Information on EC 4.4.1.20 - leukotriene-C4 synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.4.1.20
-
RECOMMENDED NAME
GeneOntology No.
leukotriene-C4 synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
leukotriene C4 = leukotriene A4 + glutathione
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alkenyl group transfer
additional information
-
multiple constructs encoding fusion proteins of green fluorescent protein as the N-terminal part and various truncated variants of human LTC4S as C-terminal part were prepared and transfected into HEK 293/T or COS-7 cells
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arachidonic acid metabolism
-
-
leukotriene biosynthesis
-
-
Metabolic pathways
-
-
arachidonic acid metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
leukotriene-C4 glutathione-lyase (leukotriene-A4-forming)
The reaction proceeds in the direction of addition. Not identical with EC 2.5.1.18, glutathione transferase.
CAS REGISTRY NUMBER
COMMENTARY hide
90698-32-1
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
-
enzyme residue Trp116 is not essential for catalysis but helps position the omega-end of leukotriene A4
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
14,15-leukotriene A4 + glutathione
?
show the reaction diagram
14,15-leukotriene A4 methyl ester + glutathione
?
show the reaction diagram
-
-
-
-
?
leukotriene A4 + glutathione
leukotriene C4
show the reaction diagram
leukotriene A4 + glutathione
leukotriene C4 + H2O
show the reaction diagram
leukotriene A4 free acid + glutathione
leukotriene C4
show the reaction diagram
leukotriene A4 methyl ester + glutathione
leukotriene C4 methyl ester
show the reaction diagram
leukotriene A4 methyl ester + glutathione
leukotriene C4 methyl ester + H2O
show the reaction diagram
leukotriene A4 methylester + glutathione
leukotriene C4 methylester
show the reaction diagram
-
pH 7.4, 37C
-
-
r
leukotriene A5 + glutathione
?
show the reaction diagram
-
37% of the activity with leukotriene A4
-
-
?
leukotriene C4
leukotriene A4 + glutathione
show the reaction diagram
additional information
?
-
-
binding structure of product analogue S-hexyl GSH to the active site of the enzyme, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
leukotriene A4 + glutathione
leukotriene C4
show the reaction diagram
leukotriene C4
leukotriene A4 + glutathione
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
stimulates
Co2+
-
inhibits the enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-benzoyl-5-(5-[(4-chlorophenyl)(methyl)amino]pyridine-2-carbonyl)benzoic acid
-
i.e. TK04, competitive mode of binding versus leukotriene A4
-
2-methyl-5-(1-methylethyl)cyclohexa-2,5-diene-1,4-dione
-
-
aspirin
-
blocks the STAT6-dependent interleukin-4-inducible expression of LTC4S
bovine serum albumin
-
5 mg, 45% inhibition
-
cysteinyl-leukotriene
-
diethylcarbamazine
-
IC50: 0.05 mM
estrone-3-sulfate
-
IC50: 1.9 mM
hexylglutathione
indomethacin
KCl
-
0.5 mM, about 25% inhibition
L-699,333
-
i.e. 2,[2-[1-(4-chlorobenzyl)-4-methyl-6-[(5-phenylpyridin-2-yl)methoxy]-4,5-dihydro-1H-thiopyrano[2,3,4-c,d]indol-2-yl]ethoxy]butanoic acid, reversible, competitive against glutathione and non-competitive against leukotriene A4
leukotriene A4
-
substrate inhibition
leukotriene C2
-
IC50: 0.0011 mM
leukotriene C4
leukotriene D4
-
-
leukotriene E4
-
-
MK-886
N-ethylmaleimide
-
inhibits the recombinant enzyme
NaCl
-
0.5 mM, about 25% inhibition
p-aminohippuric acid
-
IC50: 0.26 mM
probenecid
-
IC50: 17 mM
Rose bengal
-
IC50: 0.05 mM
sodium nitroprusside
-
in hepatic ischemia-reperfusion injured rats
Sulfobromophthalein
-
IC50: 0.06 mM
Triphenyltin chloride
-
poor inhibitor
Tumor necrosis factor alpha
-
zymosan
-
increase in LTC4S activity during differentiation of monocytic Mono Mac 6 cells by presence of leukotriene A4 is reduced by 80% in the presence of zymosan. Treatment with Zymosan for 48 h similarly attenuates LTC4S activity of primary human monocyte-derived macrophages and dendritic cells
-
additional information
-
