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Literature summary for 2.4.3.6 extracted from

  • Takakura, Y.; Tsukamoto, H.; Yamamoto, T.
    Molecular cloning, expression and properties of an alpha/beta-galactoside alpha2,3-sialyltransferase from Vibrio sp. JT-FAJ-16 (2007), J. Biochem., 142, 403-412 .
    View publication on PubMed
Search for more literature for 2.4.3.6

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli, N-terminally truncated form Vibrio sp. JT-FAJ-16

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl in presence of 500-700 mM NaCl 2fold increase in activity Vibrio sp. JT-FAJ-16

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43921
-
 MALDI-TOF of truncated enzyme with N-terminal Lys2 to Cys22 deletion Vibrio sp. JT-FAJ-16

Organism

Organism UniProt Comment Textmining
Vibrio sp. JT-FAJ-16 A8R0Y0
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant truncated enzyme Vibrio sp. JT-FAJ-16

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-Glc
-
 Vibrio sp. JT-FAJ-16 CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-Glc
-
 ?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc 127% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme Vibrio sp. JT-FAJ-16 CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
-
 ?
CMP-N-acetyl-beta-neuraminate + beta-D-N-acetylgalactosamine 58% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme Vibrio sp. JT-FAJ-16 CMP + alpha-Neu5Ac-(2->3)-beta-D-GalNAc
-
 ?
CMP-N-acetyl-beta-neuraminate + beta-D-N-acetylglucosamine 55% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme Vibrio sp. JT-FAJ-16 CMP + alpha-Neu5Ac-(2->3)-beta-D-GlcNAc
-
 ?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-Gal-(1->3)-beta-D-GlcNAc 124% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme Vibrio sp. JT-FAJ-16 CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
-
 ?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-galactopyranoside 114% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme Vibrio sp. JT-FAJ-16 CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-galactopyranoside
-
 ?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-glucopyranoside 52% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme Vibrio sp. JT-FAJ-16 CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-glucopyranoside
-
 ?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-mannopyranoside 57% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme Vibrio sp. JT-FAJ-16 CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Man
-
 ?

Subunits

Subunits Comment Organism
? x * 43921, MALDI-TOF of truncated enzyme with N-terminal Lys2 to Cys22 deletion Vibrio sp. JT-FAJ-16

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
-
 Vibrio sp. JT-FAJ-16

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
10 30 10°C: 65% of maximal activity, 30°C: 80% of maximal activity Vibrio sp. JT-FAJ-16

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
-
 Vibrio sp. JT-FAJ-16

pH Range

pH Minimum pH Maximum Comment Organism
5 9 pH 5: about 40% of maximal activity, pH 9: about 60% of maximal actzivity Vibrio sp. JT-FAJ-16