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

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.26 phenylserine aldolase
IUBMB Comments
A pyridoxal-phosphate protein.
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This record set is specific for:
Pseudomonas putida
UNIPROT: Q59IT3
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The taxonomic range for the selected organisms is: Pseudomonas putida
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
phenylserine aldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-dehydro-2-deoxy-D-gluconate-6-phosphate malonate-semialdehyde-lyase
-
-
-
-
aldolase, phenylserine
-
-
-
-
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
-
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 SUBSTRATE
NATURAL PRODUCT
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
INHIBITOR
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, 30°C
4.6
L-erythro-3-phenylserine
pH 8.5, 30°C
29
L-Thr
pH 8.5, 30°C
1.3
L-threo-3-phenylserine
pH 8.5, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1300
L-allo-Thr
pH 8.5, 30°C
7900
L-erythro-3-phenylserine
pH 8.5, 30°C
580
L-Thr
pH 8.5, 30°C
2300
L-threo-3-phenylserine
pH 8.5, 30°C
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
300
cleavage of L-threo-3-phenylserine
4.3
reaction with glycine and benzaldehyde
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
reaction with glycine and benzyldehyde
8.5
reaction with L-threo-3-phenylserine
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 24-1
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q59IT3_PSEPU
357
0
38317
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
210000
gel filtration
37400
6 * 37400, calculation from nucleotide sequence
38000
6 * 38000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K213Q
loss of activity, disappearance of absorption maximum at 420 nm
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
30°C, 10 min, stable
663708
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Misono, H.; Maeda, H.; Tuda, K.; Ueshima, S.; Miyazaki, N.; Nagata, S.
Characterization of an inducible phenylserine aldolase from Pseudomonas putida 24-1
Appl. Environ. Microbiol.
71
4602-4609
2005
Pseudomonas putida (Q59IT3), Pseudomonas putida, Pseudomonas putida 24. Jan (Q59IT3)
Manually annotated by BRENDA team