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Literature summary for 3.2.1.1 extracted from

  • Conrad, B.; Hoang, V.; Polley, A.; Hofemeister, J.
    Hybrid Bacillus amyloliquefaciens X Bacillus licheniformis alpha-amylases. Construction, properties and sequence determinants (1995), Eur. J. Biochem., 230, 481-490.
    View publication on PubMed
Search for more literature for 3.2.1.1

Protein Variants

Protein Variants Comment Organism
additional information hybrid Bacillus amyloliquefaciens X Bacillus licheniformis alpha-amylase, expression in Escherichia coli and Bacillus subtilis. The letters A and L in the hybrid names stand for the Bacillus amyloliquefaciens and the Bacillus licheniformis portion, respectively, and the numbers for the amino acid residues at the cross-over sites of the hybrid enzymes: Al76, Al108, AL112, AL142, AL147, AL149, AL151, LAL19-153, AL163, AL174 Bacillus licheniformis
additional information hybrid Bacillus amyloliquefaciens X Bacillus licheniformis alpha-amylase, expression in Escherichia coli and Bacillus subtilis. The letters A and L in the hybrid names stand for the Bacillus amyloliquefaciens and the Bacillus licheniformis portion, respectively, and the numbers for the amino acid residues at the cross-over sites of the hybrid enzymes: Al76, Al108, AL112, AL142, AL147, AL149, AL151, LAL19-153, AL163, AL174 Bacillus amyloliquefaciens

Organism

Organism UniProt Comment Textmining
Bacillus amyloliquefaciens
-
 hybrid Bacillus amyloliquefaciens X Bacillus licheniformis alpha-amylase
-
Bacillus licheniformis
-
 hybrid Bacillus amyloliquefaciens X Bacillus licheniformis alpha-amylase
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
p-nitrophenyl-alpha-D-maltopentaoside + H2O
-
 Bacillus licheniformis ?
-
 ?
p-nitrophenyl-alpha-D-maltopentaoside + H2O poor substrate Bacillus amyloliquefaciens ?
-
 ?
p-nitrophenyl-alpha-D-maltopentaoside + H2O good substrate Bacillus amyloliquefaciens ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 at pH 7.6 Bacillus amyloliquefaciens
45
-
 at pH 6.4 Bacillus amyloliquefaciens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
78
-
 half-life of the mosaic hybrid enzymes ALA76-151, ALA17-151: 5 min Bacillus licheniformis
78
-
 half-life of the mosaic hybrid enzymes ALA76-151, ALA17-151: 5 min Bacillus amyloliquefaciens
90
-
 half-life: 5 min Bacillus amyloliquefaciens
90
-
 30 min, 10-20% loss of activity of the hybrid enzymes AL76, AL108, and AL112, 35-50% loss of activity of the hybrid enzymes AL142, AL147, AL149, AL151, LAL19-163, AL163, and AL174. About 90% of activity after 30 min of the hybrid enzymes AL231, AL256 and AL263 Bacillus licheniformis
90
-
 30 min, 10-20% loss of activity of the hybrid enzymes AL76, AL108, and AL112, 35-50% loss of activity of the hybrid enzymes AL142, AL147, AL149, AL151, LAL19-163, AL163, and AL174. About 90% of activity after 30 min of the hybrid enzymes AL231, AL256 and AL263 Bacillus amyloliquefaciens
90
-
 half-life of hybrid enzymes: about 50 min for LA431, AL17, Al34 Bacillus licheniformis
90
-
 half-life of hybrid enzymes: about 50 min for LA431, AL17, Al34 Bacillus amyloliquefaciens
90
-
 half-life: 52 min Bacillus licheniformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.4 7.6 broad Bacillus licheniformis
6.4 7.6 broad Bacillus amyloliquefaciens