Information on EC 2.6.1.49 - dihydroxyphenylalanine transaminase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
2.6.1.49
-
RECOMMENDED NAME
GeneOntology No.
dihydroxyphenylalanine transaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-dopa + 2-oxoglutarate = 3,4-dihydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
(S)-reticuline biosynthesis II
-
rosmarinic acid biosynthesis II
-
Tyrosine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
3,4-dihydroxy-L-phenylalanine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aminotransferase, dihydroxyphenylalanine
-
-
-
-
aspartate-DOPP transaminase, ADT
-
-
-
-
dihydroxyphenylalanine aminotransferase
-
-
-
-
dopa aminotransferase
-
-
-
-
dopa transaminase
-
-
-
-
dopa transaminase
-
-
glutamate-DOPP transaminase, GDT
-
-
-
-
L-dopa transaminase
-
-
-
-
phenylalanine-DOPP transaminase, PDT
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37277-98-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Alcaligenes faecalis IAM 1015
IAM 1015
-
-
Manually annotated by BRENDA team
Enterobacter cloacae NB 320
NB 320
-
-
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
3-(3,4-dihydroxyphenyl)-L-alanine + 2-oxoglutarate
3-(3,4-dihydroxyphenyl)pyruvate + L-glutamate
show the reaction diagram
-
i.e. L-dopa
i.e. DOPP
?
3-(3,4-dihydroxyphenyl)-L-alanine + 2-oxoglutarate
3-(3,4-dihydroxyphenyl)pyruvate + L-glutamate
show the reaction diagram
-
i.e. L-dopa
i.e. DOPP
?
3-(3,4-dihydroxyphenyl)-L-alanine + 2-oxoglutarate
3-(3,4-dihydroxyphenyl)pyruvate + L-glutamate
show the reaction diagram
-
most effective amino acceptor
i.e. DOPP
?
3-(3,4-dihydroxyphenyl)-L-alanine + oxaloacetic acid
3-(3,4-dihydroxyphenyl)pyruvate + L-aspartate
show the reaction diagram
-
-
-
-
?
3-(3,4-dihydroxyphenyl)-L-alanine + oxaloacetic acid
3-(3,4-dihydroxyphenyl)pyruvate + L-aspartate
show the reaction diagram
-
i.e. L-Dopa, 10% of activity with 2-oxoglutarate
-
?
3-(3,4-dihydroxyphenyl)-L-alanine + phenyl 2-oxopropanoate
3-(3,4-dihydroxyphenyl)pyruvate + L-phenylalanine
show the reaction diagram
-
i.e. L-dopa
-
?
3-(3,4-dihydroxyphenyl)pyruvate + L-aspartate
3,4-dihydroxy-L-phenylalanine + oxaloacetate
show the reaction diagram
-
aspartate-3,4-dihydroxyphenylpyruvate transaminase, ADT
i.e. L-dopa
?
3-(3,4-dihydroxyphenyl)pyruvate + L-aspartate
3,4-dihydroxy-L-phenylalanine + oxaloacetate
show the reaction diagram
-
aspartate-3,4-dihydroxyphenylpyruvate transaminase, ADT
i.e. L-dopa
?
3-(3,4-dihydroxyphenyl)pyruvate + L-aspartate
3,4-dihydroxy-L-phenylalanine + oxaloacetate
show the reaction diagram
Alcaligenes faecalis IAM 1015
-
aspartate-3,4-dihydroxyphenylpyruvate transaminase, ADT
i.e. L-dopa
?
3-(3,4-dihydroxyphenyl)pyruvate + L-aspartate
3,4-dihydroxy-L-phenylalanine + oxaloacetate
show the reaction diagram
Enterobacter cloacae NB 320
-
aspartate-3,4-dihydroxyphenylpyruvate transaminase, ADT
i.e. L-dopa
?
3-(3,4-dihydroxyphenyl)pyruvate + L-glutamate
3-(3,4-dihydroxyphenyl)-L-alanine + 2-oxoglutarate
show the reaction diagram
-
glutamate-3,4-dihydroxyphenylpyruvate transaminase, GDT
i.e. L-dopa
?
3-(3,4-dihydroxyphenyl)pyruvate + L-glutamate
3-(3,4-dihydroxyphenyl)-L-alanine + 2-oxoglutarate
show the reaction diagram
-
glutamate-3,4-dihydroxyphenylpyruvate transaminase, GDT
i.e. L-dopa
?
