Information on EC 2.6.1.54 - pyridoxamine-phosphate transaminase

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The expected taxonomic range for this enzyme is: Clostridium butyricum

EC NUMBER
COMMENTARY hide
2.6.1.54
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RECOMMENDED NAME
GeneOntology No.
pyridoxamine-phosphate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
pyridoxamine 5'-phosphate + 2-oxoglutarate = pyridoxal 5'-phosphate + D-glutamate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
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Vitamin B6 metabolism
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SYSTEMATIC NAME
IUBMB Comments
pyridoxamine-5'-phosphate:2-oxoglutarate aminotransferase (D-glutamate-forming)
Also acts, more slowly, on pyridoxamine.
CAS REGISTRY NUMBER
COMMENTARY hide
9074-84-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
IFO 3353
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + D-glutamate
show the reaction diagram
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about 8% of activity compared to pyridoxamine 5'-phosphate
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?
pyridoxamine + 2-oxoglutarate
pyridoxal + D-glutamate
show the reaction diagram
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about 25% of activity compared to pyridoxamine 5'-phosphate
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?
pyridoxamine 5'-phosphate + 2-oxoglutarate
pyridoxal 5'-phosphate + D-glutamate
show the reaction diagram
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r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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metal ions do not accelerate the reaction
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glutamate
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slight inhibition
diisopropyl phosphofluoride
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0.3 mM, complete inhibition
L-cysteine
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about 35% inhibition
pyridoxal 5'-phosphate
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product inhibition
additional information
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not inhibited by sulfhydryl compounds, e.g. PCMB, phenylmercuric acetate and mercuric chloride
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-aminobutyrate
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stimulation, 177% of non-stimulated activity
D-asparagine
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stimulation, 112% of non-stimulated activity
D-Cysteine
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stimulation, 135% of non-stimulated activity
D-methionine
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stimulation, 127% of non-stimulated activity
DL-Ornithine
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stimulation, 112% of non-stimulated activity
glycine
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stimulation, 137% of non-stimulated activity
L-asparagine
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stimulation, 112% of non-stimulated activity
L-glutamate
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stimulation, 166% of non-stimulated activity
L-lysine
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stimulation, 105% of non-stimulated activity
L-methionine
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stimulation, 114% of non-stimulated activity
L-ornithine
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stimulation, 112% of non-stimulated activity
additional information
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stimulating effect of amino compounds may be caused by disappearance of the inhibitory product of the reaction, pyridoxal 5'-phosphate, forming the corresponding Schiff base
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
2-oxoglutarate
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cosubstrate pyridoxamine 5'-phosphate, pH 8.0, 37°C
9
D-glutamate
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pH 8.0, 37°C
0.01
pyridoxal 5'-phosphate
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pH 8.0, 37°C
0.004
pyridoxamine 5'-phosphate
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pH 8.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, protamine treatment, DEAE-cellulose, hydroxylapatite, DEAE-Sephadex, Sephadex G-200, partial purification
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