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Information on EC 4.1.2.48 - low-specificity L-threonine aldolase and Organism(s) Pseudomonas sp. and UniProt Accession O50584

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.48 low-specificity L-threonine aldolase
IUBMB Comments
Requires pyridoxal phosphate. The low-specificity L-threonine aldolase can act on both L-threonine and L-allo-threonine [1,2]. The enzyme from Escherichia coli can also act on L-threo-phenylserine and L-erythro-phenylserine . The enzyme can also catalyse the aldol condensation of glycolaldehyde and glycine to form 4-hydroxy-L-threonine, an intermediate of pyridoxal phosphate biosynthesis . Different from EC 4.1.2.5, L-threonine aldolase, and EC 4.1.2.49, L-allo-threonine aldolase.
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This record set is specific for:
Pseudomonas sp.
UNIPROT: O50584
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The taxonomic range for the selected organisms is: Pseudomonas sp.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
threonine aldolase, low-specificity l-threonine aldolase, serine hydroxy-methyl transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LtaE
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-threonine/L-allo-threonine acetaldehyde-lyase (glycine-forming)
Requires pyridoxal phosphate. The low-specificity L-threonine aldolase can act on both L-threonine and L-allo-threonine [1,2]. The enzyme from Escherichia coli can also act on L-threo-phenylserine and L-erythro-phenylserine [4]. The enzyme can also catalyse the aldol condensation of glycolaldehyde and glycine to form 4-hydroxy-L-threonine, an intermediate of pyridoxal phosphate biosynthesis [3]. Different from EC 4.1.2.5, L-threonine aldolase, and EC 4.1.2.49, L-allo-threonine aldolase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-allo-threonine
glycine + acetaldehyde
show the reaction diagram
-
-
-
r
L-erythro-phenylserine
glycine + benzaldehyde
show the reaction diagram
-
-
-
?
L-threo-beta-3,4-dihydroxyphenylserine
glycine + 3,4-dihydroxybenzaldehyde
show the reaction diagram
-
-
-
?
L-threo-beta-3,4-methylenedioxyphenylserine
?
show the reaction diagram
-
-
-
?
L-threo-phenylserine
glycine + benzaldehyde
show the reaction diagram
-
-
-
?
L-threonine
glycine + acetaldehyde
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
contains 1 mol of pyridoxal 5'-phosphate per mol of 38000 da subunit. Lys207 probably functions as an essential catalytic residue, forming an internal Schiff base with the pyridoxal 5'-phosphate of the enzyme to catalyze the reversible aldol reaction
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14.6
L-allo-threonine
pH 8.0, 30°C
10.2
L-erythro-phenylserine
pH 8.0, 30°C
8.3
L-threo-beta-3,4-dihydroxyphenylserine
pH 8.0, 30°C
7.4
L-threo-beta-3,4-methylenedioxyphenylserine
pH 8.0, 30°C
7.3
L-threo-phenylserine
pH 8.0, 30°C
14.7
L-threonine
pH 8.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41
pH 8.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
145000
gel filtration
38000
4 * 38000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 38000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K207A
the mutant enzyme shows no detectable enzyme activity. The mutant enzyme show the disappearance of the absorption maximum at 420 nm, indicating that the Schiff base linkage between the epsilon-amino group of the active-site lysine residue and the pyridoxal 5'-phosphate cofactor aldehyde group of the wild type is not present in the mutant enzyme
K207R
the mutant enzyme shows a specific activity of about 1000 times lower than that of the wild-type enzyme. The mutant enzyme show the disappearance of the absorption maximum at 420 nm, indicating that the Schiff base linkage between the epsilon-amino group of the active-site lysine residue and the pyridoxal 5'-phosphate cofactor aldehyde group of the wild type is not present in the mutant enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
30°C, 30 min, stable
441433
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
40°C, 15 min, 50% loss of activity
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
Liu, J.Q.; Ito, S.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.; Yamada, H.
Gene cloning, nucleotide sequencing, and purification and characterization of the low-specificity L-threonine aldolase from Pseudomonas sp. strain NCIMB 10558
Appl. Environ. Microbiol.
64
549-554
1998
Pseudomonas sp. (O50584), Pseudomonas sp., Pseudomonas sp. NCIMB 10558 (O50584)
Manually annotated by BRENDA team