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DL-selenocysteine + S-adenosyl-L-methionine
Se-methyl-selenocysteine + S-adenosyl-L-homocysteine
the stereochemical orientation of the alpha-amino group is not crucial. With DL-selenocysteine or DL-selenohomocysteine as substrates, the Km decreases. This leads to the overproportional increase of specific activity with DL-selenocysteine
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-
?
L-selenocysteine + S-adenosyl-L-methionine
Se-methyl-L-selenocysteine + S-adenosyl-L-homocysteine
the enzyme is suitable for specific detoxification of selenocysteine and preventing selenium from intrusion into downstream sulfur pathways. Plays a crucial role in conferring selenium tolerance
-
-
?
S-adenosyl-L-methionine + 4-thiobutyric acid
S-adenosyl-L-homocysteine + 4-methylthiobutyric acid
0.014% relative activity compared to activity with L-homocysteine set at 100%
-
-
?
S-adenosyl-L-methionine + D-homocysteine
?
16% relative activity compared to activity with L-homocysteine set at 100%
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-
?
S-adenosyl-L-methionine + DL-cysteine
?
-
-
-
?
S-adenosyl-L-methionine + DL-homocysteine
?
S-adenosyl-L-methionine + DL-selenocysteine
?
S-adenosyl-L-methionine + DL-selenohomocysteine
?
S-adenosyl-L-methionine + L-cysteine
S-adenosyl-L-homocysteine + S-methyl-L-cysteine
S-adenosyl-L-methionine + L-cysteine
S-methyl-L-cysteine + S-adenosyl-L-homocysteine
1% relative activity with 10 mM L-cysteine compared to 1 mM L-selenocysteine activity set at 100%
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-
?
S-adenosyl-L-methionine + L-homocysteine
?
-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
no activity with wild-type enzyme. A184T mutant enzyme gains the ability to methylate L-homocysteine
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-
?
S-adenosyl-L-methionine + L-homoserine
?
less than 0.003% relative activity compared to activity with L-homocysteine set at 100%
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-
?
S-adenosyl-L-methionine + L-selenocysteine
S-adenosyl-L-homocysteine + Se-methyl-L-selenocysteine
S-adenosyl-L-methionine + L-selenocysteine
Se-methyl-L-selenocysteine + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + L-selenohomocysteine
?
-
-
-
?
S-adenosyl-L-methionine + selenocysteamine
?
less than 1% relative activity with 1 mM selenocysteamine compared to 1 mM L-selenocysteine activity set at 100%
-
-
?
S-methyl-L-methionine + DL-selenohomocysteine
?
-
-
-
?
S-methyl-L-methionine + L-homocysteine
L-methionine + S-methyl-L-homocysteine
-
-
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
additional information
?
-
S-adenosyl-L-methionine + DL-homocysteine
?
less than 1% relative activity with 10 mM DL-homocysteine compared to activity with 1 mM DL-selenocysteine set at 100%
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-
?
S-adenosyl-L-methionine + DL-homocysteine
?
-
-
-
?
S-adenosyl-L-methionine + DL-homocysteine
?
93% relative activity compared to activity with L-homocysteine set at 100%
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-
?
S-adenosyl-L-methionine + DL-selenocysteine
?
475% relative activity with 1 mM DL-selenocysteine compared to 1 mM L-selenocysteine activity set at 100%
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-
?
S-adenosyl-L-methionine + DL-selenocysteine
?
highest preference as methyl acceptor
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-
?
S-adenosyl-L-methionine + DL-selenohomocysteine
?
25% relative activity with 1 mM DL-selenohomocysteine compared to activity with 1 mM DL-selenocysteine set at 100%
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-
?
S-adenosyl-L-methionine + DL-selenohomocysteine
?
213% relative activity compared to activity with L-homocysteine set at 100%
-
-
?
S-adenosyl-L-methionine + L-cysteine
S-adenosyl-L-homocysteine + S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + L-cysteine
S-adenosyl-L-homocysteine + S-methyl-L-cysteine
less than 0.003% relative activity compared to activity with L-homocysteine set at 100%
-
-
?
