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Literature summary extracted from

  • Ribeiro, L.F.; Furtado, G.P.; Lourenzoni, M.R.; Costa-Filho, A.J.; Santos, C.R.; Nogueira, S.C.; Betini, J.A., Polizeli, Mde L.; Murakami, M.T.; Ward, R.J.
    Engineering bifunctional laccase-xylanase chimeras for improved catalytic performance (2011), J. Biol. Chem., 286, 43026-4338.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.8 the chimeric enzymes, CorA-XynA and CorA-XynAG3, the parental enzyme XynA, and the thermostable variant XynAG3 are produced in Escherichia coli Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.8 additional information the fusion of the 1642-bp laccase (CorA) with either the 555-bp xylanase (XynA) or the thermostable variant (XynAG3) are performed by insertion of the xylanase into a surface loop of the laccase. The resulting chimeric constructs of 2197 bp contain a central region composed of the XynA or XynAG3 sequence flanked by the regions of the CorA encoding the N-terminal residues 1–216 (forming the 5' region of the chimera) and the C-terminal region comprising residues 217–513 of CorA. As a consequence, the final construct results in two linkage points between the laccase and xylanase domains Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.8 additional information
-
 1,4-beta-D-xylan Km for chimeric enzyme CorA-XynA at pH 6.5, 65°C: 6.3 mg/ml, KM for chimeric enzyme CorA-XynAG3 at pH 7.5, 75°C: 5.3 mg/ml, Km for xylanase XynA at pH 6.5, 55°C: 5.5 mg/ml, Km for thermostabel xylanase variant XynAG3 at pH 7.5, 70°C: 5.1 mg/ml Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.8 23000
-
 parental enzyme XynA, SDS-PAGE Bacillus subtilis
3.2.1.8 85500
-
 chimeric enzymes CorA-XynA and CorA-XynAG3, SDS-PAGE Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.8 Bacillus subtilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.8 the chimeric enzymes, CorA-XynA and CorA-XynAG3, the parental enzyme XynA, and the thermostable variant XynAG3 are produced in Escherichia coli Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.8 1,4-beta-D-xylan + H2O
-
 Bacillus subtilis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.8 endo-1,4-beta-xylanase
-
 Bacillus subtilis
3.2.1.8 XynA
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.8 55
-
 xylanase XynA Bacillus subtilis
3.2.1.8 65
-
 chimeric enzyme CorAXynA Bacillus subtilis
3.2.1.8 70
-
 thermostable variant XynAG3 and chimeric enzyme CorAXynAG3 Bacillus subtilis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.8 70
-
 the thermostable variant XynAG3 loses 90% of its activity after 10 min, and after 30 min no activity is observed. The chimeric CotA-XynAG3 retains 60% activity after 10 min and about 20% activity after 120 min. The half-lives of the chimeric enzymes XynAG3 and CotA-XynAG3 are 2.2 and 21 min Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.8 61
-
 1,4-beta-D-xylan pH 7.5, 70°C, thermostable xylanase variant XynAG3, calculated as D-xylose liberated from 1,4-beta-D-xylan per second Bacillus subtilis
3.2.1.8 65
-
 1,4-beta-D-xylan pH 7.5, 70°C, chimeric enzyme CorA-XynAG3, calculated as D-xylose liberated from 1,4-beta-D-xylan per second Bacillus subtilis
3.2.1.8 75
-
 1,4-beta-D-xylan pH 6.5, 65°C, chimeric enzyme CorA-XynA, calculated as D-xylose liberated from 1,4-beta-D-xylan per second Bacillus subtilis
3.2.1.8 82
-
 1,4-beta-D-xylan pH 6.5, 55°C, xylanase XynA, calculated as D-xylose liberated from 1,4-beta-D-xylan per second Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.8 6.5
-
 xylanase XynA and chimeric enzyme CorA-XynA Bacillus subtilis
3.2.1.8 7.5
-
 thermostabel xylanase variant XynAG3 and chimeric enzyme CorA-XynAG3 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
3.2.1.8 additional information
-
 1,4-beta-D-xylan kcat/Km for chimeric enzyme CorA-XynA at pH 6.5, 65°C: 12 ml/mg*ml, kcat/KM for chimeric enzyme CorA-XynAG3 at pH 7.5, 75°C: 12 ml/mg*ml, kcat/Km for xylanase XynA at pH 6.5, 55°C: 14.9 ml/mg*ml, kcat/Km for thermostabel xylanase variant XynAG3 at pH 7.5, 70°C: 11.9 ml/mg*ml Bacillus subtilis