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Information on EC 2.6.1.88 - methionine transaminase and Organism(s) Escherichia coli and UniProt Accession P77806

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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:
Escherichia coli
UNIPROT: P77806
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
methionine aminotransferase, methionine transaminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methionine aminotransferase
-
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
L-histidine + a 2-oxo acid
?
show the reaction diagram
88% activity compared to L-methionine (at 1 mM)
-
-
?
L-leucine + a 2-oxo acid
?
show the reaction diagram
11% activity compared to L-methionine (at 1 mM)
-
-
?
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)
-
-
?
L-phenylalanine + a 2-oxo acid
?
show the reaction diagram
57% activity compared to L-methionine (at 1 mM)
-
-
?
L-tyrosine + a 2-oxo acid
?
show the reaction diagram
9% activity compared to L-methionine (at 1 mM)
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on. The active site contains a bound pyridoxal 5'-phosphate, covalently attached to the conserved active site lysine residue Lys236
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45647
2 * 45647, X-ray crystallography
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 45647, X-ray crystallography
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 20°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+ affinity column chromatography and Superdex 200 pg gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C41 (DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dolzan, M.; Johansson, K.; Roig-Zamboni, V.; Campanacci, V.; Tegoni, M.; Schneider, G.; Cambillau, C.
Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function
FEBS Lett.
571
141-146
2004
Escherichia coli (P77806), Escherichia coli
Manually annotated by BRENDA team