Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Mikami, B.; Ban, M.; Suzuki, S.; Yoon, H.J.; Miyake, O.; Yamasaki, M.; Ogura, K.; Maruyama, Y.; Hashimoto, W.; Murata, K.
    Induced-fit motion of a lid loop involved in catalysis in alginate lyase A1-III (2012), Acta Crystallogr. Sect. D, 68, 1207-1216.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.2.3 sequence comparison of PL-5 alginate lyase, recombinant wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS Sphingomonas sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.2.3 purified recombinant mutants H192A and Y246F complexed with substrate 4-deoxy-L-erythro-hex-4-ene-pyranosyluronate-(mannuronate)2-mannuronic acid, hanging drop vapour diffusion method, 10 mg/ml protein in solution is mixed with reservoir solution containing 24% w/v PEG 4000, 0.3 M ammonium acetate, 0.1 M sodium citrate pH 5.5, 20°C, 1 month, X-ray diffraction structure determination and analysis at 2.2 resolution, final models of the complex forms, which comprise two monomers (of 353 amino-acid residues each), 268-287 water molecules and two tetrasaccharide substrates Sphingomonas sp.

Protein Variants

EC Number Protein Variants Comment Organism
4.2.2.3 G60A site-directed active site mutagenesis, the mutant shows 41.4% reduced activity compared to the wild-type enzyme Sphingomonas sp.
4.2.2.3 H192A site-directed active site mutagenesis, almost inactive mutant Sphingomonas sp.
4.2.2.3 M62P site-directed active site mutagenesis, two components of M62P, intactM62P and nicked M62P, are found during purification of the mutant enzyme, the nicked form is inactive, the intact form shows 56% reduced activity compared to the wild-type enzyme Sphingomonas sp.
4.2.2.3 R67A site-directed active site mutagenesis, the mutant shows 92.5% reduced activity compared to the wild-type enzyme Sphingomonas sp.
4.2.2.3 Y246F site-directed active site mutagenesis, almost inactive mutant Sphingomonas sp.
4.2.2.3 Y68F site-directed active site mutagenesis, the mutant shows 95% reduced activity compared to the wild-type enzyme Sphingomonas sp.
4.2.2.3 Y80F site-directed active site mutagenesis, the mutant shows 47% reduced activity compared to the wild-type enzyme Sphingomonas sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.2.3 additional information
-
 additional information kinetics of wild-type and mutant enzymes, overview Sphingomonas sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.2.3 additional information Sphingomonas sp. alginate lyase A1-III is a beta-D-mannuronosyl linkage-specific enzyme that acts on alginate tetrasaccharide as the minimum substrate and produces disaccharides and trisaccharides from alginate ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.2.3 Sphingomonas sp. Q75WP3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.2.3 recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS Sphingomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.2.3 4-deoxy-L-erythro-hex-4-ene-pyranosyluronate-(mannuronate)2-mannuronic acid bound in the active cleft at subsites -3 to +1, the glycosidic linkage is cleaved existed between subsites -1 and +1 Sphingomonas sp. ?
-
 ?
4.2.2.3 additional information alginate lyase A1-III is a beta-D-mannuronosyl linkage-specific enzyme that acts on alginate tetrasaccharide as the minimum substrate and produces disaccharides and trisaccharides from alginate Sphingomonas sp. ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.2.3 alginate lyase A1-III
-
 Sphingomonas sp.
4.2.2.3 PL-5 alginate lyase
-
 Sphingomonas sp.

General Information

EC Number General Information Comment Organism
4.2.2.3 evolution sequence comparison of the PL-5 alginate lyase Sphingomonas sp.
4.2.2.3 additional information structure-fucntion analysis, superposition of the open and closed lid loops suggests that the conformational change results in near-rigid-body motion, The open-closed movement of the lid loop decreases the accessible surface area by covering the active-site cleft., overview Sphingomonas sp.