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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.2.3 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

EC Number Protein Variants Comment Organism
4.2.2.3 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

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

Organism

EC Number Organism UniProt Comment Textmining
4.2.2.3 Sphingomonas sp.
-
 isozyme A1-III
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.2.3 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)

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

Synonyms

EC Number Synonyms Comment Organism
4.2.2.3 A1-III
-
 Sphingomonas sp.
4.2.2.3 alginate lyase
-
 Sphingomonas sp.