Information on EC 2.6.1.103 - (S)-3,5-dihydroxyphenylglycine transaminase

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The expected taxonomic range for this enzyme is: Amycolatopsis orientalis

EC NUMBER
COMMENTARY hide
2.6.1.103
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RECOMMENDED NAME
GeneOntology No.
(S)-3,5-dihydroxyphenylglycine transaminase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + L-glutamate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of vancomycin group antibiotics
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Monobactam biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(S)-3,5-dihydroxyphenylglycine:2-oxoglutarate aminotransferase
A pyridoxal-5'-phosphate protein. The enzyme from the bacterium Amycolatopsis orientalis catalyses the reaction in the reverse direction as part of the biosynthesis of the (S)-3,5-dihydroxyphenylglycine constituent of the glycopeptide antibiotic chloroeremomycin.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3,5-dihydroxyphenyl)(oxo)acetate + L-glutamate
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate
show the reaction diagram
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate
(3,5-dihydroxyphenyl)(oxo)acetate + L-glutamate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(3,5-dihydroxyphenyl)(oxo)acetate + L-glutamate
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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a pyridoxal-phosphate protein
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49800
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x * 49800, electrospray ionisation mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of the N-terminal His6-tagged protein in Escherichia coli
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