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Literature summary for 4.2.2.7 extracted from

  • Zhao, W.; Garron, M.L.; Yang, B.; Xiao, Z.; Esko, J.D.; Cygler, M.; Linhardt, R.J.
    Asparagine 405 of heparin lyase II prevents the cleavage of glycosidic linkages proximate to a 3-O-sulfoglucosamine residue (2011), FEBS Lett., 585, 2461-2466.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.2.7

Protein Variants

Protein Variants Comment Organism
N405A site-directed mutagenesis, compared to the wild-type enzyme, the mutant shows broadened substrate specificity and cleaves the resistant linkage proximate to the 3-O-sulfoglucosamine residue Pedobacter heparinus
N405A/H406A site-directed mutagenesis Pedobacter heparinus
N405G site-directed mutagenesis, compared to the wild-type enzyme, the mutant shows broadened substrate specificity and cleaves the resistant linkage proximate to the 3-O-sulfoglucosamine residue Pedobacter heparinus
N405G/H406A site-directed mutagenesis Pedobacter heparinus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pedobacter heparinus HepII has a broad specificity ?
-
 ?

Organism

Organism UniProt Comment Textmining
Pedobacter heparinus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information HepII has a broad specificity Pedobacter heparinus ?
-
 ?
additional information substrates are HepI heparin-derived defined tetrasaccharides, overview Pedobacter heparinus ?
-
 ?

Synonyms

Synonyms Comment Organism
heparin lyase II
-
 Pedobacter heparinus
HepII
-
 Pedobacter heparinus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Pedobacter heparinus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Pedobacter heparinus

General Information

General Information Comment Organism
physiological function heparin and heparan sulfate contain a rare 3-O-sulfoglucosamine residue critical for anticoagulation and virus recognition, respectively. The glycosidic linkage proximate to this 3-O-sulfoglucosamine is resistant to cleavage by all heparin lyases Pedobacter heparinus