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(2,6-dimethylphenyl)methane-SO-thioperoxol
(E)-[(2,6-dimethylphenyl)methylidene]sulfaniumolate
-
-
-
-
?
(E)-1-propenylsulfenic acid
(Z)-propanethial S-oxide
-
-
-
-
?
(E)-but-1-en-1-SO-peroxol
(Z)-butanethial S-oxide
-
-
-
-
?
(E)-prop-1-en-1-SO-peroxol
(Z)-propanethial oxide
-
-
-
-
ir
(E)-prop-1-en-1-SO-peroxol
(Z)-propanethial S-oxide
1-phenylethane-SO-thioperoxol
(Z)-(1-phenylethylidene)sulfaniumolate
-
-
-
-
?
1-propenesulfenic acid
(Z)-propanethial S-oxide
-
-
-
-
?
1-propenesulfenic acid
propanethial S-oxide
-
-
-
-
?
1-propenylsulfenic acid
propanethial S-oxide
2-phenylethane-SO-thioperoxol
(E)-(2-phenylethylidene)sulfaniumolate
-
-
-
-
?
ethane-SO-thioperoxol
(Z)-ethylidenesulfaniumolate
-
-
-
-
?
phenylmethanesulfenic acid
(Z)-phenylmethanethial S-oxide
prop-2-ene-1-SO-thioperoxol
(Z)-(prop-2-en-1-ylidene)sulfaniumolate
-
-
-
-
?
(E)-prop-1-en-1-SO-peroxol
(Z)-propanethial S-oxide
-
-
-
-
?
(E)-prop-1-en-1-SO-peroxol
(Z)-propanethial S-oxide
-
-
-
?
1-propenylsulfenic acid
propanethial S-oxide
-
-
-
-
?
1-propenylsulfenic acid
propanethial S-oxide
-
-
-
?
phenylmethanesulfenic acid
(Z)-phenylmethanethial S-oxide
-
-
-
-
?
phenylmethanesulfenic acid
(Z)-phenylmethanethial S-oxide
-
the enzyme catalyzes the formation of a sulfine lachrymator, (Z)-phenylmethanethial S-oxide, only in the presence of Petiveria alliacea alliinase and its natural substrate, S-benzyl-L-cysteine sulfoxide (petiveriin)
-
-
?
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(E)-1-propenylsulfenic acid
(Z)-propanethial S-oxide
-
-
-
-
?
(E)-but-1-en-1-SO-peroxol
(Z)-butanethial S-oxide
-
-
-
-
?
(E)-prop-1-en-1-SO-peroxol
(Z)-propanethial oxide
-
-
-
-
ir
(E)-prop-1-en-1-SO-peroxol
(Z)-propanethial S-oxide
1-propenesulfenic acid
(Z)-propanethial S-oxide
-
-
-
-
?
1-propenesulfenic acid
propanethial S-oxide
-
-
-
-
?
1-propenylsulfenic acid
propanethial S-oxide
phenylmethanesulfenic acid
(Z)-phenylmethanethial S-oxide
(E)-prop-1-en-1-SO-peroxol
(Z)-propanethial S-oxide
-
-
-
-
?
(E)-prop-1-en-1-SO-peroxol
(Z)-propanethial S-oxide
-
-
-
?
1-propenylsulfenic acid
propanethial S-oxide
-
-
-
-
?
1-propenylsulfenic acid
propanethial S-oxide
-
-
-
?
phenylmethanesulfenic acid
(Z)-phenylmethanethial S-oxide
-
-
-
-
?
phenylmethanesulfenic acid
(Z)-phenylmethanethial S-oxide
-
the enzyme catalyzes the formation of a sulfine lachrymator, (Z)-phenylmethanethial S-oxide, only in the presence of Petiveria alliacea alliinase and its natural substrate, S-benzyl-L-cysteine sulfoxide (petiveriin)
-
-
?