S-adenosyl-L-methionine + L-selenocysteine
S-adenosyl-L-homocysteine + Se-methyl-L-selenocysteine
-
-
-
?
S-adenosyl-L-methionine + L-selenocysteine
S-adenosyl-L-homocysteine + Se-methyl-L-selenocysteine
-
-
-
-
?
S-adenosyl-L-methionine + L-selenocysteine
S-adenosyl-L-homocysteine + Se-methyl-L-selenocysteine
S-adenosyl-L-methionine at intracellular concentrations cannot serve as an effective substrate for the enzyme
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?
S-adenosyl-L-methionine + L-selenocysteine
S-adenosyl-L-homocysteine + Se-methyl-L-selenocysteine
selenate-treated plants synthesize significantly more Se-methyl-L-selenocysteine
-
-
?
S-adenosyl-L-methionine + L-selenocysteine
S-adenosyl-L-homocysteine + Se-methyl-L-selenocysteine
-
-
-
?
S-adenosyl-L-methionine + L-selenocysteine
S-adenosyl-L-homocysteine + Se-methyl-L-selenocysteine
0.027% relative activity compared to activity with L-homocysteine set at 100%
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
-
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
-
-
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
-
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
S-methylmethionine is the physiological methyl group donor. The enzyme is involved in detoxification of selenium in selenium-accumulating plants
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-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
activity with S-methyl-L-methionine is higher than with S-adenosyl-L-methionine
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-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
-
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
-
-
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
-
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
-
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
S-methylmethionine is the physiological methyl group donor
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
activity with S-methyl-L-methionine is higher than with S-adenosyl-L-methionine
-
-
?
additional information
?
-
methylation of L-cysteine can not be detected unless the concentration is raised to 10 mM. Under this condition, the reaction velocity is approximately 1% compared with methylation of L-selenocysteine. No activity with selenocysteamine and DL-homocysteine
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-
?
additional information
?
-
-
the plant produces methylselenocysteine from selenocysteine
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-
?
additional information
?
-
-
no activity with trimethylsulfonium and glycine betaine as methyl donor
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-
?
additional information
?
-
no activity with trimethylsulfonium and glycine betaine as methyl donor
-
-
?
additional information
?
-
expression of BoSMT significantly enhances Se tolerance with an increased level of total Se accumulation in Escherichia coli
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?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.1.1.10
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-
?
additional information
?
-
-
the enzyme also catalyzes the reaction of EC 2.1.1.10
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-
?
additional information
?
-
no activity with trimethylsulfonium and glycine betaine as methyl donor
-
-
?
additional information
?
-
-
no activity with trimethylsulfonium and glycine betaine as methyl donor
-
-
?
additional information
?
-
-
the plant produces methylselenocysteine from selenocysteine
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-
?
additional information
?
-
-
the plant produces methylselenocysteine from selenocysteine
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-
?
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L-selenocysteine + S-adenosyl-L-methionine
Se-methyl-L-selenocysteine + S-adenosyl-L-homocysteine
the enzyme is suitable for specific detoxification of selenocysteine and preventing selenium from intrusion into downstream sulfur pathways. Plays a crucial role in conferring selenium tolerance
-
-
?
S-adenosyl-L-methionine + L-selenocysteine
S-adenosyl-L-homocysteine + Se-methyl-L-selenocysteine
selenate-treated plants synthesize significantly more Se-methyl-L-selenocysteine
-
-
?
S-methyl-L-methionine + L-homocysteine
L-methionine + S-methyl-L-homocysteine
-
-
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
additional information
?
-
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
-
-
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
-
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
S-methylmethionine is the physiological methyl group donor. The enzyme is involved in detoxification of selenium in selenium-accumulating plants
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
-
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
-
-
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
-
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
-
-
-
?
S-methyl-L-methionine + L-selenocysteine
L-methionine + Se-methyl-L-selenocysteine
S-methylmethionine is the physiological methyl group donor
-
-
?
additional information
?
-
-
the plant produces methylselenocysteine from selenocysteine
-
-
?
additional information
?
-
-
the plant produces methylselenocysteine from selenocysteine
-
-
?
additional information
?
-
-
the plant produces methylselenocysteine from selenocysteine
-
-
?