cell treatment with ERK 1/2 specific inhibitor 1,4-diamino-2,3-dicyano-1,4-bis[2-aminophenylthio]butadiene (U0126) blocks LTC4S expression, pyrrolidine dithiocarbamate inhibits reactive oxygen species generation and NF-?B activation, which in turn blocks LTC4S expression
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17-beta-estradiol-3-sulfate
-
stimulates
17-beta-estradiol-3-sulfate-17 glucuronide
-
stimulates
A23187
-
a calcium ionophore
actinomycin D
-
in addition to retinoic acid
daunorubicin
-
-
estriol-3-sulfate
-
stimulates
leukotriene A4
-
presence of leukotriene A4 results in 20fold increased LTC4S activity during differentiation of monocytic Mono Mac 6 cells, which is reduced by 80% in the presence of zymosan
lipopolysaccharide
-
from Escherichia coli serotype O26:B26, increases mRNA expression in heart, brain, liver and adrenal gland
Mg2+
-
-
mitomycin C
-
-
retinoic acid
-
-
additional information
-
expression and activity of LTC4S is upregulated after treatment with D-galactosamine/lipopolysaccharide in a fulminant hepatic failure model
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13
14,15-Leukotriene A4
-
pH 8.0, 37C
0.07
14,15-Leukotriene A4 methyl ester
-
pH 8.0, 37C
0.0004 - 24.6
glutathione
0.0036 - 2.38
leukotriene A4
0.0188
leukotriene A4 free acid
4C, pH 7.35
0.00344 - 0.02
leukotriene A4 methyl ester
0.015
leukotriene methyl ester
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.022 - 84
glutathione
0.5 - 81
leukotriene A4
0.019 - 2.1
leukotriene A4 methyl ester
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.46 - 870
glutathione
44
1.3 - 2300
leukotriene A4
807
3.63 - 577
leukotriene A4 methyl ester
2490
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000037
2-benzoyl-5-(5-[(4-chlorophenyl)(methyl)amino]pyridine-2-carbonyl)benzoic acid
-
pH 7.8, temperature not specified in the publication, recombinant enzyme
-
0.01
2-methyl-5-(1-methylethyl)cyclohexa-2,5-diene-1,4-dione
-
IC50 value
0.0023
leukotriene A4
-
pH 7.4, 25C
0.00036
leukotriene C2
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000135
2-benzoyl-5-(5-[(4-chlorophenyl)(methyl)amino]pyridine-2-carbonyl)benzoic acid
Mus musculus
-
pH 7.8, temperature not specified in the publication, recombinant enzyme
-
0.05
diethylcarbamazine
Homo sapiens
-
IC50: 0.05 mM
1.9
estrone-3-sulfate
Rattus norvegicus
-
IC50: 1.9 mM
1.4
hexylglutathione
Cavia porcellus
-
IC50: 1.4 mM
1
indomethacin
Mus musculus
-
IC50: 1.0 mM
0.0011
leukotriene C2
Homo sapiens
-
IC50: 0.0011 mM
0.0021
leukotriene C4
Cavia porcellus
-
IC50: 0.0021 mM, inhibits reaction with leukotriene C4 methyl ester
0.0027 - 0.0031
MK-886
0.018 - 0.02
NEM
0.26
p-aminohippuric acid
Rattus norvegicus
-
IC50: 0.26 mM
17
probenecid
Rattus norvegicus
-
IC50: 17 mM
0.05
Rose bengal
Mus musculus
-
IC50: 0.05 mM
0.06
Sulfobromophthalein
Rattus norvegicus
-
IC50: 0.06 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000399
-
differentiated cells
0.00786
-
-
0.044
-
mutant R104K, 22C, pH not specified in the publication
0.0562
with leukotriene A4 free acid as substrate
0.0813
with leukotriene A4 methyl ester as substrate
0.29
-
crude enzyme from homogenate, at 25C
0.4
-
mutant R104T, 22C, pH not specified in the publication
0.729
-
-
1.6
-
mutant R104S, 22C, pH not specified in the publication
1.74
-
-
2
-
mutant R104A, 22C, pH not specified in the publication
4.135
-
-
4.3
-
mutant R31A, 22C, pH not specified in the publication
10
-
mutant R51Q, 22C, pH not specified in the publication
10.5
-
mutant R31Q, 22C, pH not specified in the publication
20
-
mutant R51A, 22C, pH not specified in the publication
28
-
recombinant enzyme, after 97fold purification, at 25C
30.5
-
-
35
-
wild-type, 22C, pH not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6 - 8.2
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.8
-
pH 5.5: about 25% of maximal activity, pH 8.8: about 45% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.69
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
monocytic leukemia cell line
Manually annotated by BRENDA team
-
