Literature summary for 4.2.2.3 extracted from

Yoon, H.J.; Hashimoto, W.; Miyake, O.; Okamoto, M.; Mikami, B.; Murata, K.
Overexpression in Escherichia coli, purification, and characterization of Sphingomonas sp. A1 alginate lyases (2000), Protein Expr. Purif., 19, 84-90.

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Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	isozymes A1-I and A1-II are not affected by addition of 1 mM EDTA, DTT, GSH, 2-mercaptoethanol, iodoacetic acid, and sugars, L-fucose, D-galactose, D-glucose, D-glucuronic acid, D-mannose, L-rhamnose, and D-xylose, no effect on isozymes A1-I and A1-II of Ca2+, Co2+, Mg2+, and Mn2+ at 1 mM	Sphingomonas sp.

Cloned(Commentary)

Cloned (Comment)	Organism
the 3 isozymes are natively expressed as 1 precursor molecule and are posttranslationally processed to monomeric forms, overexpression of all isozymes A1-I, A1-II, and A1-III in Escherichia coli	Sphingomonas sp.

Inhibitors

Inhibitors	Comment	Organism	Structure
Hg2+	40% inhibition at 1 mM of isozyme A1-I and A1-II	Sphingomonas sp.
additional information	isozymes A1-I and A1-II are not affected by addition of 1 mM EDTA, DTT, GSH, 2-mercaptoethanol, iodoacetic acid, and sugars, L-fucose, D-galactose, D-glucose, D-glucuronic acid, D-mannose, L-rhamnose, and D-xylose, no effect on isozymes A1-I and A1-II of Ca2+, Co2+, Mg2+, and Mn2+ at 1 mM	Sphingomonas sp.

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
25000	-	isozyme A1-II, gel filtration	Sphingomonas sp.
40000	-	isozyme A1-III, gel filtration	Sphingomonas sp.
63000	-	1 * 63000, A1-I, SDS-PAGE, 1 * 25000, A1-II, SDS-PAGE, 1 * 40000, A1-III, SDS-PAGE	Sphingomonas sp.
66000	-	isozyme A1-I, gel filtration	Sphingomonas sp.

Organism

Organism	UniProt	Comment	Textmining
Sphingomonas sp.	-	isoforms A1-I, A1-II, and A1-III	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	A1-I is autolytically cleaved into A1-II and A1-III, which shows different substrate specificities, therfore A1-I possesses 3 active sites, 1 protease and 2 alginate lyase sites	Sphingomonas sp.

Purification (Commentary)

Purification (Comment)	Organism
recombinant isozymes A1-I 11.2fold, A1-II 25.5fold, and A1-III 4.9fold, from Escherichia coli	Sphingomonas sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
45	-	purified isozyme A1-III	Sphingomonas sp.
73.1	-	purified isozyme A1-I	Sphingomonas sp.
109	-	purified isozyme A1-II	Sphingomonas sp.

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
alginate	isozyme A1-II and A1-I: endolytic cleavage of the glycosidic bonds, beta-elimination reaction, A1-II shows a preference for polyguluronate instead of polymannuronate	Sphingomonas sp.	unsaturated algino-oligosaccharides	A1-I produces mainly di- and trisaccharides, A1-II produces mainly tri- and tetrasaccharides	?
additional information	no activity with gellan, xanthan, and pectin of A1-I and A1-II	Sphingomonas sp.	?	-	?

Subunits

Subunits	Comment	Organism
monomer	1 * 63000, A1-I, SDS-PAGE, 1 * 25000, A1-II, SDS-PAGE, 1 * 40000, A1-III, SDS-PAGE	Sphingomonas sp.

Synonyms

Synonyms	Comment	Organism
alginate lyase	-	Sphingomonas sp.

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Sphingomonas sp.
45	-	isozyme A1-I	Sphingomonas sp.
70	-	isozyme A1-I	Sphingomonas sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
45	-	pH 7.2, 10 min, loss f 50% activity, isozyme A1-I	Sphingomonas sp.
50	-	pH 7.2, 10 min, loss f 50% activity, isozyme A1-I	Sphingomonas sp.

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.2	-	assay at	Sphingomonas sp.
8	-	isozymes A1-I and A1-II	Sphingomonas sp.

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Release 2023.1 (January 2023)