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additional information
-
the post-secondary structure assembled by conserved Cys207, Cys272, and Cys273 residues is believed to form such a geometrical catalytic pocket which will position the sulfur group of L-homocysteine in close proximity to Thr147, responsible for methyl group transfer by donating a hydrogen bond
malfunction
-
overexpression of SMT decreases the negative effect of selenium on sulforaphane synthesis, while knockdown of SMT by RNAi enhances the negative effect
malfunction
-
overexpression of BjSMT in tobacco substantially enhances tolerance to selenite stress manifested as significantly higher fresh weight, plant height, and chlorophyll content than control plants. The BjSMT-transformed tobacco plants accumulate a high level of Se upon selenite stress, and the plants also have significantly increased MeSeCys production potential in their leaves. The enzyme is highly induced by selenite and especially selenate. BjSMT overexpressing plants maintain a higher level of GSH-Px activity and chlorophyll content under severe selenite treatment
malfunction
-
overexpression of SMT decreases the negative effect of selenium on sulforaphane synthesis, while knockdown of SMT by RNAi enhances the negative effect
-
metabolism
detoxification of selenium-containing compounds
metabolism
detoxification of selenium-containing compounds
metabolism
enzyme plays a crucial role in the detoxification of selenium in Astragalus bisulcatus
metabolism
SMT is the key enzyme for Se-methylselenocysteine synthesis
metabolism
-
an increase of SMT gene expression leads to a rise in APX and POX, but a suppression of CAT and GR enzymes activities in Astragalus chrysochlorus. Selenium might be involved in the antioxidant metabolism in Astragalus chrysochlorus
physiological function
expression of BoSMT significantly enhances Se tolerance, high levels of Se accumulate in Broccoli plants exposed to selenate, but addition of high levels of 1 or 10 mM sulfate shows a strong inhibitory effect on Se accumulation
physiological function
-
compared to wild type, ATP sulfurylase and selenocysteine methyltransferase, expressing plants also accumulate increased concentrations of selenium when treated with selenite. Selenocysteine methyltransferase, is able to carry out Se phytoremediation more efficiently when the plants are supplied with selenium in the form of selenate
physiological function
-
selenocysteine methyltransferase plays a critical role in the Se/S metabolism system. The enzyme plays a key role in sulforaphane synthesis in a selenium-rich environment
physiological function
-
plants can easily absorb and assimilate Se in the form of selenate and selenite through sulfur transport proteins and metabolic pathways and remove it by converting it into volatilized methylated forms. The Se substitution of S in proteins can destroy the molecular function of these proteins, so an increased level of Se is toxic to most organisms. In plants,selenates are reduced and assimilated to organic Se which can be converted to methylselenocysteine (MeSeCys) in addition to selenocysteine (SeCys), selenomethionine (SeMet), and dimethylselenide (DMSe). Selenocysteine methyltransferase (SMT) is the key enzyme responsible for Se-methylselenocysteine (MeSeCys) formation. Brassica juncea is a selenium accumulator. BjSMT also possesses a conserved Thr187 which is involved in transferring a methyl group to L-homocysteine (HoCys) by donating a hydrogen bond, suggesting that BjSMT can methylate both HoCys and SeCys substrates
physiological function
-
selenocysteine methyltransferase (SMT) is responsible for forming methylselenocysteine (MeSeCys)
physiological function
-
selenocysteine methyltransferase plays a critical role in the Se/S metabolism system. The enzyme plays a key role in sulforaphane synthesis in a selenium-rich environment
-
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A184T
mutant enzyme gains the ability to methylate L-homocysteine
additional information
the but lacks the selenocysteine methyltransferase activity in vitro, explaining why little or no detectable levels of Se-methylselenocysteine accumulation are observed in the non-accumulator plant. Sequence analysis reveals that the selenocysteine methyltransferase from all plant that accumulate selenium contain a glycine residue at position 24, whereas the plants that do not accumulate selenium possess an alanine residue. A phenylalanine residue at position 148 in the accumulator selenocysteine methyltransferases is replaced by a tyrosine residue in non-accumulators. Thr334 is common among the Se accumulator species is lacking in the non-accumulator selenocysteine methyltransferase sequences and it appears as a complete deletion of the Thr334 codon of the DNA sequence
