4.2.2.26: oligo-alginate lyase
This is an abbreviated version!
For detailed information about oligo-alginate lyase, go to the full flat file.
Word Map on EC 4.2.2.26
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4.2.2.26
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oligoalginate
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polysaccharide
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biofuels
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degradation
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polyg
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seaweed
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saccharification
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exolytic
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lyases
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shewanella
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metagenomics
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synthesis
- 4.2.2.26
- oligoalginate
- polysaccharide
-
biofuels
- degradation
- polyg
- seaweed
-
saccharification
-
exolytic
- lyases
- shewanella
-
metagenomics
- synthesis
Reaction
Cleavage of poly(4-deoxy-alpha-L-erythro-hexopyranuronoside) oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends into 4-deoxy-alpha-L-erythro-hex-4-enopyranuronate monosaccharides =
Synonyms
Alg17C, Oal, OalC17, OalC6, oalS17, oligoalginate lyase, Smlt2602
ECTree
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Engineering
Engineering on EC 4.2.2.26 - oligo-alginate lyase
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R236A
mutant exhibits endolytic activity. The overexpressed mutant protein (79.6 kDa) is proteolytically cleaved into the N-terminal 32.0-kDa and the C-terminal 47.6-kDa fragments. Both fragments show endolytic lyase activity
R236A
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mutant exhibits endolytic activity. The overexpressed mutant protein (79.6 kDa) is proteolytically cleaved into the N-terminal 32.0-kDa and the C-terminal 47.6-kDa fragments. Both fragments show endolytic lyase activity
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H208F
in addition to cleaving alginate-based substrates, mutant displays significant exolytic glucuronan activity
Y455F
significantly diminished yet measurable activity toward alginate and M and G blocks
H208F
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in addition to cleaving alginate-based substrates, mutant displays significant exolytic glucuronan activity
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Y455F
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significantly diminished yet measurable activity toward alginate and M and G blocks
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