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Literature summary for 2.4.3.1 extracted from

  • Mine, T.; Katayama, S.; Kajiwara, H.; Tsunashima, M.; Tsukamoto, H.; Takakura, Y.; Yamamoto, T.
    An alpha2,6-sialyltransferase cloned from Photobacterium leiognathi strain JT-SHIZ-119 shows both sialyltransferase and neuraminidase activity (2010), Glycobiology, 20, 158-165.
    View publication on PubMed
Search for more literature for 2.4.3.1

Application

Application Comment Organism
synthesis the enzyme may be a powerful tool for the synthesis of sialosides and the modification of sialyl-glycoconjugates Photobacterium leiognathi

Cloned(Commentary)

Cloned (Comment) Organism
expression cassettes of the full-length form in pLST-FL and of the truncated form (N-terminal Lys2 to Ala15 deletion) in pLST-DELTAN expressed in Escherichia coli Photobacterium leiognathi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.3
-
 CMP-Neu5Ac alpha2,6-sialyltransferase activity of the truncated recombinant enzyme Photobacterium leiognathi
15.4
-
 N-acetyllactosamine alpha2,6-sialyltransferase activity of the truncated recombinant enzyme Photobacterium leiognathi
17.2
-
 lactose alpha2,6-sialyltransferase activity of the truncated recombinant enzyme Photobacterium leiognathi

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl alpha2,6-sialyltransferase activity is increased approximately 40% in the presence of 300-800 mM Photobacterium leiognathi

Organism

Organism UniProt Comment Textmining
Photobacterium leiognathi
-
-
-
Photobacterium leiognathi JT-SHIZ-119
-
-
-

Purification (Commentary)

Purification (Comment) Organism
N-terminal truncated form, by gel filtration, 15.2fold, with a yield of 53.2% Photobacterium leiognathi

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.103
-
 neuraminidase activity of the truncated recombinant enzyme Photobacterium leiognathi
5.5
-
 crude extract, alpha2,6-sialyltransferase activity of the truncated recombinant enzyme Photobacterium leiognathi
82.9
-
 alpha2,6-sialyltransferase activity of the 15.2fold purified truncated recombinant enzyme Photobacterium leiognathi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CMP-Neu5Ac + lactose alpha2,6-sialyltransferase activity Photobacterium leiognathi CMP + Neu5Acalpha(2-6)Lac
-
 ?
CMP-Neu5Ac + lactose alpha2,6-sialyltransferase activity Photobacterium leiognathi JT-SHIZ-119 CMP + Neu5Acalpha(2-6)Lac
-
 ?
CMP-Neu5Ac + methyl-beta-D-galactopyranoside alpha2,6-sialyltransferase activity Photobacterium leiognathi CMP + Neu5Acalpha(2-6)Gal-alpha-methyl
-
 ?
CMP-Neu5Ac + methyl-beta-D-galactopyranoside alpha2,6-sialyltransferase activity Photobacterium leiognathi JT-SHIZ-119 CMP + Neu5Acalpha(2-6)Gal-alpha-methyl
-
 ?
CMP-Neu5Ac + N-acetyllactosamine alpha2,6-sialyltransferase activity Photobacterium leiognathi CMP + Neu5Acalpha(2-6)LacNAc
-
 ?
CMP-Neu5Ac + N-acetyllactosamine alpha2,6-sialyltransferase activity Photobacterium leiognathi JT-SHIZ-119 CMP + Neu5Acalpha(2-6)LacNAc
-
 ?
additional information neuraminidase activity is specific for the Neu5Acalpha2,6Gal linkage Photobacterium leiognathi ?
-
 ?
additional information neuraminidase activity is specific for the Neu5Acalpha2,6Gal linkage Photobacterium leiognathi JT-SHIZ-119 ?
-
 ?

Synonyms

Synonyms Comment Organism
beta-galactoside alpha2,6-sialyltransferase
-
 Photobacterium leiognathi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
 alpha2,6-sialyltransferase activity and neuraminidase activity of the truncated recombinant enzyme Photobacterium leiognathi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 6 pH 5: alpha2,6-sialyltransferase activity of the truncated recombinant enzyme, pH 6: neuraminidase activity of the truncated recombinant enzyme Photobacterium leiognathi

General Information

General Information Comment Organism
physiological function shows both alpha2,6-sialyltransferase and alpha2,6-linkage-specific neuraminidase activity. Sialyltransferase activity of pLST-DELTAN is much higher than that of pLST-FL, and reaches 1477 U/l culture broth Photobacterium leiognathi