additional information
-
the but lacks the selenocysteine methyltransferase activity in vitro, explaining why little or no detectable levels of Se-methylselenocysteine accumulation are observed in the non-accumulator plant. Sequence analysis reveals that the selenocysteine methyltransferase from all plant that accumulate selenium contain a glycine residue at position 24, whereas the plants that do not accumulate selenium possess an alanine residue. A phenylalanine residue at position 148 in the accumulator selenocysteine methyltransferases is replaced by a tyrosine residue in non-accumulators. Thr334 is common among the Se accumulator species is lacking in the non-accumulator selenocysteine methyltransferase sequences and it appears as a complete deletion of the Thr334 codon of the DNA sequence
additional information
transgenic expression in Nicotiana tabacum. When plants are watered with 200 microM selenate, overexpression of a selenocysteine methyltransferase transgene causes a 2- to 4fold increase in Se accumulation resulting in increased numbers of leaf lesions and areas of necrosis, production of methylselenocysteine up to 20% of total Se and generation of volatile dimethyl diselenide derived directly from methylselenocysteine. Despite the greatly increased accumulation of total Se, this does not result in increased Se toxicity effects on growth. Overexpression of ATP sulfurylase does not increase Se accumulation from selenate. Lines overexpressing both ATP sulfurylase and selenocysteine methyltransferase do not show a further increase in total Se accumulation or in leaf toxicity symptoms relative to overexpression of selenocysteine methyltransferase alone, but direct a greater proportion of Se into methylselenocysteine
additional information
-
overexpression of BjSMT in tobacco substantially enhances tolerance to selenite stress manifested as significantly higher fresh weight, plant height, and chlorophyll content than control plants. Transgenic plants exhibited low glutathione peroxidase activity in response to a lower dose of selenite stress (with a higher dose of selenite stress resulting in a high activity response) compared with the controls. The BjSMT-transformed tobacco plants accumulate a high level of Se upon selenite stress, and the plants also have significantly increased MeSeCys production potential in their leaves
additional information
-
overexpression of SMT decreases the negative effect of selenium on sulforaphane synthesis, while knockdown of SMT by RNAi enhances the negative effect
additional information
-
overexpression of SMT decreases the negative effect of selenium on sulforaphane synthesis, while knockdown of SMT by RNAi enhances the negative effect
-
additional information
-
transgenic expression in arabidopsis thaliana. After high zinc stress, the transgenic plants over-expressing SmtA show higher survival rate than the wild type. Over-expression of SmtA in Arabidopsis increases the activities of superoxide dismutase and peroxidase, and enhances the tolerance to zinc stress
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Ellis, D.R.; Sors, T.G.; Brunk, D.G.; Albrecht, C.; Orser, C.; Lahner, B.; Wood, K.V.; Harris, H.H.; Pickering, I.J.; Salt, D.E.
Production of Se-methylselenocysteine in transgenic plants expressing selenocysteine methyltransferase
BMC Plant Biol.
4
1
2004
Astragalus bisulcatus
brenda
Neuhierl, B.; Bck, A.
On the mechanism of selenium tolerance in selenium-accumulating plants. Purification and characterization of a specific selenocysteine methyltransferase from cultured cells of Astragalus bisculatus
Eur. J. Biochem.
239
235-238
1996
Astragalus bisulcatus (P56707)
brenda
Neuhierl, B.; Thanbichler, M.; Lottspeich, F.; Bck, A.
A family of S-methylmethionine-dependent thiol/selenol methyltransferases. Role in selenium tolerance and evolutionary relation
J. Biol. Chem.
274
5407-5414
1999
Astragalus bisulcatus, Astragalus bisulcatus (P56707), Escherichia coli (Q47690), Escherichia coli
brenda
Sors, T.G.; Martin, C.P.; Salt, D.E.
Characterization of selenocysteine methyltransferases from Astragalus species with contrasting selenium accumulation capacity
Plant J.
59
110-122
2009
Astragalus bisulcatus (P56707), Astragalus bisulcatus
brenda
Xu, J.; Tian, Y.S.; Peng, R.H.; Xiong, A.S.; Zhu, B.; Hou, X.L.; Yao, Q.H.
