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Enzyme Nomenclature
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
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EC NUMBER 
COMMENTARY 
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
ORGANISM
UNIPROT
LITERATURE
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + L-glutamate
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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the enzyme is involved in the biosynthesis of (S)-3,5-dihydroxyphenylglycine of the glycopeptide antibiotic chloroeremomycin
physiological function
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the enzyme is involved in the biosynthesis of (S)-3,5-dihydroxyphenylglycine of the glycopeptide antibiotic chloroeremomycin
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3,5-dihydroxyphenyl)(oxo)acetate + L-glutamate
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate
(3,5-dihydroxyphenyl)(oxo)acetate + L-glutamate
(3,5-dihydroxyphenyl)(oxo)acetate + L-glutamate
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate
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the enzyme is involved in the biosynthesis of (S)-3,5-dihydroxyphenylglycine constituent of the glycopeptide antibiotic chloroeremomycin
-
-
?
(3,5-dihydroxyphenyl)(oxo)acetate + L-glutamate
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate
-
the enzyme is involved in the biosynthesis of (S)-3,5-dihydroxyphenylglycine constituent of the glycopeptide antibiotic chloroeremomycin
-
-
?
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate
(3,5-dihydroxyphenyl)(oxo)acetate + L-glutamate
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-
-
-
?
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate
(3,5-dihydroxyphenyl)(oxo)acetate + L-glutamate
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-
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3,5-dihydroxyphenyl)(oxo)acetate + L-glutamate
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate
(3,5-dihydroxyphenyl)(oxo)acetate + L-glutamate
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate
-
the enzyme is involved in the biosynthesis of (S)-3,5-dihydroxyphenylglycine constituent of the glycopeptide antibiotic chloroeremomycin
-
-
?
(3,5-dihydroxyphenyl)(oxo)acetate + L-glutamate
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate
-
the enzyme is involved in the biosynthesis of (S)-3,5-dihydroxyphenylglycine constituent of the glycopeptide antibiotic chloroeremomycin
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of the N-terminal His6-tagged protein in Escherichia coli
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LINKS TO OTHER DATABASES (specific for EC-Number 2.6.1.103)
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