Information on EC 2.6.1.88 - methionine transaminase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.6.1.88
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RECOMMENDED NAME
GeneOntology No.
methionine transaminase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-methionine + a 2-oxo carboxylate = 2-oxo-4-methylthiobutanoate + an L-amino acid
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
dimethylsulfoniopropanoate biosynthesis III (algae)
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ethylene biosynthesis III (microbes)
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L-homomethionine biosynthesis
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Col-0
SwissProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
no activity in Lactococcus lactis
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Manually annotated by BRENDA team
no activity in Lactococcus lactis IL1403
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Manually annotated by BRENDA team
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
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
2-oxo-4-methylthiobutanoate + L-glutamate
L-methionine + 2-oxoglutarate
show the reaction diagram
2-oxo-4-methylthiobutanoate + L-glutamate
L-methionine + ?
show the reaction diagram
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?
2-oxo-4-methylthiobutanoate + L-isoleucine
L-methionine + 2-oxo-methylvalerate
show the reaction diagram
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-
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?
2-oxo-4-methylthiobutanoate + L-leucine
L-methionine + 2-oxo-isocaproate
show the reaction diagram
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-
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r
2-oxo-4-methylthiobutanoate + L-phenylalanine
L-methionine + 2-oxo-3-phenylpropanoate
show the reaction diagram
2-oxo-4-methylthiobutanoate + L-phenylalanine
L-methionine + ?
show the reaction diagram
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-
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?
2-oxo-4-methylthiobutanoate + L-tryptophan
L-methionine + 3-(1H-indol-3-yl)-2-oxopropanoate
show the reaction diagram
2-oxo-4-methylthiobutanoate + L-tyrosine
L-methionine + 2-oxoglutarate
show the reaction diagram
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r
2-oxo-4-methylthiobutanoate + L-valine
L-methionine + 2-oxo-isovalerate
show the reaction diagram
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?
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
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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
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r
L-histidine + a 2-oxo acid
?
show the reaction diagram
88% activity compared to L-methionine (at 1 mM)
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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
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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
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r
L-leucine + a 2-oxo acid
?
show the reaction diagram
11% activity compared to L-methionine (at 1 mM)
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L-methionine + 2-oxo-isocaproate
2-oxo-4-methylthiobutanoate + L-leucine
show the reaction diagram
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r
L-methionine + 2-oxoglutarate
2-oxo-4-methylthiobutanoate + L-tyrosine
show the reaction diagram
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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)
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r
L-methionine + a 2-oxo acid
?
show the reaction diagram
the enzyme shows a preference for L-methionine (100% activity at 1 mM L-methionine)
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L-phenylalanine + a 2-oxo acid
?
show the reaction diagram
57% activity compared to L-methionine (at 1 mM)
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L-tyrosine + a 2-oxo acid
?
show the reaction diagram
9% activity compared to L-methionine (at 1 mM)
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additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-nitrotyrosine
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approximately 20% inhibition at 1 mM
Canaline
carboxymethoxylamine
hydroxylamine-O-sulfonic acid
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about 10% residual activity at 1 mM
malate
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approximately 20% inhibition at 1 mM
O-allylhydroxylamine
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mixed-type inhibition, about 10% residual activity at 1 mM
O-Benzylhydroxylamine
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mixed-type inhibition, about 10% residual activity at 1 mM
O-ethylhydroxylamine
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about 20% residual activity at 1 mM
O-nitrobenzylhydroxylamine
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about 30% residual activity at 1 mM
O-pentafluorobenzylhydroxylamine
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about 30% residual activity at 1 mM
O-tert-butyldimethylsilylhydroxylamine
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about 10% residual activity at 1 mM
O-tert-butylhydroxylamine
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mixed-type inhibition, about 7% residual activity at 1 mM
O-tetrahydropyranylhydroxylamine
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about 20% residual activity at 1 mM
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045 - 4.2
2-oxo-4-methylthiobutanoate
9.53 - 11.93
L-glutamate
2.85
L-isoleucine
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apparent Km value, at pH 7.4, 37C
2.5
L-leucine
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apparent Km value, at pH 7.4, 37C
0.93
L-methionine
recombinant enzyme, pH and temperature not specified in the publication
2.01 - 7.44
L-phenylalanine
1.42
L-tryptophan
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recombinant enzyme, in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37C
2.01
L-tyrosine
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recombinant enzyme, in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37C
1.77
L-valine
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apparent Km value, at pH 7.4, 37C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02097 - 0.1424
carboxymethoxylamine
0.02161 - 0.2
O-allylhydroxylamine
0.0082 - 0.08408
O-Benzylhydroxylamine
0.01102 - 0.0856
O-tert-butylhydroxylamine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00314
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crude recombinant enzyme, after incubation with 2 mM each amino acid (ADEFGHIKLNQRSTWY) and 1 mM 2-oxo-4-methylthiobutanoate in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37C
0.7227
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recombinant enzyme after 722.7fold purification, after incubation with 2 mM each amino acid (ADEFGHIKLNQRSTWY) and 1 mM 2-oxo-4-methylthiobutanoate in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5'-phosphate, at 37C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.2 M NaCl, 0.1 M sodium/potassium phosphate, pH 6.3, and 23.5% (w/v) PEG1000, at 20C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography, Red-120 Sepharose column chromatography, Mono-Q column chromatography, S200-Sephacryl gel filtration, and phenylethyl column chromatography
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Ni2+ affinity column chromatography
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Ni2+ affinity column chromatography and Superdex 200 pg gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) CodonPlus-RIL cells
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expressed in Escherichia coli C41 (DE3) cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
branched-chain aminotransferase4 transcription is induced by wounding. Branched-chain aminotransferase4 mRNA accumulation is light dependent
Show AA Sequence (337 entries)
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