Cyanobacteria MT gene SmtA enhance zinc tolerance in Arabidopsis
Mol. Biol. Rep.
37
1105-1110
2010
Synechococcus elongatus
brenda
McKenzie, M.; Hunter, D.; Pathirana, R.; Watson, L.; Joyce, N.; Matich, A.; Rowan, D.; Brummell, D.
Accumulation of an organic anticancer selenium compound in a transgenic Solanaceous species shows wider applicability of the selenocysteine methyltransferase transgene from selenium hyperaccumulators
Transgenic Res.
18
407-424
2009
Astragalus bisulcatus (P56707)
brenda
Brummell, D.A.; Watson, L.M.; Pathirana, R.; Joyce, N.I.; West, P.J.; Hunter, D.A.; McKenzie, M.J.
Biofortification of tomato (Solanum lycopersicum) fruit with the anticancer compound methylselenocysteine using a selenocysteine methyltransferase from a selenium hyperaccumulator
J. Agric. Food Chem.
59
10987-10994
2011
Astragalus bisulcatus
brenda
Freeman, J.L.; Tamaoki, M.; Stushnoff, C.; Quinn, C.F.; Cappa, J.J.; Devonshire, J.; Fakra, S.C.; Marcus, M.A.; McGrath, S.P.; Van Hoewyk, D.; Pilon-Smits, E.A.
Molecular mechanisms of selenium tolerance and hyperaccumulation in Stanleya pinnata
Plant Physiol.
153
1630-1652
2010
Stanleya pinnata, Stanleya albescens
brenda
Lyi, S.M.; Heller, L.I.; Rutzke, M.; Welch, R.M.; Kochian, L.V.; Li, L.
Molecular and biochemical characterization of the selenocysteine Se-methyltransferase gene and Se-methylselenocysteine synthesis in broccoli
Plant Physiol.
138
409-420
2005
Brassica oleracea (Q4VNK0)
brenda
Zhu, L.; Jiang, C.; Deng, W.; Gao, X.; Wang, R.; Wan, X.
Cloning and expression of selenocysteine methyltransferase cDNA from Camellia sinensis
Acta Physiol. Plant.
30
167-174
2008
Camellia sinensis (Q1HL00)
-
brenda
Ari, S.; Cakir, O.; Turgut-Kara, N.
Selenium tolerance in Astragalus chrysochlorus: Identification of a cDNA fragment encoding a putative Selenocysteine methyltransferase
Acta Physiol. Plant.
32
1085-1092
2010
Astragalus chrysochlorus (F8QPI4)
-
brenda
LeDuc, D.L.; AbdelSamie, M.; Montes-Bayon, M.; Wu, C.P.; Reisinger, S.J.; Terry, N.
Overexpressing both ATP sulfurylase and selenocysteine methyltransferase enhances selenium phytoremediation traits in Indian mustard
Environ. Pollut.
144
70-76
2006
Astragalus bisulcatus
brenda
Cakir, A.; Ari, A.
Cloning and molecular characterization of selenocysteine methyltransferase (AchSMT) cDNA from Astragalus chrysochlorus
Plant OMICS
6
100-106
2013
Astragalus chrysochlorus (F8QPI4)
-
brenda
Huang, K.; Lin, J.; Wu, Q.; Yan, J.; Liu, M.; Zhang, S.; Xiao, W.
Changes in sulforaphane and selenocysteine methyltransferase transcript levels in broccoli treated with sodium selenite
Plant Mol. Biol. Rep.
34
807-814
2015
Brassica oleracea, Brassica oleracea BOP-04-28-6
-
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Cakir, .; Turgut-Kara, N.; Ari, S.
Selenium induced selenocysteine methyltransferase gene expression and antioxidant enzyme activities in Astragalus chrysochlorus
Acta Bot. Croat.
75
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Astragalus chrysochlorus
-
brenda
Chen, M.; Zeng, L.; Luo, X.; Mehboob, M.Z.; Ao, T.; Lang, M.
Identification and functional characterization of a novel selenocysteine methyltransferase from Brassica juncea L.
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70
6401-6416
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Brassica juncea
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