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Information on EC 2.6.1.88 - methionine transaminase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LE06

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.88 methionine transaminase
IUBMB Comments
The enzyme is most active with L-methionine. It participates in the L-methionine salvage pathway from S-methyl-5'-thioadenosine, a by-product of polyamine biosynthesis. The enzyme from the bacterium Klebsiella pneumoniae can use several different amino acids as amino donor, with aromatic amino acids being the most effective . The enzyme from the plant Arabidopsis thaliana is also a part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates .
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9LE06
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
methionine aminotransferase, methionine transaminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
branched-chain aminotransferase4
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
L-methionine:2-oxo-acid aminotransferase
The enzyme is most active with L-methionine. It participates in the L-methionine salvage pathway from S-methyl-5'-thioadenosine, a by-product of polyamine biosynthesis. The enzyme from the bacterium Klebsiella pneumoniae can use several different amino acids as amino donor, with aromatic amino acids being the most effective [1]. The enzyme from the plant Arabidopsis thaliana is also a part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates [3].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxo-4-methylthiobutanoate + an L-amino acid
L-methionine + a 2-oxo acid
show the reaction diagram
recombinant enzyme shows high activity with 2-oxo-4-methylthiobutanoate (100% activity at 0.1 and 2 mM)
-
-
r
4-methyl-2-oxopentanoate + ?
L-methionine + a 2-oxo acid
show the reaction diagram
41% activity at 2 mM compared to 2-oxo-4-methylthiobutanoate
-
-
r
5-methylthio-2-oxopentanoate + ?
L-methionine + a 2-oxo acid
show the reaction diagram
48% activity at 0.1 mM and 53% activity at 2 mM compared to 2-oxo-4-methylthiobutanoate
-
-
r
L-homomethionine + a 2-oxo acid
?
show the reaction diagram
37% activity at 1 mM and 65% activity at 5 mM compared to L-methionine
-
-
r
L-leucine + a 2-oxo acid
2-oxo-4-methylthiobutanoate + an L-amino acid
show the reaction diagram
29% activity at 1 mM and 62% activity at 5 mM compared to 2-oxo-4-methylthiobutanoate
-
-
r
L-methionine + a 2-oxo acid
2-oxo-4-methylthiobutanoate + an L-amino acid
show the reaction diagram
recombinant enzyme shows high efficiency with L-methionine (100% activity at 1 and 5 mM)
-
-
r
additional information
?
-
the enzyme does not use L-isoleucine (at 1 mM), L-valine (at 1 and 5 mM), 4-methyl-2-oxopentanoate (at 0.1 mM), 6-methylthio-2-oxohexanoate, 3-methyl-2-oxopentanoate, and 3-methyl-2-oxobutyrate as substrates (at 0.1 mM each)
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045
2-oxo-4-methylthiobutanoate
recombinant enzyme, pH and temperature not specified in the publication
0.93
L-methionine
recombinant enzyme, pH and temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Col-0
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
branched-chain aminotransferase4 is part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates in Arabidopsis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BCAT4_ARATH
354
0
39019
Swiss-Prot
other Location (Reliability: 3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
branched-chain aminotransferase4 transcription is induced by wounding. Branched-chain aminotransferase4 mRNA accumulation is light dependent
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schuster, J.; Knill, T.; Reichelt, M.; Gershenzon, J.; Binder, S.
Branched-chain aminotransferase4 is part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates in Arabidopsis
Plant Cell
18
2664-2679
2006
Arabidopsis thaliana (Q9LE06)
Manually annotated by BRENDA team