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Literature summary for 3.2.1.8 extracted from

  • Bu, Y.; Cui, Y.; Peng, Y.; Hu, M.; Tian, Y.; Tao, Y.; Wu, B.
    Engineering improved thermostability of the GH11 xylanase from Neocallimastix patriciarum via computational library design (2018), Appl. Microbiol. Biotechnol., 102, 3675-3685 .
    View publication on PubMed
Search for more literature for 3.2.1.8

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Neocallimastix patriciarum

Protein Variants

Protein Variants Comment Organism
G201L increase in melting temperature by 8.5 degrees Neocallimastix patriciarum
N38Y/F52W/G56Y/G201L increase in melting temperature by 14 degrees Neocallimastix patriciarum

Organism

Organism UniProt Comment Textmining
Neocallimastix patriciarum Q9UV68
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beechwood xylan + H2O
-
 Neocallimastix patriciarum xylooligosaccharides + ?
-
 ?

Subunits

Subunits Comment Organism
? x * 25827, mutant N38Y/F52W/G56Y/G201L, calculated, x * 25800, SDS-PAGE Neocallimastix patriciarum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
 wild-type Neocallimastix patriciarum
65
-
 mutant N38Y/F52W/G56Y/G201L Neocallimastix patriciarum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
 20 min, wild-type, 70% loss of activity, mutant N38Y/F52W/G56Y/G201L, about 10% loss of activity Neocallimastix patriciarum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 both wild-type and mutant N38Y/F52W/G56Y/G201L Neocallimastix patriciarum