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Literature summary for 2.4.1.175 extracted from

  • Shimbo, M.; Suzuki, R.; Fuseya, S.; Sato, T.; Kiyohara, K.; Hagiwara, K.; Okada, R.; Wakui, H.; Tsunakawa, Y.; Watanabe, H.; Kimata, K.; Narimatsu, H.; Kudo, T.; Takahashi, S.
    Postnatal lethality and chondrodysplasia in mice lacking both chondroitin sulfate N-acetylgalactosaminyltransferase-1 and -2 (2017), PLoS ONE, 12, e0190333 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.175

Cloned(Commentary)

Cloned (Comment) Organism
gene Cpha266_2341, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of MBP-tagged enzyme in Escherichia coli strain XJa from plasmid CpCS/pMAL-c4E Chlorobium phaeobacteroides

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, 3fold activation at 1-10 mM Chlorobium phaeobacteroides
Mn2+ required, 18fold activation at 1-10 mM Chlorobium phaeobacteroides

Organism

Organism UniProt Comment Textmining
Chlorobium phaeobacteroides A1BIV2
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Chlorobium phaeobacteroides DSM 266 A1BIV2
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Purification (Commentary)

Purification (Comment) Organism
recombinant MBP-tagged enzyme from Escherichia coli strain XJa by amylose affinity chromatography Chlorobium phaeobacteroides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information analysis of acceptor and donor substrate specificity, product analysis by gel filtration, overview. No substantial incorporation of radiolabeled [3H]GlcA into polymer is observed if UDP-GalNAc is omitted, although very low incorporation is detected when UDP-GlcNAc, the C4 epimer used as an HA polymer donor, is substituted for UDP-GalNAc. The recombinant enzyme shows negligible activity with UDP-Glc and UDP-Gal, and no activity with UDP-GlcA and UDP-GalA. The enzyme shows no de novo initiation of chondroitin sulfate synthesis. It is active with the cognate chondroitin tetrasaccharide acceptor. The Chlorobium CpCS enzyme readily extends hyaluronan or heparosan with longer chondroitin chains Chlorobium phaeobacteroides ?
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additional information analysis of acceptor and donor substrate specificity, product analysis by gel filtration, overview. No substantial incorporation of radiolabeled [3H]GlcA into polymer is observed if UDP-GalNAc is omitted, although very low incorporation is detected when UDP-GlcNAc, the C4 epimer used as an HA polymer donor, is substituted for UDP-GalNAc. The recombinant enzyme shows negligible activity with UDP-Glc and UDP-Gal, and no activity with UDP-GlcA and UDP-GalA. The enzyme shows no de novo initiation of chondroitin sulfate synthesis. It is active with the cognate chondroitin tetrasaccharide acceptor. The Chlorobium CpCS enzyme readily extends hyaluronan or heparosan with longer chondroitin chains Chlorobium phaeobacteroides DSM 266 ?
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Synonyms

Synonyms Comment Organism
chondroitin synthase
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 Chlorobium phaeobacteroides
CpCS
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 Chlorobium phaeobacteroides
Cpha266_2341
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 Chlorobium phaeobacteroides
More see also EC 2.4.1.226 Chlorobium phaeobacteroides

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Chlorobium phaeobacteroides

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Chlorobium phaeobacteroides

General Information

General Information Comment Organism
evolution the enzyme belongs to the GH family 2. The sequence from the photosynthetic green sulfur bacteria, Chlorobium phaeobacteroides DSM 266, which is very similar (about 62% identical) to the open reading frames of known bifunctional chondroitin synthases (Pasteurella multocida PmCS and Escherichia coli KfoC) some segments are strikingly conserved amongst the three proteins. Recombinant Escherichia coli-derived Chlorobium enzyme preparations are found to possess bona fide chondroitin synthase activity in vitro. This catalyst, CpCS, has a more promiscuous acceptor usage than the prototypical PmCS, which may be of utility in novel chimeric GAG syntheses. The finding of such a similar chondroitin synthase enzyme in Chlorobium phaeobacteroides is unexpected for several reasons including (a) a free-living nonpathogenic organism should not require an animal self molecule for protection, (b) the Proteobacteria and the green sulfur bacterial lineages diverged 2.5-3 billion years ago and (c) the ecological niches of these bacteria are not thought to overlap substantially to facilitate horizontal gene transfer. But this Chlorobium has somehow acquired the gene via horizontal gene transfer as the probability of such close functional evolutionary convergence seems a less likely alternative Chlorobium phaeobacteroides
additional information structure-function relationship, and structure comparisons with the bifunctional chondroitin synthases from Pasteurella multocida (PmCS) and Escherichia coli (KfoC), overview Chlorobium phaeobacteroides