Information on EC 2.6.1.72 - D-4-hydroxyphenylglycine transaminase

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The expected taxonomic range for this enzyme is: Pseudomonas

EC NUMBER
COMMENTARY
2.6.1.72
-
RECOMMENDED NAME
GeneOntology No.
D-4-hydroxyphenylglycine transaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-4-hydroxyphenylglycine + 2-oxoglutarate = 4-hydroxyphenylglyoxylate + L-glutamate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-4-hydroxyphenylglycine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aminotransferase, D-hydroxyphenylglycine
-
-
-
-
D-PhgAT
Q6VY99
-
D-PhgAT
Pseudomonas stutzeri ST201
Q6VY99
-
-
dpgA
Q6VY99
gene name
dpgA
Pseudomonas stutzeri ST201
Q6VY99
gene name
-
hydroxyphenylglycine aminotransferase
-
-
CAS REGISTRY NUMBER
COMMENTARY
117444-05-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain LW-4
-
-
Manually annotated by BRENDA team
strain LW-4; strain MW 27
-
-
Manually annotated by BRENDA team
Pseudomonas putida LW-4
strain LW-4
-
-
Manually annotated by BRENDA team
Pseudomonas putida MW 27
strain MW 27
-
-
Manually annotated by BRENDA team
Pseudomonas stutzeri ST201
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-hydroxyphenylglyoxylate + L-glutamate
D-4-hydroxyphenylglycine + 2-oxoglutarate
show the reaction diagram
-
enzyme is involved in biosynthesis of D-4-hydroxyphenylglycine
-
-
?
D-3-hydroxyphenylglycine + 2-oxoglutarate
3-hydroxyphenylglyoxylate + L-glutamate
show the reaction diagram
Pseudomonas putida, Pseudomonas putida LW-4
-
enantioselective reaction
-
r
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
show the reaction diagram
-
-
-
-
-
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
show the reaction diagram
-
enantioselective reaction
-
?
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
show the reaction diagram
-
enantioselective reaction
-
r
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
show the reaction diagram
Pseudomonas putida MW 27
-
-
-
-
-
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
show the reaction diagram
Pseudomonas putida MW 27
-
enantioselective reaction
-
?
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
show the reaction diagram
Pseudomonas putida LW-4
-
-
-
-
-
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
show the reaction diagram
Pseudomonas putida LW-4
-
enantioselective reaction
-
?
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
show the reaction diagram
Pseudomonas putida LW-4
-
-
-
-
-
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
show the reaction diagram
Pseudomonas putida LW-4
-
enantioselective reaction
-
r
additional information
?
-
Pseudomonas putida, Pseudomonas putida MW 27, Pseudomonas putida LW-4
-
no substrate: pyruvate, phenylpyruvate, oxalacetate, 2-oxobutanoate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-hydroxyphenylglyoxylate + L-glutamate
D-4-hydroxyphenylglycine + 2-oxoglutarate
show the reaction diagram
-
enzyme is involved in biosynthesis of D-4-hydroxyphenylglycine
-
-
?
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
show the reaction diagram
-
-
-
-
-
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
show the reaction diagram
Pseudomonas putida MW 27, Pseudomonas putida LW-4
-
-
-
-
-
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
show the reaction diagram
Pseudomonas putida LW-4
-
-
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
a pyridoxal phosphate protein
pyridoxal 5'-phosphate
-
absolute requirement
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Aminooxyacetate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.25
-
-
pH 7.0, 30°C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
metabolic engineering of the Escherichia coli L-phenylalanine pathway for the production of D-phenylglycine. Expression of hydroxymandelate synthase from Amycolatopsis orientalis, hydroxymandelate oxidase from Streptomyces coelicolor and hydroxyphenylglycine aminotransferase from Pseudomonas putida in Escherichia coli
synthesis
Q6VY99
functional expression in Pichia pastoris. Co-expression of Escherichia coli chaperonins GroEL-GroES with the enzyme gene dramatically improves the soluble active enzyme production. Increasing gene dosage of both the enzyme and those of the chaperones further increases functional protein yield up to 14400fold higher than when the enzyme is expressed alone. Optimization of cultivation condition further increases activity yield from the best co-expressing strain by 1.2fold
synthesis
Pseudomonas stutzeri ST201
-
functional expression in Pichia pastoris. Co-expression of Escherichia coli chaperonins GroEL-GroES with the enzyme gene dramatically improves the soluble active enzyme production. Increasing gene dosage of both the enzyme and those of the chaperones further increases functional protein yield up to 14400fold higher than when the enzyme is expressed alone. Optimization of cultivation condition further increases activity yield from the best co-expressing strain by 1.2fold
-