2.6.1.72: D-4-hydroxyphenylglycine transaminase
This is an abbreviated version!
For detailed information about D-4-hydroxyphenylglycine transaminase, go to the full flat file.
Word Map on EC 2.6.1.72
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2.6.1.72
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l-glutamate
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transamination
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stutzeri
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synthesis
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putida
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benzoylformate
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salinarum
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enantiomerically
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mandelate
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ferredoxin
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pyridoxal-5'-phosphate
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halophilic
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inexpensive
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l-amino
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halobacterium
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analysis
- 2.6.1.72
- l-glutamate
-
transamination
- stutzeri
- synthesis
- putida
- benzoylformate
- salinarum
-
enantiomerically
- mandelate
- ferredoxin
- pyridoxal-5'-phosphate
-
halophilic
-
inexpensive
-
l-amino
-
halobacterium
- analysis
Reaction
Synonyms
aminotransferase, D-hydroxyphenylglycine, D-phenylglycine aminotransferase, D-PhgAT, dpgA, HpgAT, hydroxyphenylglycine aminotransferase, PhgAT
ECTree
2.6.1.72 D-4-hydroxyphenylglycine transaminaseAdvanced search results
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Application on EC 2.6.1.72 - D-4-hydroxyphenylglycine transaminase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
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development of a simple, inexpensive, accurate and precise kinetic method for the quantitation of 2-oxoglutarate (AKG) in cardioplegic solution and athletic supplements. The assay relies on an enzymatic transamination of AKG and D-4-hydroxyphenylglycine to form 4-hydroxybenzoylformate and L-glutamate using D-phenylglycine aminotransferase. The method shows good linearity (r2 = 0.9994) over an AKG concentration range of 0.020-0.160 mM. The limits of detection and quantitation are 0.00409 and 0.01362 mM, respectively. The detection is not interfered with by excipients in the samples
synthesis
synthesis
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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
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
N-terminus of PhgAT is genetically fused with short peptides from a ferredoxin enzyme of halophilic archaeon, Halobacterium salinarum. The fused enzymes display a reduced pI and increase in solubility in TEMP (pH 7.6) storage, and in CAPSO (pH 9.5) reaction buffers, respectively. All the fused PhgAT display higher enzymatic reaction rates than the wild-type at all concentrations of L-glutamate used. the halophilic fusion significantly increases the tolerance of PhgAT in the presence of NaCl and KCl
synthesis
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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
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synthesis
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N-terminus of PhgAT is genetically fused with short peptides from a ferredoxin enzyme of halophilic archaeon, Halobacterium salinarum. The fused enzymes display a reduced pI and increase in solubility in TEMP (pH 7.6) storage, and in CAPSO (pH 9.5) reaction buffers, respectively. All the fused PhgAT display higher enzymatic reaction rates than the wild-type at all concentrations of L-glutamate used. the halophilic fusion significantly increases the tolerance of PhgAT in the presence of NaCl and KCl
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