4.2.2.3	acetyl-beta1,4-D-mannuronic acid	-	
4.2.2.3	alginate	incorporated into cells, substrate of alginate lyase isozymes A1-I, A1-II, and A1-III	
4.2.2.3	alginate	the bacterial alginate is degraded towards the end of cell culture by the wild-type strain ATCC 9046 in industrial alginate production	
4.2.2.3	alginate	Atu3025 is an exotype alginate lyase potentially involved in the assimilation of low-molecular-weight alginate in strain C58	
4.2.2.3	alginate	the alginate oligomers prepared by the lyase show growth-promoting activity on the roots of banana plantlets (Streptomyces sp. A5 is isolated from banana rhizosphere)	
4.2.2.3	alginate	the bifunctional alginate lyase shows substrate specificity for poly(alpha-L-guluronate) and poly(beta-D-mannuronate) units in alginate molecules, cf. EC 4.2.2.11	
4.2.2.3	alginate	a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid	
4.2.2.3	alginate	a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid	
4.2.2.3	alginate	AlgL plays a main role in alginate depolymerization	
4.2.2.3	alginate	increased expression of alginate lyase in mucoid strain 8830 leads to alginate degradation and increased cell detachment. When expressed from a regulated promoter, the alginate lyase can induce enhanced sloughing of cells because of degradation of the alginate. Possible role for lyase in the development of bacterial growth films