3-(3,4-dihydroxyphenyl)pyruvate + L-glutamate
3-(3,4-dihydroxyphenyl)-L-alanine + 2-oxoglutarate
show the reaction diagram
Alcaligenes faecalis IAM 1015
-
glutamate-3,4-dihydroxyphenylpyruvate transaminase, GDT
i.e. L-dopa
?
3-(3,4-dihydroxyphenyl)pyruvate + L-glutamate
3-(3,4-dihydroxyphenyl)-L-alanine + 2-oxoglutarate
show the reaction diagram
Enterobacter cloacae NB 320
-
glutamate-3,4-dihydroxyphenylpyruvate transaminase, GDT
i.e. L-dopa
?
3-(3,4-dihydroxyphenyl)pyruvate + L-phenylalanine
3,4-dihydroxy-L-phenylalanine + L-phenylpyruvate
show the reaction diagram
-
phenylalanine-3,4-dihydroxyphenylpyruvate transaminase, PDT
i.e. L-dopa
?
3-(3,4-dihydroxyphenyl)pyruvate + L-phenylalanine
3,4-dihydroxy-L-phenylalanine + L-phenylpyruvate
show the reaction diagram
-
phenylalanine-3,4-dihydroxyphenylpyruvate transaminase, PDT
i.e. L-dopa
?
3-(3,4-dihydroxyphenyl)pyruvate + L-phenylalanine
3,4-dihydroxy-L-phenylalanine + L-phenylpyruvate
show the reaction diagram
Alcaligenes faecalis IAM 1015
-
phenylalanine-3,4-dihydroxyphenylpyruvate transaminase, PDT
i.e. L-dopa
?
3-(3,4-dihydroxyphenyl)pyruvate + L-phenylalanine
3,4-dihydroxy-L-phenylalanine + L-phenylpyruvate
show the reaction diagram
Enterobacter cloacae NB 320
-
phenylalanine-3,4-dihydroxyphenylpyruvate transaminase, PDT
i.e. L-dopa
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
8% of activity with L-Dopa
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
8% of activity with L-Dopa
-
?
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-hydroxy-4-benzyloxyamine dihydrogen phosphate
-
NSD 1055, up to 30 mM
Al3+
-
strong inhibition
carbidopa
-
MK 486, inhibition is more marked if 2-oxoglutarate is used as amino group acceptor rather than phenylpyruvate, pyridoxal 5'-phosphate protects
carbidopa
-
0.75 mM, significant decrease of activity
Co2+
-
weak inhibition
Cu2+
-
strong inhibition
Fe2+
-
strong inhibition
-
iodoacetic acid
-
1 mM, 75% inhibition
Ni2+
-
inhibition of ADT and GDT, not PDT
p-Chloromercuriphenyl sulfonic acid
-
0.02 mM, 92% inhibition, addition of 1 mM glutathione protects to 100%
Zn2+
-
weak inhibition
KCN
-
1 mM, 93% inhibition, pyridoxal 5'-phosphate protects
additional information
-
not inhibited by benserazide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal phosphate
-
a pyridoxal phosphate protein, Km: 0.016 mM
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.48
-
2-oxoglutarate
-
pH 8.2, 37C
41
-
L-Dopa
-
pH 8.2, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0366
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.5
-
-
GDT, PDT
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
9
-
approx. 35% of maximal activity at pH 7.0, approx. 60% of activity at pH 9.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
55
-
approx. 40% of maximal activity at 35C, approx. 90% of maximal activity at 55C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
8.5
-
45C, 30 min, enzyme GDT stable
8
-
-
45C, 30 min, enzyme GDT stable
8.5
9
-
45C, 30 min, enzyme PDT stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
40
-
15 min, heat activation, enzyme GDT
55
-
-
6 min, pH 7.0, stable
60
-
-
15 min, complete loss of activity, enzyme GDT
60
-
-
15 min, complete loss of activity, enzyme GDT
additional information
-
-
pyridoxal phosphate, Ca2+, Mg2+ or Mn2+ protects against heat inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
pyridoxal phosphate, Ca2+, Mg2+ or Mn2+ protects against heat inactivation
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate, 52C, calcium phosphate gel, alumina C, Sephadex G-200
-