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C107A
-
the mutant exhibits 89.9% of wild type activity
E112Q
-
the mutant exhibits 104% of wild type activity
E88A
-
the mutant exhibits 0.585% of wild type activity
E88D
-
the mutant exhibits 0.571% of wild type activity
F104A
-
the mutant exhibits 2.18% of wild type activity
F104Y
-
the mutant exhibits 21% of wild type activity
F84A
-
the mutant exhibits 1.32% of wild type activity
L47A
-
the mutant exhibits 52.8% of wild type activity
L54A
-
the mutant exhibits 108% of wild type activity
M118A
-
the mutant exhibits 85.5% of wild type activity
M143A
-
the mutant exhibits 130% of wild type activity
M51A
-
the mutant exhibits 102% of wild type activity
R71A/E88A
-
the mutant exhibits 0.303% of wild type activity
R71K
-
the mutant exhibits 55.8% of wild type activity
R71L/E88Q
the mutations completely abolish the enzymatic reaction
T109A
-
the mutant exhibits 110% of wild type activity
T109A/E112Q/Y114F
the mutant shows very low activity compared to the wild type enzyme
V73A
-
the mutant exhibits 91.3% of wild type activity
W133A
-
the mutant exhibits 3.86% of wild type activity
W155A
-
the mutant exhibits 1.51% of wild type activity
Y102A
-
the mutant exhibits 0.133% of wild type activity
Y102F
-
the mutant exhibits 11.5% of wild type activity
Y114A
-
the mutant exhibits 2.78% of wild type activity
Y114F
-
the mutant exhibits 1.52% of wild type activity
E88Q
inactive
E88Q
-
the mutant exhibits 0.53% of wild type activity
R71L
inactive
R71L
-
the mutant exhibits 0.453% of wild type activity
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Arakawa, T.; Sato, Y.; Yamada, M.; Takabe, J.; Moriwaki, Y.; Masamura, N.; Kato, M.; Aoyagi, M.; Kamoi, T.; Terada, T.; Shimizu, K.; Tsuge, N.; Imai, S.; Fushinobu, S.
Dissecting the stereocontrolled conversion of short-lived sulfenic acid by lachrymatory factor synthase
ACS Catal.
10
9-19
2020
Allium cepa
-
brenda
Silvaroli, J.A.; Pleshinger, M.J.; Banerjee, S.; Kiser, P.D.; Golczak, M.
Enzyme that makes you cry-crystal structure of lachrymatory factor synthase from Allium cepa
ACS Chem. Biol.
12
2296-2304
2017
Allium cepa (P59082), Allium cepa
brenda
Masamura, N.; McCallum, J.; Kenel, F.; Pither-Joyce, M.; Khrustaleva, L.; Suzuki, G.; Mukai, Y.; Yamauchi, N.; Shigyo, M.
Genome organization of gene encoding lachrymatory factor synthase in Allium cepa
Acta Hortic.
969
73-80
2012
Allium cepa
brenda
Masamura, N.; Aoyagi, M.; Tsuge, N.; Kamoi, T.; Imai, S.
Proton transfer in a reaction catalyzed by onion lachrymatory factor synthase
Biosci. Biotechnol. Biochem.
76
1799-1801
2012
Allium cepa
brenda
Masamura, N.; Ohashi, W.; Tsuge, N.; Imai, S.; Ishii-Nakamura, A.; Hirota, H.; Nagata, T.; Kumagai, H.
Identification of amino acid residues essential for onion lachrymatory factor synthase activity
Biosci. Biotechnol. Biochem.
76
447-453
2012
Allium cepa (P59082), Allium cepa
brenda
Kubec, R.; Cody, R.; Dane, A.; Musah, R.; Schraml, J.; Vattekkatte, A.; Block, E.
Applications of direct analysis in real time-mass spectrometry (DART-MS) in Allium chemistry. (Z)-butanethial S-oxide and 1-butenyl thiosulfinates and their S-(E)-1-butenylcysteine S-oxide precursor from Allium siculum
J. Agric. Food Chem.
58
1121-1128
2010
Allium siculum
brenda
Aoyagi, M.; Kamoi, T.; Kato, M.; Sasako, H.; Tsuge, N.; Imai, S.
Structure and bioactivity of thiosulfinates resulting from suppression of lachrymatory factor synthase in onion
J. Agric. Food Chem.
59
10893-10900
2011
Allium cepa
brenda
Imai, S.
Discovery of lachrymatory factor synthase (LFS) in Allium cepa (onion), and its related research
Jpn. J. Food Eng.
16
181-184
2015
Allium cepa
-
brenda
He, Q.; Kubec, R.; Jadhav, A.P.; Musah, R.A.
First insights into the mode of action of a lachrymatory factor synthase - implications for the mechanism of lachrymator formation in Petiveria alliacea, Allium cepa and Nectaroscordum species
Phytochemistry
72
1939-1946
2011
Allium cepa, Petiveria alliacea
brenda
Eady, C.C.; Kamoi, T.; Kato, M.; Porter, N.G.; Davis, S.; Shaw, M.; Kamoi, A.; Imai, S.
Silencing onion lachrymatory factor synthase causes a significant change in the sulfur secondary metabolite profile
Plant Physiol.
147
2096-2106
2008
Allium cepa
brenda
Musah, R.A.; He, Q.; Kubec, R.
Discovery and characterization of a novel lachrymatory factor synthase in Petiveria alliacea and its influence on alliinase-mediated formation of biologically active organosulfur compounds
Plant Physiol.
151
1294-1303
2009
Petiveria alliacea
brenda
5.3.99.12 lachrymatory-factor synthase
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