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

BRENDA support

Literature summary extracted from

  • Furtado, G.; Ribeiro, L.; Lourenzoni, M.; Ward, R.
    A designed bifunctional laccase/beta-1,3-1,4-glucanase enzyme shows synergistic sugar release from milled sugarcane bagasse (2013), Protein Eng. Des. Sel., 26, 15-23.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.73 gene bglS, expression of mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme in Escherichia coli Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.73 the crystal structure of the enzyme is used for structure modelling, PDB ID 3O5S Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.73 additional information construction of a chimeric bifunctional laccase/beta-1,3-1,4-glucanase mutant enzyme by insertion fusion of the bglS and cotA genes, protein CotA, UniProt ID P07788, the approximation of the two catalytic domains in the chimeric enzyme, and the formation of an inter-domain interface increase catalytic activities,molecular dynamics simulations, overview. The laccase efficiency with substrate 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonic acid) is higher in the chimera, while the glucanase activity with lichenan shows a Kcat/KM value increased by 26%, a lower Km anf kcat. The beta-1,3-1,4-glucanase hydrolyzes plant cell wall beta-glucans, and the copper-dependent oxidase laccase catalyzes the oxidation of aromatic compounds with simultaneous reduction of oxygen to water. The mutant chimeric enzyme shows synergistic sugar release from milled sugarcane bagasse Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.73 2.1
-
 lichenan pH 6.0, 50°C, mutant chimeric enzyme Bacillus subtilis
3.2.1.73 3.1
-
 lichenan pH 6.0, 50°C, wild-type enzyme Bacillus subtilis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.73 28000
-
 x * 28000, recombinant enzyme, SDS-PAGE, x * 96000, recombinant CotA-BglS chimeric mutant enzyme, SDS-PAGE Bacillus subtilis
3.2.1.73 96000
-
 x * 28000, recombinant enzyme, SDS-PAGE, x * 96000, recombinant CotA-BglS chimeric mutant enzyme, SDS-PAGE Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.73 lichenan + H2O Bacillus subtilis
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus subtilis 168
-
 ?
-
 ?
3.2.1.73 additional information Bacillus subtilis the enzyme hydrolyzes plant cell wall beta-glucans ?
-
 ?
3.2.1.73 additional information Bacillus subtilis 168 the enzyme hydrolyzes plant cell wall beta-glucans ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.73 Bacillus subtilis P04957 gene bglS
-
3.2.1.73 Bacillus subtilis 168 P04957 gene bglS
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.73 recombinant mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme from Escherichia coli by nickel affinity chromatography and ultrafiltration Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.73 lichenan + H2O
-
 Bacillus subtilis ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus subtilis 168 ?
-
 ?
3.2.1.73 additional information the enzyme hydrolyzes plant cell wall beta-glucans Bacillus subtilis ?
-
 ?
3.2.1.73 additional information the enzyme hydrolyzes plant cell wall beta-glucans Bacillus subtilis 168 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.73 ? x * 28000, recombinant enzyme, SDS-PAGE, x * 96000, recombinant CotA-BglS chimeric mutant enzyme, SDS-PAGE Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
3.2.1.73 beta-1,3-1,4-glucanase
-
 Bacillus subtilis
3.2.1.73 BglS
-
 Bacillus subtilis
3.2.1.73 Lichenase
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.73 50
-
 recombinant mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme, substrate lichenan Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.73 1120
-
 lichenan pH 6.0, 50°C, mutant chimeric enzyme Bacillus subtilis
3.2.1.73 1220
-
 lichenan pH 6.0, 50°C, wild-type enzyme Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.73 6
-
 recombinant mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme, substrate lichenan Bacillus subtilis

General Information

EC Number General Information Comment Organism
3.2.1.73 evolution the beta-1,3-1,4-glucanases are family-16 glycosyl hydrolases that hydrolyze 1,4-beta-D-glycosidic linkages in beta-D-glucans containing mixed 1,3 and 1,4 linkages, which are abundant polysaccharide components found in the cell walls of grasses and the endosperm of cereals Bacillus subtilis
3.2.1.73 additional information the two glutamic acids in the EIDIEF motif are key residues involved in the hydrolytic activity Bacillus subtilis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.73 394
-
 lichenan pH 6.0, 50°C, wild-type enzyme Bacillus subtilis
3.2.1.73 534
-
 lichenan pH 6.0, 50°C, mutant chimeric enzyme Bacillus subtilis