acid sequence
65000
75000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 65000-70000, sucrose velocity sedimentation
heterodimer
-
1 * 57000 + 1 * 20000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
the enzyme has six putative N-glycosylation sites
glycoprotein
-
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 60
-
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in NIH/3T3 cells
expressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lieberman, M.; Shields, J.; Will, Y.; Reed, D.; Carter, B.
gamma-Glutamyl leukotrienase cleavage of leukotriene C4
Adv. Exp. Med. Biol.
469
301-306
2000
Mus musculus
Manually annotated by BRENDA team
Han, B.; Luo, G.; Shi, Z.; Barrios, R.; Atwood, D.; Liu, W.; Habib, G.; Sifers, R.; Corry, D.; Lieberman, M.
gamma-Glutamyl leukotrienase, a novel endothelial membrane protein, is specifically responsible for leukotriene D4 formation in vivo
Am. J. Pathol.
161
481-490
2002
Mus musculus
Manually annotated by BRENDA team
Carter, B.; Wiseman, A.; Orkiszewski, R.; Ballard, K.; Ou, C.; Lieberman, M.
Metabolism of leukotriene C4 in gamma-glutamyl transpeptidase-deficient mice
J. Biol. Chem.
272
12305-12310
1997
Mus musculus
Manually annotated by BRENDA team
Carter, B.; Shi, Z.; Barrios, R.; Lieberman, M.
gamma-Glutamyl leukotrienase, a gamma-glutamyl transpeptidase gene family member, is expressed primarily in spleen
J. Biol. Chem.
273
28277-28285
1998
Mus musculus (Q9Z2A9), Mus musculus
Manually annotated by BRENDA team
Shi, Z.; Han, B.; Habib, G.; Matzuk, M.; Lieberman, M.
Disruption of gamma-glutamyl leukotrienase results in disruption of leukotriene D4 synthesis in vivo and attenuation of the acute inflammatory response
Mol. Cell. Biol.
21
5389-5395
2001
Mus musculus
Manually annotated by BRENDA team