Literature summary for 4.2.2.3 extracted from

Yoon, H.J.; Choi, Y.J.; Miyake, O.; Hashimoto, W.; Murata, K.; Mikami, B.
Effect of His192 mutation on the activity of alginate lyase A1-III from Sphingomonas species A1 (2001), J. Microbiol. Biotechnol., 11, 118-123.

No PubMed abstract available

Search for more literature for 4.2.2.3

Cloned(Commentary)

Cloned (Comment)	Organism
DNA sequence determination and analysis of the gene encoding isozyme A1-III, expression of wild-type and mutant H192A in Escherichia coli	Sphingomonas sp.

Protein Variants

Protein Variants	Comment	Organism
H192A	site-directed mutagenesis, mutation of active site His residue, mutant shows highly reduced activity, ut no conformational change, insensitive against metyl-4-nitrobenzenesulfonate treatment	Sphingomonas sp.

Inhibitors

Inhibitors	Comment	Organism	Structure
Methyl-4-nitrobenzenesulfonate	40% reduced activity with recombinant wild-type enzyme, no effect on mutant H192A	Sphingomonas sp.

Organism

Organism	UniProt	Comment	Textmining
Sphingomonas sp.	-	isozyme A1-III	-

Reaction

Reaction	Comment	Organism	Reaction ID
R2-beta-D-mannuronic acid-R1 = R2-OH + 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1	His192 is an active site residue, essential for activity	Sphingomonas sp.	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
alginate	recombinant and native wild-type enzymes show similar activity levels	Sphingomonas sp.	?	-	?

Synonyms

Synonyms	Comment	Organism
A1-III	-	Sphingomonas sp.
alginate lyase	-	Sphingomonas sp.

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Release 2023.1 (January 2023)