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H311A
0.3% of wild-type activity
R199A
4.3% of wild-type activity
W467A
0.45% of wild-type activity
Y365F
0.011% of wild-type activity
T185N
NCR-truncated protein, mutant has lost its M-producing capability but retained the ability to yield G units by almost completely degrading 2-aminobenzamide-labeled G4 chains. Mutant T185N can degrade 2-aminobenzamide-labeled G5 and 2-aminobenzamide-labeled M5 fractions at greater proportions than wild-type
A78S
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 820 U/mg, against poly(alpha-L-guluronic acid) 938 U/mg. Ratio of activities 1.1
A78S/T89I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 228 U/mg, against poly(alpha-L-guluronic acid) 34.3 U/mg. Ratio of activities 0.2
A78S/T89I/A217E
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 187 U/mg, against poly(alpha-L-guluronic acid) 29.8 U/mg. Ratio of activities 0.2
G26E
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 692 U/mg, against poly(alpha-L-guluronic acid) 787 U/mg. Ratio of activities 1.1
G26E/P39H
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 246 U/mg, against poly(alpha-L-guluronic acid) 19.5 U/mg. Ratio of activities 0.1. In the absence of Ca2+, no detectable activity against G-M linkages
G304V
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 828 U/mg, against poly(alpha-L-guluronic acid) 878 U/mg. Ratio of activities 1.1
I51M
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 731 U/mg, against poly(alpha-L-guluronic acid) 786 U/mg. Ratio of activities 1.1
I51M/T89I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 227 U/mg, against poly(alpha-L-guluronic acid) 18.8 U/mg. Ratio of activities 0.1
I51M/T89I/G304V
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 153 U/mg, against poly(alpha-L-guluronic acid) 13.3 U/mg. Ratio of activities 0.1
P39H
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 356 U/mg, against poly(alpha-L-guluronic acid) 37 U/mg. Ratio of activities 0.1
P39T
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 216 U/mg, against poly(alpha-L-guluronic acid) 71 U/mg. Ratio of activities 0.3
S35R
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 443 U/mg, against poly(alpha-L-guluronic acid) 448 U/mg. Ratio of activities 1.0
S35R/P39T
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 32.6 U/mg, against poly(alpha-L-guluronic acid) 6.9 U/mg. Ratio of activities 0.2
S35R/P39T/A224V
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 43 U/mg, against poly(alpha-L-guluronic acid) 3.4 U/mg. Ratio of activities 0.1
S37I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 53.8 U/mg, against poly(alpha-L-guluronic acid) 4.3 U/mg. Ratio of activities 0.1
S86L
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 31 U/mg, against poly(alpha-L-guluronic acid) 9.1 U/mg. Ratio of activities 0.3
T85A
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) 24.8 is U/mg, against poly(alpha-L-guluronic acid) 4.4 U/mg. Ratio of activities 0.32
T89I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 218 U/mg, against poly(alpha-L-guluronic acid) 31 U/mg. Ratio of activities 0.1
V6I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is858 U/mg, against poly(alpha-L-guluronic acid) 851 U/mg. Ratio of activities 1.0
V6I/T85A
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 23.6 U/mg, against poly(alpha-L-guluronic acid) 2.2 U/mg. Ratio of activities 0.1
H202L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H415A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
N201A
site-directed mutagenesis, inactive mutant
Q149A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R260A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R438A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y258A
site-directed mutagenesis, inactive mutant
Y450A
site-directed mutagenesis, inactive mutant
additional information
a truncated protein consisting of the catalytic module degrades alginate into unsaturated oligosaccharides with maximal activity at 30°C, 10°C lower than the temperature for wild-type. Thermostability ranges from 0 to 30°C and highest activity is at pH 7.0
additional information
-
engineering of different lyases, each of which cleaves only one of the four possible linkages in alginates: G-G, G-M, M-G, and M-M. The substitutions conferring altered specificity to the mutant enzymes are located in conserved regions in the polysaccharide lyase family 7 alginate lyases. Structure-function analyses suggests that the improved G-G specificity might be caused by increased affinity for nonproductive binding of the alternating G-M structure