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

BRENDA support

Literature summary for 3.2.1.78 extracted from

  • Yan, X.X.; An, X.M.; Gui, L.L.; Liang, D.C.
    From structure to function: insights into the catalytic substrate specificity and thermostability displayed by Bacillus subtilis mannanase BCman (2008), J. Mol. Biol., 379, 535-544.
    View publication on PubMed
Search for more literature for 3.2.1.78

Crystallization (Commentary)

Crystallization (Comment) Organism
to 1.45 A resolution, crystal shows a typical (beta/alpha)8 folding type. The catalytic acid/base Glu167 and nucleophile Glu266 are positioned on the beta4 and beta7 strands, respectively Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
E167A about 60% loss of catalytic efficiency Bacillus subtilis
E266A complete loss of activity Bacillus subtilis
H1A/H23A about 10% loss of catalytic efficiency Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis Q5PSP8 isoform BCman-GH26
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glucomannan + H2O from konjac flour Bacillus subtilis ?
-
 ?
ivory nut mannan + H2O
-
 Bacillus subtilis ?
-
 ?
locust bean gum + H2O
-
 Bacillus subtilis ?
-
 ?
additional information no substrates: mannobiose, mannotriose, mannotetraose, mannohexaose Bacillus subtilis ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information turnover numbers are 61.2 per s, substrate locust bean gum, wild-type, 75.1 per s, konjac flour, wild-type, 11 per s, ivory nut mannan, wild-type, 1.97 per s, locust bean gum, mutant E167A, 26.5 per s, locust bean gum, mutant H1A/H23A, respectively, at 37°C, pH 7.0 Bacillus subtilis