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Information on EC 2.6.1.72 - D-4-hydroxyphenylglycine transaminase
for references in articles please use BRENDA:EC2.6.1.72
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EC Tree 2 Transferases
2.6 Transferring nitrogenous groups
2.6.1 Transaminases
2.6.1.72 D-4-hydroxyphenylglycine transaminase
IUBMB Comments
A pyridoxal-phosphate protein.
The enzyme appears in viruses and cellular organisms
- 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 Schemes
showSynonyms
d-phgat, d-phenylglycine aminotransferase, hpgat, phgat, hydroxyphenylglycine aminotransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminotransferase, D-hydroxyphenylglycine
-
-
-
-
D-PhgAT
dpgA
PhgAT
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-4-hydroxyphenylglycine + 2-oxoglutarate = 4-hydroxyphenylglyoxylate + L-glutamate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
D-phenylglycine degradation
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SYSTEMATIC NAME
IUBMB Comments
D-4-hydroxyphenylglycine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
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CAS REGISTRY NUMBER
COMMENTARY
117444-05-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-hydroxyphenylglyoxylate + L-glutamate
D-4-hydroxyphenylglycine + 2-oxoglutarate
-
Substrates: enzyme is involved in biosynthesis of D-4-hydroxyphenylglycine
Products: -
Products: -
?
D-phenylglycine + 2-oxoglutarate
phenylglyoxylate + L-glutamate
-
Substrates: -
Products: -
Products: -
?
D-3-hydroxyphenylglycine + 2-oxoglutarate
3-hydroxyphenylglyoxylate + L-glutamate
-
Substrates: enantioselective reaction
Products: -
Products: -
r
D-3-hydroxyphenylglycine + 2-oxoglutarate
3-hydroxyphenylglyoxylate + L-glutamate
-
Substrates: enantioselective reaction
Products: -
Products: -
r
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
-
Substrates: enantioselective reaction
Products: -
Products: -
r
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
-
Substrates: enantioselective reaction
Products: -
Products: -
?
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
-
Substrates: -
Products: -
Products: -
?
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
-
Substrates: enantioselective reaction
Products: -
Products: -
?
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
-
Substrates: -
Products: -
Products: -
?
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
-
Substrates: enantioselective reaction
Products: -
Products: -
r
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
-
Substrates: -
Products: -
Products: -
?
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
-
Substrates: enantioselective reaction
Products: -
Products: -
?
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: pyruvate, phenylpyruvate, oxalacetate, 2-oxobutanoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: pyruvate, phenylpyruvate, oxalacetate, 2-oxobutanoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: pyruvate, phenylpyruvate, oxalacetate, 2-oxobutanoate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-hydroxyphenylglyoxylate + L-glutamate
D-4-hydroxyphenylglycine + 2-oxoglutarate
-
Substrates: enzyme is involved in biosynthesis of D-4-hydroxyphenylglycine
Products: -
Products: -
?
D-phenylglycine + 2-oxoglutarate
phenylglyoxylate + L-glutamate
-
Substrates: -
Products: -
Products: -
?
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
-
Substrates: -
Products: -
Products: -
?
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
-
Substrates: -
Products: -
Products: -
?
D-4-hydroxyphenylglycine + 2-oxoglutarate
4-hydroxyphenylglyoxylate + L-glutamate
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
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
-
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
Stutzerimonas stutzeri ST-201
-
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
Stutzerimonas 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
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Van den Tweel, W.J.J.; Widjojoatmodjo, M.N.; de Bont, J.A.M.
DL-4-Hydroxyphenylglycine catabolism in Pseudomonas putida MW27
Arch. Microbiol.
150
471-476
1988
Pseudomonas putida, Pseudomonas putida LW-4, Pseudomonas putida MW 27
-
brenda
Van den Tweel, W.J.J.; Smits, J.P.; Ogg, R.L.H.P.; de Bont, J.A.M.
The involvement of an enantioselctive transaminase in the metabolism of D-3- and D-4-hydroxyphenylglycine in Pseudomonas putida LW-4
Appl. Microbiol. Biotechnol.
29
224-230
1988
Pseudomonas putida, Pseudomonas putida LW-4
-
brenda
Mller, U.; van Assema, F.; Gunsior, M.; Orf, S.; Kremer, S.; Schipper, D.; Wagemans, A.; Townsend, C.A.; Sonke, T.; Bovenberg, R.; Wubbolts, M.
Metabolic engineering of the E. coli L-phenylalanine pathway for the production of D-phenylglycine (D-Phg)
Metab. Eng.
8
196-208
2006
Pseudomonas putida
brenda
Jariyachawalid, K.; Laowanapiban, P.; Meevootisom, V.; Wiyakrutta, S.
Effective enhancement of Pseudomonas stutzeri D-phenylglycine aminotransferase functional expression in Pichia pastoris by co-expressing Escherichia coli GroEL-GroES
Microb. Cell Fact.
11
47
2012
Stutzerimonas stutzeri (Q6VY99), Stutzerimonas stutzeri ST201 (Q6VY99)
brenda
Javid, H.; Jomrit, J.; Chantarasiri, A.; Isarangkul, D.; Meevootisom, V.; Wiyakrutta, S.
Effects of halophilic peptide fusion on solubility, stability, and catalytic performance of D-phenylglycine aminotransferase
J. Microbiol. Biotechnol.
24
597-604
2014
Stutzerimonas stutzeri (Q6VY99), Stutzerimonas stutzeri ST-201 (Q6VY99)
brenda
Rojanarata, T.; Laiwattanapaisal, W.; Ngawhirunpat, T.; Opanasopit, P.; Worrawethanakul, K.; Chantadee, T.; Fuangwattana, T.
Fast, affordable and eco-friendly enzyme kinetic method for the assay of alpha-ketoglutaric acid in medical product and sports supplements
Enzyme Microb. Technol.
116
72-76
2018
Pseudomonas putida
brenda
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