4.2.2.26: oligo-alginate lyase

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For detailed information about oligo-alginate lyase, go to the full flat file.

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

     4 Lyases

         4.2 Carbon-oxygen lyases

             4.2.2 Acting on polysaccharides

                4.2.2.26 oligo-alginate lyase

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1	Activating Compound
31	AA Sequence
5	Application
4	Cloned(Commentary)
1	General Information
18	Inhibitors
12	kcat/KM [mM/s]
13	KM Value [mM]
1	Localization
12	Metals/Ions
6	Molecular Weight [Da]
2	Natural Substrates/ Products (Substrates)
24	Organism
1	Pathway
6	pH Optimum
3	pH Stability
1	pI Value
1	Posttranslational Modification
19	Protein Variants
1	Purification (Commentary)
1	Reaction
16	Reference
6	Specific Activity [micromol/min/mg]
31	Substrates and Products (Substrate)
8	Subunits
10	Synonyms
1	Systematic Name
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2	Temperature Stability [°C]
10	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 4.2.2.26 - oligo-alginate lyase

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SYSTEMATIC NAME

IUBMB Comments

alginate oligosaccharide 4-deoxy-alpha-L-erythro-hex-4-enopyranuronate-(1?4)-hexananopyranuronate lyase

The enzyme degrades unsaturated oligosaccharides produced by the action of alginate lyases (EC 4.2.2.3 and EC 4.2.2.11) on alginate, by repeatedly removing the unsaturated residue from the non-reducing end until only unsaturated monosaccharides are left. The enzyme catalyses a beta-elimination reaction, generating a new unsaturated non-reducing end after removal of the pre-existing one.