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Literature summary for 5.1.3.17 extracted from

  • Mochizuki, H.; Yamagishi, K.; Suzuki, K.; Kim, Y.S.; Kimata, K.
    Heparosan-glucuronate 5-epimerase molecular cloning and characterization of a novel enzyme (2015), Glycobiology, 25, 735-744 .
    View publication on PubMed
Search for more literature for 5.1.3.17

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic tree, recombinant expression of soluble FLAG-tagged enzyme mutant lacking the transmembrane domain (N-terminal 33 amino acids) in insect cells using the baculovirus expression system Lissachatina fulica

Protein Variants

Protein Variants Comment Organism
additional information generation of a soluble form of the enzyme HG-5epi by replacement of the transmembrane domain (N-terminal 33 amino acids) with the immunoglobulin Kappa signal sequence and a FLAG tag Lissachatina fulica

Inhibitors

Inhibitors Comment Organism Structure
CHAPS
-
 Lissachatina fulica
additional information CHAPS and n-octyl beta-D-glucoside slightly inhibite the activity, the effect of Triton X-100 is negligible Lissachatina fulica
n-octyl-beta-D-glucoside
-
 Lissachatina fulica
sodium deoxycholate complete inhibition at 0.1% Lissachatina fulica

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane a type II transmembrane protein Lissachatina fulica 16020
-

Organism

Organism UniProt Comment Textmining
Lissachatina fulica O94923
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the recombinant FLAG-tagged enzyme mutant is probably N-glycosylated. The enzyme contains four possible N-glycosylation sites Lissachatina fulica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information recombinant enzyme HG-5epi, expressed in insect cells, epimerizes GlcA residues in heparosan, but not in N-sulfated-heparosan. Conversion of IdoA to GlcA is also catalyzed by HG-5epi when completely desulfated N-acetylated heparin is used as the substrate, indicating a reversible reaction mechanism. At equilibrium of the epimerization, the proportion of IdoA in the reaction product reaches up to 30% of total hexuronic acid. The recombinant enzyme catalyzes the epimerization of non-sulfated heparosan, product identification by using a combination of anion-exchange HPLC and postcolumn fluorescent labeling system Lissachatina fulica ?
-
 ?

Subunits

Subunits Comment Organism
? x * 68000, about, sequence calculation, x * 75000, recombinant FLAG-tagged enzyme mutant, SDS-PAGE Lissachatina fulica

Synonyms

Synonyms Comment Organism
heparosan-glucuronate 5-epimerase
-
 Lissachatina fulica
HG-5epi
-
 Lissachatina fulica
HNSG-5epi
-
 Lissachatina fulica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 recombinant FLAG-tagged enzyme mutant Lissachatina fulica

pH Range

pH Minimum pH Maximum Comment Organism
5 7.5 activity range, low activity below and above, recombinant FLAG-tagged enzyme mutant Lissachatina fulica

General Information

General Information Comment Organism
physiological function iduronic acid (IdoA) is a critical component of heparan sulfate in its interaction with functional proteins. Heparosan-N-sulfate-glucuronate 5-epimerase (HNSG-5epi) converts D-glucuronic acid (GlcA) residues in N-sulfated heparosan (NS-heparosan), as an intermediate in heparan sulfate biosynthesis, to IdoA. HG-5epi (heparosan-glucuronate 5-epimerase) is involved in acharan sulfate biosynthesis possesia distinct substrate specificity in Achatina fulica Lissachatina fulica