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Literature summary for 3.1.3.23 extracted from

  • Godinho, L.M.; de Sa-Nogueira, I.
    Characterization and regulation of a bacterial sugar phosphatase of the haloalkanoate dehalogenase superfamily, AraL, from Bacillus subtilis (2011), FEBS J., 278, 2511-2524.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.23

Cloned(Commentary)

Cloned (Comment) Organism
araL gene, the fourth cistron of the transcriptional unit araABDLMNPQ-abfA, DNA and amino acid sequence determination and analysis, overexpression of the His-tagged enzyme in Escherichia coli Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
G12D strain IQB849 carrying a single-base substitution C to A introduced in the hairpin region displaying an augment in araL'-'lacZ expression of about 30fold in the presence of inducer, the point mutation increases the free energy of the mRNA secondary structure Bacillus subtilis
additional information a translational fusion of the 5'-end of the araL gene to the lacZ reporter gene from Escherichia coli is constructed and integrated into the Bacillus subtilis chromosome. The construct comprises the araL ribosome-binding site, the initiation codon and a fusion between codon 10 of araL and codon 7 of Escherichia coli lacZ Bacillus subtilis
T9K/G12D the double point mutation, C to A and G to T, introduced a compensatory T in the other part of the stem, thus regenerating the stem-loop structure in strain IQB857 and drastically reducing the expression of araL'-'lacZ Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
24.96
-
 D-glucose 6-phosphate pH 7.0, 37°C Bacillus subtilis
27.36
-
 D-arabinose 5-phosphate pH 7.0, 37°C Bacillus subtilis
29.14
-
 D-xylulose 5-phosphate pH 7.0, 37°C Bacillus subtilis
34.89
-
 D-fructose 6-phosphate pH 7.0, 37°C Bacillus subtilis
40.74
-
 D-galactose 1-phosphate pH 7.0, 37°C Bacillus subtilis
40.78
-
 D-fructose 1,6-bisphosphate pH 7.0, 37°C Bacillus subtilis
50
-
 4-nitrophenyl phosphate pH 7.0, 37°C Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ absolutely required for catalysis, optimal at 15 mM Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28900
-
 x * 28900, about, sequence calculation Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bacillus subtilis AraL shows low specificity and catalytic activity towards several sugar phosphates, which are metabolic intermediates of the glycolytic and pentose phosphate pathways, substrate specificity, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
 araL gene
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 95% homogeneity Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O AraL is a phosphatase displaying activity towards the synthetic substrate 4-nitrophenyl phosphate, although there is no evidence that pNPPase activity is physiologically relevant Bacillus subtilis 4-nitrophenol + phosphate
-
 ?
D-arabinose 5-phosphate + H2O
-
 Bacillus subtilis D-arabinose + phosphate
-
 ?
D-fructose 1,6-bisphosphate + H2O
-
 Bacillus subtilis ?
-
 ?
D-fructose 6-phosphate + H2O
-
 Bacillus subtilis D-fructose + phosphate
-
 ?
D-galactose 1-phosphate + H2O
-
 Bacillus subtilis D-galactose + phosphate
-
 ?
D-glucose 6-phosphate + H2O
-
 Bacillus subtilis D-glucose + phosphate
-
 ?
D-xylulose 5-phosphate + H2O
-
 Bacillus subtilis D-xylulose + phosphate
-
 ?
additional information AraL shows low specificity and catalytic activity towards several sugar phosphates, which are metabolic intermediates of the glycolytic and pentose phosphate pathways, substrate specificity, overview Bacillus subtilis ?
-
 ?

Subunits

Subunits Comment Organism
? x * 28900, about, sequence calculation Bacillus subtilis

Synonyms

Synonyms Comment Organism
AraL
-
 Bacillus subtilis
More the enzyme is a member of the ubiquitous haloalkanoate dehalogenase superfamily Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
 recombinant enzyme Bacillus subtilis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 70 optimal activity at 37°C, no activity at 25°C, profile, overview Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.012
-
 4-nitrophenyl phosphate pH 7.0, 37°C Bacillus subtilis
1.49
-
 D-fructose 1,6-bisphosphate pH 7.0, 37°C Bacillus subtilis
2.49
-
 D-glucose 6-phosphate pH 7.0, 37°C Bacillus subtilis
2.75
-
 D-xylulose 5-phosphate pH 7.0, 37°C Bacillus subtilis
2.817
-
 D-fructose 6-phosphate pH 7.0, 37°C Bacillus subtilis
2.92
-
 D-arabinose 5-phosphate pH 7.0, 37°C Bacillus subtilis
4.28
-
 D-galactose 1-phosphate pH 7.0, 37°C Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 recombinant enzyme Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
4 9 although, at pH 8 and pH 9, the enzyme activity is considerably lower than at pH 7.0, the values are higher than at pH 6.0, no activity below pH 4.0, profile, overview Bacillus subtilis

General Information

General Information Comment Organism
metabolism context of araL within the arabinose metabolic operon araABDLMNPQ-abfA, as involved in the transport of L-arabinose oligomers. the ability of AraL to catabolize several secondary metabolites, related to detoxification of accidental accumulation of phosphorylated metabolites, requires regulation at the genetic level. Production of AraL is regulated by a structure in the translation initiation region of the mRNA, which most probably blocks access to the ribosome-binding site, preventing protein synthesis, existence of a genetic regulatory mechanism controlling the production of AraL, overview Bacillus subtilis
physiological function putative physiological role of the enzyme AraL in the detoxification of accidental accumulation of phosphorylated metabolites Bacillus subtilis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.00024
-
 4-nitrophenyl phosphate pH 7.0, 37°C Bacillus subtilis
0.0365
-
 D-fructose 1,6-bisphosphate pH 7.0, 37°C Bacillus subtilis
0.0807
-
 D-fructose 6-phosphate pH 7.0, 37°C Bacillus subtilis
0.0943
-
 D-xylulose 5-phosphate pH 7.0, 37°C Bacillus subtilis
0.0998
-
 D-glucose 6-phosphate pH 7.0, 37°C Bacillus subtilis
0.102
-
 D-galactose 1-phosphate pH 7.0, 37°C Bacillus subtilis
0.106
-
 D-arabinose 5-phosphate pH 7.0, 37°C Bacillus subtilis