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Literature summary for 2.4.1.212 extracted from

  • Weigel, P.H.; Baggenstoss, B.A.
    Hyaluronan synthase polymerizing activity and control of product size are discrete enzyme functions that can be uncoupled by mutagenesis of conserved cysteines (2012), Glycobiology, 22, 1302-1310.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.212

Protein Variants

Protein Variants Comment Organism
C226A site-directed mutagenesis, the mutant shows 44% of wild-type activity Streptococcus dysgalactiae subsp. equisimilis
C226A/C262A site-directed mutagenesis, the mutant shows 36% of wild-type activity, mutant kinetics compared to the wild-type enzyme Streptococcus dysgalactiae subsp. equisimilis
C226A/C281A site-directed mutagenesis, the mutant shows 68% of wild-type activity Streptococcus dysgalactiae subsp. equisimilis
C226A/C367A site-directed mutagenesis, the mutant shows 102% of wild-type activity Streptococcus dysgalactiae subsp. equisimilis
C226S site-directed mutagenesis, the mutant shows 45% of wild-type activity, mutant kinetics compared to the wild-type enzyme Streptococcus dysgalactiae subsp. equisimilis
C262A site-directed mutagenesis, the mutant shows 79% of wild-type activity Streptococcus dysgalactiae subsp. equisimilis
C262A/C281A site-directed mutagenesis, the mutant shows 82% of wild-type activity, mutant kinetics compared to the wild-type enzyme Streptococcus dysgalactiae subsp. equisimilis
C262S site-directed mutagenesis, the mutant shows 85% of wild-type activity Streptococcus dysgalactiae subsp. equisimilis
C281A site-directed mutagenesis, the mutant shows 91% of wild-type activity Streptococcus dysgalactiae subsp. equisimilis
C281A/C367A site-directed mutagenesis, the mutant shows 107% of wild-type activity Streptococcus dysgalactiae subsp. equisimilis
C281S site-directed mutagenesis, the mutant shows 57% of wild-type activity Streptococcus dysgalactiae subsp. equisimilis
C367A site-directed mutagenesis, the mutant shows 126% of wild-type activity Streptococcus dysgalactiae subsp. equisimilis
C367S site-directed mutagenesis, the mutant shows 80% of wild-type activity Streptococcus dysgalactiae subsp. equisimilis
additional information generation of several deletion mutants, DELTA3-C281, DELTA3-C226, DELTA3-C262, and DELTA3-C367, and of a C-null mutant, all show reduced activity and altered kinetics compared to the wild-type enzyme Streptococcus dysgalactiae subsp. equisimilis

Inhibitors

Inhibitors Comment Organism Structure
additional information HA product size is decreased by increasing concentrations of glycerol Streptococcus dysgalactiae subsp. equisimilis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Streptococcus dysgalactiae subsp. equisimilis

Organism

Organism UniProt Comment Textmining
Streptococcus dysgalactiae subsp. equisimilis
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
13.4
-
 mutant C226A/C262A, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
14
-
 deletion mutant DELTA3-C281, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
16.4
-
 mutant C226A, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
16.5
-
 mutant C226S, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
21.2
-
 mutant C281S, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
22.9
-
 deletion mutant C-Null, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
25.3
-
 mutant C226A/C281A, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
27
-
 deletion mutant DELTA3-C367, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
29.1
-
 mutant C262A, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
29.5
-
 mutant C367S, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
30.2
-
 mutant C262A/C281A, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
31.4
-
 mutant C262S, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
31.6
-
 deletion mutant DELTA3-C262, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
33.7
-
 mutant C281A, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
37
-
 wild-type enzyme, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
37.8
-
 mutant C226A/C367A, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
38.6
-
 deletion mutant DELTA3-C226, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
39.5
-
 mutant C281A/C367A, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis
46.7
-
 mutant C367A, pH 7.0, 30°C Streptococcus dysgalactiae subsp. equisimilis

Synonyms

Synonyms Comment Organism
HA synthase
-
 Streptococcus dysgalactiae subsp. equisimilis
HAS
-
 Streptococcus dysgalactiae subsp. equisimilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Streptococcus dysgalactiae subsp. equisimilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Streptococcus dysgalactiae subsp. equisimilis

General Information

General Information Comment Organism
additional information HA product size is decreased by increasing concentrations of glycerol. The four Cys residues in SeHAS are clustered close together and are located at the membrane-HAS interface within the enzyme active site. Involvement of these Cys residues in HAS activity, overview Streptococcus dysgalactiae subsp. equisimilis