co-localization for 5-lipoxygenase activating protein, LTC4 synthase, cyclooxygenase-1 and prostaglandin D2 synthase in nasal biopsies. 10-43% of LTC4 synthase-positive cells being macrophages in perennial and seasonal allergic rhinitis biopsies. In the rhinitic biopsies, LTC4 synthase is detectable in 6-76% of macrophages
Manually annotated by BRENDA team
-
monocytic Mono Mac 6 cell
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
throughout the gray matter
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
additional information
-
nasal biopsies
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
emanating from the vasopressinergic magnocellular neurons of the hypothalamic paraventricular, supraoptic and suprachiasmatic nuclei as well as the retrochiasmatic area to the pars nervosa of the pituitary gland. It is also observed in the axons of the extrahypothalamic system
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16567
-
x * 16567, calculation from nucleotide sequence
16800
calculated from amino acid sequence
17000
-
x * 17000, SDS-PAGE
39200
-
gel filtration
180000
-
2 * 180000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
-
-
trimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
phosphoregulation of LTC4S, as increased activity during MM6 cell differentiation correlates with reduced phosphorylation of 70-kDa ribosomal protein S6 kinase, which can phosphorylate purified LTC4S. The ribosomal protein S6 kinase inhibitor rapamycin at 20 nM doubles LTC4S activity of undifferentiated MM6 cells, and protein kinase A and C inhibitors H-89, CGP-53353, and staurosporine reverse the zymosan-induced suppression of LTC4S activity
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
its apo and GSH-complexed forms to 2.00 and 2.15 A resolution, using the sitting drop vapour diffusion technique
-
large number of parameters are important in obtaining big and well-ordered 2D crystals of LTC4S. Order can be induced by a combination of dividing/selecting fractions during the purification as well as a low lipid-to-protein ratio. To obtain a favorable diameter, salt (optimal: 50 mM), temperature (optimal: 23-24C), glycerol (optimal: 20%), and initial detergent concentration (optimal: 1%) have to be controlled. Several crystal forms can be grown, namely the plane group symmetries of p2, p3, p312, and two different unit cell sizes of plane group symmetry p321 with unit cell dimensions of a = b = 73.4 A, c = 120 and the second p321 type with larger unit cell size of a = b = 83.0 A, c = 120. Four transmembrane alpha-helices present, to 7.5 A resolution
-
LTC4S crystallized with glutathione, The structure is determined by the multiwavelength anomalous diffraction method by using the diffraction images from native LTC4S and a selenomethionine-substituted Leu121Met mutant
-
purified enzyme in apoform or in complex with either one of three product analogues, S-hexyl-, 4-phenyl-butyl-, and 2-hydroxy-4-phenyl-butyl-glutathione, sitting drop vapor diffusion, mixing of 0.001 ml of 3.5 mg/ml protein solution containing 1 mM GSH with 0.001 ml of reservoir solution containing 1.8-2.2 M NH4SO4, 0.2 M NaCl, and 0.1 M sodium cacodylate, pH 6.1-6.8, 1-4 days, room temperature, soaking in 1 mM ligand solutions, X-ray diffraction structure determination and analysis at 2.4-3.2 A resolution
-
resolution of 4.5 A
-
the interaction of residue R104 with the thiol group of GSH reduces its pKa to allow formation of a thiolate anion and subsequent nucleophilic attack at C6 of LTA4.Crystal structure of mutant R31Q at 2.1 A reveals a Q31 side chain pointing away from the active site
-
wild-type to 1.9 A resolution, space group F23. Mutants R31A and R104A, space groups F23 and C222, respectively. The architecture for GSH binding is conserved. The GSH binding site is a V-shaped cleft at each intermonomer interface in the LTC4S trimer, and nine amino acid residues directly participate in the GSH binding. Residue R30 multiply binds the carboxyl group of the gamma-glutamyl moiety, and R104 interacts with both the thiol group and the carbonyl group of the cysteinyl moiety of GSH. The side chain of R31 is flexible in the crystal structure
-
