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Literature summary for 2.4.3.1 extracted from

  • Okino, N.; Kakuta, Y.; Kajiwara, H.; Ichikawa, M.; Takakura, Y.; Ito, M.; Yamamoto, T.
    Purification, crystallization and preliminary crystallographic characterization of the alpha 2,6-sialyltransferase from Photobacterium sp. JT-ISH-224 (2007), Acta Crystallogr. Sect. F, F63, 662-664.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
the putative mature form of JT-ISH-224 alpha2,6-sialyltransferase is overproduced in Escherichia coli Photobacterium sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapour-diffusion method at 20°C. The crystal belongs to space group P3(1)2(1) or P3(2)2(1), with unit-cell parameters a = b = 90.29, c = 204.33 A. X-ray diffraction data are collected to 2.5 A resolution Photobacterium sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
 x * 55000, SDS-PAGE Photobacterium sp.
59000
-
 gel filtration Photobacterium sp.

Organism

Organism UniProt Comment Textmining
Photobacterium sp.
-
 JT-ISH-224
-

Purification (Commentary)

Purification (Comment) Organism
-
 Photobacterium sp.

Subunits

Subunits Comment Organism
? x * 55000, SDS-PAGE Photobacterium sp.

Synonyms

Synonyms Comment Organism
alpha 2,6-sialyltransferase
-
 Photobacterium sp.
alpha2,6-STase
-
 Photobacterium sp.