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Literature summary extracted from

  • Ding, M.; Teng, Y.; Yin, Q.; Zhao, J.; Zhao, F.
    The N-terminal cellulose-binding domain of EGXA increases thermal stability of xylanase and changes its specific activities on different substrates (2008), Acta Biochim. Biophys. Sin. (Shanghai), 40, 949-954.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.8 additional information activity of rtEGXA depends on the concentration of Cl- Ampullaria crossean

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.8 full-length EGXA cloned into pFastBac vector and transformed into bacmid-containing Escherichia coli DH10Bac cells. Heterogeneously expressed in insect Tn5 cells Ampullaria crossean

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.8 additional information cellulose-binding domain decreases the recombinant EGXA's specific activities on p-nitrophenyl-beta-D-cellobioside and sodium carboxymethyl cellulose Ampullaria crossean

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.8 63000
-
 1 * 63000, SDS-PAGE, recombinant EGXA Ampullaria crossean

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.8 Ampullaria crossean Q7Z1V6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.8 on Ni-NTA resin Ampullaria crossean

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.8 stomach EGX, truncated version of EGXA Ampullaria crossean
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.8 0.9
-
 recombinant EGXA with p-nitrophenyl beta-D-cellobioside as substrate Ampullaria crossean
3.2.1.8 7.5
-
 recombinant EGXA with sodium carboxymethyl cellulose as substrate Ampullaria crossean
3.2.1.8 12.5
-
 wild-type EGX with sodium carboxymethyl cellulose as substrate Ampullaria crossean
3.2.1.8 40.3
-
 wild-type EGX with p-nitrophenyl beta-D-cellobioside as substrate Ampullaria crossean
3.2.1.8 275
-
 wild-type EGX with xylan as substrate Ampullaria crossean
3.2.1.8 391.8
-
 recombinant EGXA with xylan as substrate Ampullaria crossean

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.8 p-nitrophenyl beta-D-cellobioside + H2O
-
 Ampullaria crossean p-nitrophenol + beta-D-cellobiose
-
 ?
3.2.1.8 sodium carboxymethyl cellulose + H2O recombinant EGXA with a cellulose-binding domain binds to the cellulose with higher affinity than wild-type EGX, which lacks the cellulose-binding domain Ampullaria crossean ?
-
 ?
3.2.1.8 xylan + H2O
-
 Ampullaria crossean ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.8 monomer 1 * 63000, SDS-PAGE, recombinant EGXA Ampullaria crossean

Synonyms

EC Number Synonyms Comment Organism
3.2.1.8 EGXA
-
 Ampullaria crossean

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.8 45
-
 recombinant EGXA with xylan as substrate Ampullaria crossean

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.8 45
-
 recombinant EGXA and wild-type EGX lose activity quickly when Cl- is at a low concentration. In the presence of 50 mM Cl-, the rtEGXA’s activity loss is only 15% after 5 h incubation at 45°C. Wild-type EGX loses activity at a faster speed than the recombinant EGXA, in both 0.5 mM Cl- and 50 mM Cl-. Cellulose-binding domain increases thermal stability of the recombinant enzyme Ampullaria crossean

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.8 6
-
 recombinant EGXA with xylan as substrate Ampullaria crossean