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Literature summary for 3.2.1.26 extracted from

  • Guo, P.C.; Wang, Q.; Wang, Z.; Dong, Z.; He, H.; Zhao, P.
    Biochemical characterization and functional analysis of invertase Bmsuc1 from silkworm, Bombyx mori (2018), Int. J. Biol. Macromol., 107, 2334-2341 .
    View publication on PubMed
Search for more literature for 3.2.1.26

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 (DE3) Bombyx mori

Protein Variants

Protein Variants Comment Organism
D181A mutant enzyme shows no detectable activity Bombyx mori
D63A catalytic efficiency (kcat/Km) of the mutant enzyme is 1.6% compared to the catalytic efficiency of the wild-type enzyme Bombyx mori
E234A catalytic efficiency (kcat/Km) of the mutant enzyme is 1.8% compared to the catalytic efficiency of the wild-type enzyme Bombyx mori

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.37
-
 sucrose pH 7.5, 37°C, wild-type enzyme Bombyx mori
9.85
-
 sucrose pH 7.5, 37°C, mutant enzyme E234A Bombyx mori
13.14
-
 sucrose pH 7.5, 37°C, mutant enzyme D63A Bombyx mori

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Bombyx mori
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53800
-
 mature protein after removal of the signal peptide, calculated from sequence Bombyx mori
57000
-
 gel filtration Bombyx mori

Organism

Organism UniProt Comment Textmining
Bombyx mori B2DD57
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bombyx mori

Source Tissue

Source Tissue Comment Organism Textmining
midgut the enzyme is highly and specifically expressed in the midgut and silk gland Bombyx mori
-
silk gland expressed at high levels at both the transcriptional and translational levels. The enzyme might function as a digestive enzyme to hydrolyze sugar in the silk gland lumen Bombyx mori
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose + H2O
-
 Bombyx mori beta-D-fructose + alpha-D-glucose
-
 ?

Subunits

Subunits Comment Organism
monomer
-
 Bombyx mori

Synonyms

Synonyms Comment Organism
Bmsuc1
-
 Bombyx mori

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
 Bombyx mori

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 60 25°C: about 30% of maximal activity, 60°C: about 30% of maximal activity Bombyx mori

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
53.8
-
 Tm-value, thermal denaturations transition of Bmsuc1 is a cooperative process Bombyx mori

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.32
-
 sucrose pH 7.5, 37°C, mutant enzyme E234A Bombyx mori
0.38
-
 sucrose pH 7.5, 37°C, mutant enzyme D63A Bombyx mori
2.43
-
 sucrose pH 7.5, 37°C, wild-type enzyme Bombyx mori

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8
-
 Bombyx mori

pH Range

pH Minimum pH Maximum Comment Organism
5 9 pH 5.0: about 60% of maximal activity, pH 9.0: about 75% of maximal activity Bombyx mori

pI Value

Organism Comment pI Value Maximum pI Value
Bombyx mori mature protein after removal of the signal peptide, calculated from sequence
-
 4.8

General Information

General Information Comment Organism
physiological function the enzyme might function as a digestive enzyme to hydrolyze sugar in the silk gland lumen Bombyx mori

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.029
-
 sucrose pH 7.5, 37°C, mutant enzyme D63A Bombyx mori
0.032
-
 sucrose pH 7.5, 37°C, mutant enzyme E234A Bombyx mori
1.77
-
 sucrose pH 7.5, 37°C, wild-type enzyme Bombyx mori