Information on EC 4.1.2.26 - phenylserine aldolase and Organism(s) Pseudomonas putida and UniProt Accession Q59IT3

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Pseudomonas putida
UNIPROT: Q59IT3
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria


The taxonomic range for the selected organisms is: Pseudomonas putida

EC NUMBER
COMMENTARY hide
4.1.2.26
-
RECOMMENDED NAME
GeneOntology No.
phenylserine aldolase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-threo-3-phenylserine benzaldehyde-lyase (glycine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
37290-60-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 24-1
SwissProt
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
glycine + benzaldehyde
L-threo-3-phenylserine + L-erythro-3-phenylserine
show the reaction diagram
-
-
-
r
L-allo-Thr
glycine + acetaldehyde
show the reaction diagram
-
-
-
?
L-erythro-3-phenylserine
glycine + benzaldehyde
show the reaction diagram
no activity with D-erythro-3-phenylserine
-
-
r
L-Thr
glycine + acetaldehyde
show the reaction diagram
-
-
-
?
L-threo-3-phenylserine
glycine + benzaldehyde
show the reaction diagram
no activity with D-threo-3-phenylserine
-
-
r
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
0.7 mol of pyridoxal 5'-phosphate per mol of subunit, K213 of the enzyme probably forms a Schiff base with pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-(ethylamino)phenol
competitive against DL-threo-3-phenylserine
D-cycloserine
1 mM, 98% inhibition
DL-3-hydroxy-n-butyrate
20 mM, 30% inhibition
DL-3-hydroxynorvaline
20 mM, 49% inhibition
DL-3-hydroxyphenylethylamine
20 mM, 79% inhibition
hydroxylamine
1 mM, 97% inhibition
L-3-phenyllactate
10 mM, 39% inhibition
phenylhydrazine
1 mM, 52% inhibition
Semicarbazide
1 mM, 97% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22
L-allo-Thr
pH 8.5, 30C
4.6
L-erythro-3-phenylserine
pH 8.5, 30C
29
L-Thr
pH 8.5, 30C
1.3
L-threo-3-phenylserine
pH 8.5, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1300
L-allo-Thr
Pseudomonas putida
Q59IT3
pH 8.5, 30C
7900
L-erythro-3-phenylserine
Pseudomonas putida
Q59IT3
pH 8.5, 30C
580
L-Thr
Pseudomonas putida
Q59IT3
pH 8.5, 30C
2300
L-threo-3-phenylserine
Pseudomonas putida
Q59IT3
pH 8.5, 30C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.1
3-(ethylamino)phenol
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3
reaction with glycine and benzaldehyde
300
cleavage of L-threo-3-phenylserine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
reaction with glycine and benzyldehyde
8.5
reaction with L-threo-3-phenylserine
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37400
6 * 37400, calculation from nucleotide sequence
38000
6 * 38000, SDS-PAGE
210000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
6 * 37400, calculation from nucleotide sequence; 6 * 38000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
30C, 10 min, stable
663708
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, pH 7.2, 10 mM TES buffer, 0.01% 2-mercaptoethanol, 0.05 mM pyridoxal 5'-phosphate, 30% glycerol, stable for several months
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K213Q
loss of activity, disappearance of absorption maximum at 420 nm