Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.1.280 extracted from

  • 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. (2019), J. Exp. Bot., 70, 6401-6416 .
    View publication on PubMed

Application

Application Comment Organism
agriculture Brassica juncea SMT demonstrates its potential applications in crop MeSeCys biofortification and phytoremediation of Se pollution Brassica juncea

Cloned(Commentary)

Cloned (Comment) Organism
gene SMT, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of GFP-tagged enzyme under control of 35S promoter in Nicotiana tabacum, quantitative real-time PCR enzyme expression analysis Brassica juncea

Protein Variants

Protein Variants Comment Organism
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 Brassica juncea

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ the presence of the conserved amino acids in BjSMT at positions Cys248, Cys315, and Cys316 suggests that BjSMT may also coordinate the binding of Zn2+ Brassica juncea

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-methyl-L-methionine + L-homocysteine Brassica juncea
-
L-methionine + S-methyl-L-homocysteine
-
?
S-methyl-L-methionine + L-selenocysteine Brassica juncea
-
L-methionine + Se-methyl-L-selenocysteine
-
?

Organism

Organism UniProt Comment Textmining
Brassica juncea
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Brassica juncea
-
additional information semiquantitative RT-PCR expression analysis of BjSMT transcript accumulation in leaves and roots of Indian mustard plants supplied with 0.04 mM Na2SeO4, 0.04 mM Na2SeO3, and 0.001 mM MgSO4 in the medium, overview Brassica juncea
-
root
-
Brassica juncea
-
seedling
-
Brassica juncea
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-methyl-L-methionine + L-homocysteine
-
Brassica juncea L-methionine + S-methyl-L-homocysteine
-
?
S-methyl-L-methionine + L-selenocysteine
-
Brassica juncea L-methionine + Se-methyl-L-selenocysteine
-
?

Synonyms

Synonyms Comment Organism
BjSMT
-
Brassica juncea
selenocysteine methyltransferase
-
Brassica juncea
SMT
-
Brassica juncea

Expression

Organism Comment Expression
Brassica juncea BjSMT responds to selenite [Se(IV)] and selenate [Se(VI)] stress in Brassica juncea. BjSMT expression is nearly undetectable in the Brassica juncea plant without Se exposure, but in the plant leaves it can be rapidly and significantly upregulated upon a low level of selenite stress, and enormously upregulated upon selenate treatment up

General Information

General Information Comment Organism
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 Brassica juncea
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 Brassica juncea
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 Brassica juncea