4.2.2.25: gellan lyase
This is an abbreviated version!
For detailed information about gellan lyase, go to the full flat file.
Word Map on EC 4.2.2.25
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4.2.2.25
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polysaccharide
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tetrasaccharide
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depolymerization
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heteropolysaccharide
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beta-d-glucosidase
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glucuronyl
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monosaccharides
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oligosaccharide
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unsaturated
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lyases
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huge
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geobacillus
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bulgarian
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exopolysaccharide
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extracellularly
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rhamnose
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spring
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deacetylated
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stearothermophilus
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nonreducing
- 4.2.2.25
- polysaccharide
- tetrasaccharide
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depolymerization
- heteropolysaccharide
- beta-d-glucosidase
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glucuronyl
- monosaccharides
- oligosaccharide
- unsaturated
- lyases
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huge
-
geobacillus
-
bulgarian
- exopolysaccharide
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extracellularly
- rhamnose
-
spring
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deacetylated
- stearothermophilus
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nonreducing
Reaction
Eliminative cleavage of beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyluronate bonds of gellan backbone releasing tetrasaccharides containing a 4-deoxy-4,5-unsaturated D-glucopyranosyluronic acid at the non-reducing end. The tetrasaccharide produced from deacetylated gellan is beta-D-4-deoxy-Delta4-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp. =
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Posttranslational Modification
Posttranslational Modification on EC 4.2.2.25 - gellan lyase
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proteolytic modification
Bacillus sp. GL1, gellan lyase is first produced as a huge precursor protein (263 kDa) and then the protein is posttranslationally processed into extracellular mature form (140 kDa) through excising a C-terminal peptide of about 120 kDa
proteolytic modification
the 260 kDa enzyme is cleaved between the 1205Gly and 1206Leu residues to yield the mature 130 kDa form of the gellan lyase
proteolytic modification
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Bacillus sp. GL1, gellan lyase is first produced as a huge precursor protein (263 kDa) and then the protein is posttranslationally processed into extracellular mature form (140 kDa) through excising a C-terminal peptide of about 120 kDa
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proteolytic modification
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the 260 kDa enzyme is cleaved between the 1205Gly and 1206Leu residues to yield the mature 130 kDa form of the gellan lyase
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