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Literature summary for 2.4.1.10 extracted from

  • Mäntsälä, P.; Puntala, M.
    Comparison of levansucrase from Bacillus subtilis and from Bacillus amyloliquefaciens (1982), FEMS Microbiol. Lett., 13, 395-399.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
dithiothreitol complete inhibition at 1 mM Bacillus amyloliquefaciens
dithiothreitol complete inhibition at 1 mM Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
14
-
sucrose
-
Bacillus subtilis
19
-
sucrose
-
Bacillus amyloliquefaciens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Bacillus subtilis
-
-
extracellular
-
Bacillus amyloliquefaciens
-
-
membrane associated Bacillus subtilis 16020
-
membrane associated Bacillus amyloliquefaciens 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
amino acid composition Bacillus subtilis
additional information
-
amino acid composition Bacillus amyloliquefaciens
50000 52000 extracellular and membrane-associated enzyme forms, SDS-PAGE, gel filtration Bacillus subtilis
50000 52000 extracellular and membrane-associated enzyme forms, SDS-PAGE, gel filtration Bacillus amyloliquefaciens
52000
-
1 * 52000, extracellular and membrane-associated form, SDS-PAGE Bacillus subtilis
52000
-
1 * 52000, extracellular and membrane-associated form, SDS-PAGE Bacillus amyloliquefaciens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sucrose + (2,6-beta-D-fructosyl)n Bacillus subtilis activity is affected by sacU mutation glucose + (2,6-beta-D-fructosyl)n+1
-
?
sucrose + (2,6-beta-D-fructosyl)n Bacillus amyloliquefaciens activity is affected by sacU mutation glucose + (2,6-beta-D-fructosyl)n+1
-
?
sucrose + (2,6-beta-D-fructosyl)n Bacillus subtilis QB127 activity is affected by sacU mutation glucose + (2,6-beta-D-fructosyl)n+1
-
?

Organism

Organism UniProt Comment Textmining
Bacillus amyloliquefaciens
-
strain ATCC 23350
-
Bacillus subtilis
-
-
-
Bacillus subtilis QB127
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
203
-
purified enzyme Bacillus subtilis
415
-
purified enzyme Bacillus amyloliquefaciens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose + (2,6-beta-D-fructosyl)n
-
Bacillus subtilis glucose + (2,6-beta-D-fructosyl)n+1
-
?
sucrose + (2,6-beta-D-fructosyl)n
-
Bacillus amyloliquefaciens glucose + (2,6-beta-D-fructosyl)n+1
-
?
sucrose + (2,6-beta-D-fructosyl)n activity is affected by sacU mutation Bacillus subtilis glucose + (2,6-beta-D-fructosyl)n+1
-
?
sucrose + (2,6-beta-D-fructosyl)n activity is affected by sacU mutation Bacillus amyloliquefaciens glucose + (2,6-beta-D-fructosyl)n+1
-
?
sucrose + (2,6-beta-D-fructosyl)n
-
Bacillus subtilis QB127 glucose + (2,6-beta-D-fructosyl)n+1
-
?
sucrose + (2,6-beta-D-fructosyl)n activity is affected by sacU mutation Bacillus subtilis QB127 glucose + (2,6-beta-D-fructosyl)n+1
-
?

Subunits

Subunits Comment Organism
monomer 1 * 52000, extracellular and membrane-associated form, SDS-PAGE Bacillus subtilis
monomer 1 * 52000, extracellular and membrane-associated form, SDS-PAGE Bacillus amyloliquefaciens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Bacillus subtilis
25
-
assay at Bacillus amyloliquefaciens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
t1/2: 9 min Bacillus amyloliquefaciens
50
-
t1/2: 4 min Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.6 6
-
Bacillus subtilis
6 6.2
-
Bacillus amyloliquefaciens