X-ray structure refined to 2.15 A resolution
-
purified enzyme in apoform or in complex with substrate glutathione or product analogue S-hexyl-GSH, mixing of 0.001 ml of 3.5 mg/ml protein in 0.03% w/v DDM w/v, 20 mM Tris pH 8.0, 100 mM NaCl, and 0.5 mM TCEP, with or without 1 mM GSH, with 0.001 ml of reservoir solution containing 1.8-2.2 M NH4SO4, 0.2 M NaCl and 0.1 M Na cacodylate pH 6.1-6.8, for S-hexyl GSH-enzyme crystals, S-hexyl GSH is added to mother liquor and soaking of apo-crystals, X-ray diffraction structure determination and analysis at 2.65-2.7 A resolution
-
sitting drop vapour diffusion method using the MbClass and MbClass II suites
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
t1/2: 18 h
25
-
t1/2: 18 h
37
-
3 min, 50 min loss of activity, 10 mM glutathione completely protects against inactivation
40
-
5 min, 90% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
partially purified enzyme requires substrate stabilization for long-term storage
-
reduced glutathione irreversibly inactivates the enzyme when present during freeze/thaw cycles and storage at concentrations above 5 mM
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, enzyme in the membrane fraction from human platelets can be stored without major loss of activity
-
-80C, in presence of 2-4 mM glutathione, stable for up to 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography purification based on specific interaction between leukotriene C4 synthase and microsomal glutathione S-transferase which ocurs in the presence of magnesium ion
-
extraction with a Triton X-100/Triton-DOC mixture, two affinity chromatography steps and gel filtration
-
fractioning
-
Ni-Sepharose column chromatography, S-hexylglutathione agarose chromatography, and Superdex 200 gel filtration
-
partial
solubilized with sodium deoxycholic acid and DDM, four steps of column chromatography, including affinity chromatography with S-hexyl GSH
-
the recombinant enzyme from Schizosaccharomyces pombe, to apparent homogeneity
-
to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
COS-7 cells transfected with either human or cloned mouse leukotriene C4 synthase cDNA by DEAE-dextran transfection
expressed as an N-terminal hexa-histidine-tagged fusion protein in Pichia pastoris KM71H cells
-
expressed in COS-7 cells; expression in rat basophilic leukemia RBL-2H3 cells
-
expressed in Schizosaccharomyces pombe
-
expression in COS-7 cells
-
expression in Escherichia coli, construction of an enhanced green fluorescent protein under the control of the mouse leukotriene C4 synthase promoter
-
expression in Pichia pastoris
-
expression in Schizosaccharomyces pombe
-
expression in Spodoptera frugiperda
overexpressed
-
overexpression in fission yeast with a His6 tag at the C terminus
-
overexpression in the yeast Pichia pastoris with a His6 tag
-
preparation of pRluc-LTC4S and pGFPLTC4S (full length and truncated forms). Full length and truncated forms of LTC4S excised from the pGFP vector and subcloned in frame with GST in a pGEX vector and transformed into Escherichia coli Y1090. Full length LTC4S subcloned into a pDsRed vector. HEK 293/T cells co-transfected with pRluc-LTC4S and pGFP fusion constructs. COS-7 cells co-transfected with GFP-5-lipoxygenase activating protein and dsRed-LTC4S
-
recombinant enzyme expression in Pichia pastoris strain KM71H
-
recombinant expression of wild-type and mutant enzymes in Pichia pastoris strain KM71H
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression in mast cells is not apparent in healthy subjects
-
is not suppressed by pretreatment with the p38 inhibitor
LTC4s increases following spared nerve injury, significant increase 3 days after nerve injury and continues at least for 14 days. LTC4s mRNA is expressed constitutively throughout the grey matter and increases after nerve injury in dorsal horn. This increase in LTC4s mRNA mainly occurrs in cells with small nuclei
mRNA levels for the three key enzymes/proteins in the biosynthesis of cysteinyl-leukotrienes, 5-lipoxygenase, 5-LO-activating protein, and LTC4 synthase, are significantly increased in the wall of human abdominal aortic aneurysm
