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Literature summary for 3.2.1.26 extracted from

  • Mera, A.; de Lima, M.Z.T.; Bernardes, A.; Garcia, W.; Muniz, J.R.C.
    Low-resolution structure, oligomerization and its role on the enzymatic activity of a sucrose-6-phosphate hydrolase from Bacillus licheniformis (2019), Amino Acids, 51, 599-610 .
    View publication on PubMed
Search for more literature for 3.2.1.26

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus licheniformis

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis Q65DN5
-
-
Bacillus licheniformis ATCC 14580 Q65DN5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus licheniformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose + H2O
-
 Bacillus licheniformis beta-D-fructose + alpha-D-glucose
-
 ?
sucrose + H2O
-
 Bacillus licheniformis ATCC 14580 beta-D-fructose + alpha-D-glucose
-
 ?

Subunits

Subunits Comment Organism
homodimer the enzyme forms homodimers in solution which are formed via the interaction of beta-sandwich domains Bacillus licheniformis

Synonyms

Synonyms Comment Organism
BlsacA
-
 Bacillus licheniformis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
 Bacillus licheniformis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
15 35 15°C: about % of maximal activity, 356°C: about % of maximal activity Bacillus licheniformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 7.5
-
 Bacillus licheniformis

pH Range

pH Minimum pH Maximum Comment Organism
6 9 pH 6.0: about 50% of maximal activity, pH 9.0: about 70% of maximal activity Bacillus licheniformis