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Literature summary for 4.1.2.48 extracted from

  • 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 (1998), Appl. Environ. Microbiol., 64, 549-554.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.2.48

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Pseudomonas sp.

Protein Variants

Protein Variants Comment Organism
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 Pseudomonas sp.
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 Pseudomonas sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.3
-
 L-threo-phenylserine pH 8.0, 30°C Pseudomonas sp.
7.4
-
 L-threo-beta-3,4-methylenedioxyphenylserine pH 8.0, 30°C Pseudomonas sp.
8.3
-
 L-threo-beta-3,4-dihydroxyphenylserine pH 8.0, 30°C Pseudomonas sp.
10.2
-
 L-erythro-phenylserine pH 8.0, 30°C Pseudomonas sp.
14.6
-
 L-allo-threonine pH 8.0, 30°C Pseudomonas sp.
14.7
-
 L-threonine pH 8.0, 30°C Pseudomonas sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
 4 * 38000, SDS-PAGE Pseudomonas sp.
145000
-
 gel filtration Pseudomonas sp.

Organism

Organism UniProt Comment Textmining
Pseudomonas sp. O50584
-
-
Pseudomonas sp. NCIMB 10558 O50584
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
41
-
 pH 8.0, 30°C Pseudomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-allo-threonine
-
 Pseudomonas sp. glycine + acetaldehyde
-
 r
L-allo-threonine
-
 Pseudomonas sp. NCIMB 10558 glycine + acetaldehyde
-
 r
L-erythro-phenylserine
-
 Pseudomonas sp. glycine + benzaldehyde
-
 ?
L-erythro-phenylserine
-
 Pseudomonas sp. NCIMB 10558 glycine + benzaldehyde
-
 ?
L-threo-beta-3,4-dihydroxyphenylserine
-
 Pseudomonas sp. glycine + 3,4-dihydroxybenzaldehyde
-
 ?
L-threo-beta-3,4-dihydroxyphenylserine
-
 Pseudomonas sp. NCIMB 10558 glycine + 3,4-dihydroxybenzaldehyde
-
 ?
L-threo-beta-3,4-methylenedioxyphenylserine
-
 Pseudomonas sp. ?
-
 ?
L-threo-beta-3,4-methylenedioxyphenylserine
-
 Pseudomonas sp. NCIMB 10558 ?
-
 ?
L-threo-phenylserine
-
 Pseudomonas sp. glycine + benzaldehyde
-
 ?
L-threonine
-
 Pseudomonas sp. glycine + acetaldehyde
-
 r
L-threonine
-
 Pseudomonas sp. NCIMB 10558 glycine + acetaldehyde
-
 r

Subunits

Subunits Comment Organism
tetramer 4 * 38000, SDS-PAGE Pseudomonas sp.

Synonyms

Synonyms Comment Organism
L-TA
-
 Pseudomonas sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
-
 Pseudomonas sp.
30
-
 assay at Pseudomonas sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
 40°C, 15 min, 50% loss of activity Pseudomonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Pseudomonas sp.
8 8.5
-
 Pseudomonas sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
5.5 9 30°C, 30 min, stable Pseudomonas sp.

Cofactor

Cofactor Comment Organism Structure
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 Pseudomonas sp.