-
no upregulation by interleukin-4 in the THP-1 cell line
-
significantly elevated immunoexpression of LTC4 synthase observed in perennial allergic rhinitis biopsies
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A444C
-
the mutation is associated with the risk of ischemic cerebrovascular disease
A52S
-
mutation increases the Km-value for the recombinant enzyme for glutathione
C56S/C82
-
mutant enzyme without altered function
C82V
-
mutant enzyme without altered function
E4K
-
causes allergic diseases in patients such as bronchial asthma or allergic dermatitis
G1072A
-
the mutation is associated with the risk of ischemic cerebrovascular disease
L121M
-
by site-directed mutagenesis to prepare the selenomethionine-substituted LTC4S, the mutant yeast clone is grown with selenomethionine, purified and crystallized similarly to the wild-type enzyme
LTCS(1-115)
-
C-terminally truncated protein, gives a bioluminescence resonance energy transfer signal when fused to Renilla luciferase
LTCS(1-24)
-
C-terminally truncated protein, gives no bioluminescence resonance energy transfer signal when fused to Renilla luciferase
LTCS(1-58)
-
C-terminally truncated protein, gives no bioluminescence resonance energy transfer signal when fused to Renilla luciferase
LTCS(1-88)
-
C-terminally truncated protein, gives a bioluminescence resonance energy transfer signal when fused to Renilla luciferase
LTCS(114-150)
-
N-terminally truncated protein, gives a bioluminescence resonance energy transfer signal when fused to Renilla luciferase
LTCS(23-115)
-
C- and N-terminally truncated protein, gives a bioluminescence resonance energy transfer signal when fused to Renilla luciferase
LTCS(23-150)
-
N-terminally truncated protein, gives a bioluminescence resonance energy transfer signal when fused to Renilla luciferase
LTCS(57-150)
-
N-terminally truncated protein, gives a bioluminescence resonance energy transfer signal when fused to Renilla luciferase
LTCS(87-150)
-
N-terminally truncated protein, gives a bioluminescence resonance energy transfer signal when fused to Renilla luciferase
N55A
-
mutation increases the Km-value for the recombinant enzyme for glutathione
R104K
-
0.1% of wild-type activity
R104Q
-
substrate leukotriene A4, 2% of wild-type activity. No activity with substrate leukotriene A4 methyl ester
R104S
-
4.6% of wild-type activity
R104T
-
1.1% of wild-type activity
R113A
-
substrate leukotriene A4, 140% of wild-type activity
R113Q
-
substrate leukotriene A4, 150% of wild-type activity
R31E
-
substrate leukotriene A4, 3% of wild-type activity
R31L
-
substrate leukotriene A4, 3% of wild-type activity
R51A
-
57% of wild-type activity
R51H
-
fully active mutant enzyme
R51K
-
fully active mutant enzyme
R51Q
-
29% of wild-type activity
R51T
-
mutant enzyme without activity
R90A
-
substrate leukotriene A4, 6% of wild-type activity, substrate leukotriene A4 methyl ester, 21% ot wild-type activity
R90Q
-
substrate leukotriene A4, about 20% of wild-type activity
R92A
-
substrate leukotriene A4, about 95% of wild-type activity
R92Q
-
substrate leukotriene A4, about 105% of wild-type activity
R99A
-
substrate leukotriene A4, about 100% of wild-type activity
R99Q
-
substrate leukotriene A4, about 70% of wild-type activity
V49F
-
mutation increases the Km-value for the recombinant enzyme for glutathione
W116A
-
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
W116F
-
site-directed mutagenesis, the mutant shows a 3fold increased turnover of leukotriene A4 compared to the wild-type enzyme
Y59F
-
mutation increases the Km-value for the recombinant enzyme for glutathione
Y97F
-
mutation increases the Km-value for the recombinant enzyme for glutathione
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
although structural differences near the active site and along the C-terminal alpha-helix V suggest that the mouse and human enzymes may function differently in vivo, the mouse enzyme is a useful tool in pharmacological research and drug development
drug development
medicine
molecular biology