Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.1.25 extracted from

  • Leoni, C.; Manzari, C.; Tran, H.; Golyshin, P.N.; Pesole, G.; Volpicella, M.; Ceci, L.R.
    Identification of an amylomaltase from the halophilic archaeon Haloquadratum walsbyi by functional metagenomics structural and functional insights (2022), Life, 12, 85.
    View publication on PubMed
Search for more literature for 2.4.1.25

Cloned(Commentary)

Cloned (Comment) Organism
cloning from a fosmid library, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, real-time PCR enzyme expression analysis, recombinant expression of His5-tagged enzyme in Escherichia coli strain Origami (DE3) Haloquadratum walsbyi

General Stability

General Stability Organism
80% loss of starch transglycosylation activity at 0.5-4 M NaCl Haloquadratum walsbyi

Inhibitors

Inhibitors Comment Organism Structure
NaCl 80% inhibition of starch transglycosylation activity at 0.5-4 M NaCl Haloquadratum walsbyi

Organism

Organism UniProt Comment Textmining
Haloquadratum walsbyi
-
 isolated from the crystallization pond 'Imperatrice' (36% of salinity, 30°C, pH 7.2) of the Margherita di Savoia saltern, located on the south-eastern coast of Italy on June 2017
-

Purification (Commentary)

Purification (Comment) Organism
recombinant expression of His5-tagged enzyme in Escherichia coli strain Origami (DE3) by nickel affinity chromatography, dialysis, and ultrafiltration Haloquadratum walsbyi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information transglycosylation activity assay using starch as donor substrate, and glucose, maltose, maltotriose, maltotetraose, maltohexaose, and maltoheptaose as acceptor substrates, starch degradation is determined by the iodine solution method. D-glucose ist the preferred acceptor substrate, higher activity also with maltose and maltohexaose, lower activity with maltotriose and maltotetraose. The activity of enzyme Hw-A is much higher than that of commercial amylase from Bacillus licheniformis Haloquadratum walsbyi ?
-
-
starch + D-glucose
-
 Haloquadratum walsbyi ?
-
 ?
starch + maltoheptaose
-
 Haloquadratum walsbyi ?
-
 ?
starch + maltohexaose
-
 Haloquadratum walsbyi ?
-
 ?
starch + maltose
-
 Haloquadratum walsbyi ?
-
 ?
starch + maltotetraose
-
 Haloquadratum walsbyi ?
-
 ?
starch + maltotriose
-
 Haloquadratum walsbyi ?
-
 ?

Synonyms

Synonyms Comment Organism
amylomaltase
-
 Haloquadratum walsbyi
Hw-A
-
 Haloquadratum walsbyi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
-
 Haloquadratum walsbyi

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 70 about 20% of maximal starch transglycosylation activity at 30-50°C, 80% at 60°C, and maximal activity at 70°C, loss of activity at 80°C, inactive at 90°C Haloquadratum walsbyi

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
72
-
 Tm of enzyme Hw-A Haloquadratum walsbyi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.2
-
-
 Haloquadratum walsbyi

pH Range

pH Minimum pH Maximum Comment Organism
5 8 about 20% of maximal starch transglycosylation activity at pH 6.2-8.0, maximal activity at pH 5.2 Haloquadratum walsbyi

General Information

General Information Comment Organism
evolution the enzyme belongs to the glycoside hydrolase family 77, GH77, which contains specific 4-alpha-glucanotransferases identified only in plants and algae (known as disproportionating or D-enzymes) and in prokaryotes (amylomaltases). Most of the GH77 enzymes reported in CAZy are of bacterial origin, while only few are from Archaea, plants, and algae. The gene encoding the amylomaltase in halophilic archaeon Haloquadratum walsbyi is not part of any operon involved in the metabolism of maltooligosaccharides or glycogen, as it has been found in bacteria. The gene has specific insertions yet unknown in homologous genes in prokaryotes, and present only in amylomaltase genes identified in the genomes of other Haloquadratum walsbyi strains. Amylomaltases can be classified in at least four distinct groups, structural features, overview Haloquadratum walsbyi