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Literature summary extracted from

  • Suyotha, W.; Yano, S.; Takagi, K.; Rattanakit-Chandet, N.; Tachiki, T.; Wakayama, M.
    Domain structure and function of alpha-1,3-glucanase from Bacillus circulans KA-304, an enzyme essential for degrading basidiomycete cell walls (2013), Biosci. Biotechnol. Biochem., 77, 639-647.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.59 recombinant expression of wild-type and deletion mutant enzymes in Escherichia coli strain Rosetta-gami B (DE3), secretion of enzyme to the culture medium, recombinant expression as GFP-tagged proteins, overview Niallia circulans

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.59 additional information generation of domain deletion enzyme mutants lacking discoidin domains DS1 and DS2, the uncharacterized conserved domain, and/or carbohydrate binding module family 6, AglDELTADS1, AglDELTADS1CB6, AglDELTADS1CB6DS2, and AglDELTADCD-UCD. Only the DS1 domain deletion mutant shows some activity, the other mutants show only residual or no activity, overview Niallia circulans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.59 additional information
-
 additional information Km is 5.6 mg/ml for alpha-1,3-glucan with the recombinant wild-type enzyme, pH 6.5, 30°C, kinetics of recombinant wild-type and domain deletion mutants, overview Niallia circulans

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.59 Niallia circulans
-
-
-
3.2.1.59 Niallia circulans KA-304
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.59 recombinant secreted wild-type and deletion mutant enzymes from Escherichia coli strain Rosetta-gami B (DE3) culture supernatant by dialysis, anion exchange chromatography, ammonium sulfate fractionation and hydrophobic interaction chromatography Niallia circulans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.59 alpha-1,3-glucan + H2O prepared from sucrose using Streptococcus mutans ATCC700610 glucosyltransferase I Niallia circulans ?
-
 ?
3.2.1.59 alpha-1,3-glucan + H2O prepared from sucrose using Streptococcus mutans ATCC700610 glucosyltransferase I Niallia circulans KA-304 ?
-
 ?
3.2.1.59 fungal cell walls + H2O
-
 Niallia circulans ?
-
 ?
3.2.1.59 fungal cell walls + H2O
-
 Niallia circulans KA-304 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.59 More the enzyme structure includes an N-terminal discoidin domain (DS1), a carbohydrate binding module family 6 (CB6), threonine and proline repeats (TPs), a second discoidin domain (DS2), an uncharacterized conserved domain (UCD), and a C-terminal catalytic domain Niallia circulans

Synonyms

EC Number Synonyms Comment Organism
3.2.1.59 Agl-KA
-
 Niallia circulans
3.2.1.59 alpha-1,3-glucanase
-
 Niallia circulans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.59 30
-
-
 Niallia circulans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.59 additional information
-
 additional information the amount of reducing sugar in the supernatant of the enzyme assay is determined Niallia circulans
3.2.1.59 91.3
-
 alpha-1,3-glucan recombinant wild-type enzyme, pH 6.5, 30°C Niallia circulans
3.2.1.59 106.6
-
 alpha-1,3-glucan recombinant mutant AglDELTADS1, pH 6.5, 30°C Niallia circulans
3.2.1.59 130.7
-
 alpha-1,3-glucan recombinant mutant AglDELTADS1CB6, pH 6.5, 30°C Niallia circulans
3.2.1.59 134.4
-
 alpha-1,3-glucan recombinant mutant AglDELTADS1CB6DS2, pH 6.5, 30°C Niallia circulans
3.2.1.59 158.7
-
 alpha-1,3-glucan recombinant mutant AglDELTADCD-UCD, pH 6.5, 30°C Niallia circulans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.59 6.5
-
-
 Niallia circulans

General Information

EC Number General Information Comment Organism
3.2.1.59 malfunction domain deletion enzyme mutants lacking discoidin domains DS1 and DS2 and carbohydrate binding module family 6 domain exhibit lower alpha-1,3-glucan-hydrolyzing and substrate-binding activities than the wild-type enzyme. A dramatic decrease in protoplast formation in the Schizophyllum commune mycelium is observed given only a domain DS1 deletion Niallia circulans
3.2.1.59 additional information discoidin domains DS1 and DS2 and carbohydrate binding module family 6 domain are involved in alpha-1,3-glucan and fungal cell wall substrate binding, while the uncharacterized conserved domain is not, overview Niallia circulans
3.2.1.59 physiological function the enzyme is involved in fungal cell wall degradation Niallia circulans