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Literature summary for 2.4.1.226 extracted from

  • Ogawa, H.; Shionyu, M.; Sugiura, N.; Hatano, S.; Nagai, N.; Kubota, Y.; Nishiwaki, K.; Sato, T.; Gotoh, M.; Narimatsu, H.; Shimizu, K.; Kimata, K.; Watanabe, H.
    Chondroitin sulfate synthase-2/chondroitin polymerizing factor has two variants with distinct function (2010), J. Biol. Chem., 285, 34155-34167.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.226

Cloned(Commentary)

Cloned (Comment) Organism
individual overexpression of soluble forms of FLAG- and Myc-tagged splice variants CSS2A and CSS2B in COS-7 cells, co-expression with CSS1. Whereas CSS2A facilitates chondroitin sulfate biosynthesis, CSS2B inhibits it. Analysis of transcription levels of CSS2 variants Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum both splice variants CSS2A and CSS2B Mus musculus 5783
-
Golgi apparatus both splice variants CSS2A and CSS2B Mus musculus 5794
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ activates Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus CSS1, CSS2, and CSS3 contain two glycosyltransferase domains, beta-3 domain at the N-terminal region and beta-4 domain at the C-terminal region and exhibit dual enzymatic activities of N-acetylgalactosaminyltransferase-II, GalNAcTII, and glucuronyltransferase-II, GlcAT-II. Chondroitin sulfate glucuronyltransferase, similarly containing two glycosyltransferase domains, shows only GlcAT-I activity, EC 2.4.1.135 ?
-
 ?
additional information Mus musculus C57/BL6 CSS1, CSS2, and CSS3 contain two glycosyltransferase domains, beta-3 domain at the N-terminal region and beta-4 domain at the C-terminal region and exhibit dual enzymatic activities of N-acetylgalactosaminyltransferase-II, GalNAcTII, and glucuronyltransferase-II, GlcAT-II. Chondroitin sulfate glucuronyltransferase, similarly containing two glycosyltransferase domains, shows only GlcAT-I activity, EC 2.4.1.135 ?
-
 ?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan Mus musculus
-
 UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan
-
 ?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan Mus musculus C57/BL6
-
 UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-
Mus musculus C57/BL6
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Mus musculus
-
cartilage
-
 Mus musculus
-
fibroblast
-
 Mus musculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0000006
-
 recombinant CSS2B variant in COS-7 cells, pH 6.2, 37°C Mus musculus
0.0000024
-
 recombinant CSS2A variant in COS-7 cells, pH 6.2, 37°C Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information CSS1, CSS2, and CSS3 contain two glycosyltransferase domains, beta-3 domain at the N-terminal region and beta-4 domain at the C-terminal region and exhibit dual enzymatic activities of N-acetylgalactosaminyltransferase-II, GalNAcTII, and glucuronyltransferase-II, GlcAT-II. Chondroitin sulfate glucuronyltransferase, similarly containing two glycosyltransferase domains, shows only GlcAT-I activity, EC 2.4.1.135 Mus musculus ?
-
 ?
additional information CSS2A exhibits both GalNAcT-II and GlcAT-II activities, CSS2B also shows both GalNAcT-II and GlcAT-II activities, but they are 82.8% and 26.5% that of CSS2A, respectively Mus musculus ?
-
 ?
additional information CSS1, CSS2, and CSS3 contain two glycosyltransferase domains, beta-3 domain at the N-terminal region and beta-4 domain at the C-terminal region and exhibit dual enzymatic activities of N-acetylgalactosaminyltransferase-II, GalNAcTII, and glucuronyltransferase-II, GlcAT-II. Chondroitin sulfate glucuronyltransferase, similarly containing two glycosyltransferase domains, shows only GlcAT-I activity, EC 2.4.1.135 Mus musculus C57/BL6 ?
-
 ?
additional information CSS2A exhibits both GalNAcT-II and GlcAT-II activities, CSS2B also shows both GalNAcT-II and GlcAT-II activities, but they are 82.8% and 26.5% that of CSS2A, respectively Mus musculus C57/BL6 ?
-
 ?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan
-
 Mus musculus UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan
-
 ?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan chondroitin sulfate A-8, chondroitin sulfate C-8,chondroitin-8, and GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-methoxy-phenyl as acceptor substrates Mus musculus UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan
-
 ?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan
-
 Mus musculus C57/BL6 UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan
-
 ?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan chondroitin sulfate A-8, chondroitin sulfate C-8,chondroitin-8, and GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-methoxy-phenyl as acceptor substrates Mus musculus C57/BL6 UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan
-
 ?

Subunits

Subunits Comment Organism
More homology modeling of the N-terminal domain of CSS2 variants, three-dimensional structure of the N-terminal domain of CSS2 variants showing differences in the catalytic sites, overview Mus musculus

Synonyms

Synonyms Comment Organism
GlcAT-II
-
 Mus musculus
glucuronyltransferase-II
-
 Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2
-
 assay at Mus musculus

General Information

General Information Comment Organism
malfunction reduced glucuronyltransferase activity for splice variant CSS2B and no polymerizing activity for CSS2B co-expressed with CSS1, in contrast to splice variant CSS2A co-expressed with CSS1 Mus musculus
additional information either of CSS2A, CSS2B, and CSS1/ChSy-1 heterogeneously and homogeneously interact with each other, suggesting that they form a complex of multimers Mus musculus
physiological function CSS2 is involved in elongation of chondroitin sulfate chains. Splice variant CSS2A facilitates chondroitin sulfate biosynthesis, while splice variant CSS2B inhibits it, molecular modeling and mechanisms of chondroitin sulfate biosynthesis regulation, overview. The ratio of CSS2 variants correlates with age-dependent change of chondroitin sulfate chain length in brain of mice Mus musculus