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Literature summary for 2.4.3.1 extracted from

  • Sun, M.; Li, Y.; Chokhawala, H.A.; Henning, R.; Chen, X.
    N-Terminal 112 amino acid residues are not required for the sialyltransferase activity of Photobacterium damsela alpha2,6-sialyltransferase (2008), Biotechnol. Lett., 30, 671-676.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
cloned as N- and C- His-tagged fusion proteins with different lengths (16-497 aa or 113-497 aa). Expression and activity assays indicate that the N-terminal 112 amino acid residues of the protein are not required for its alpha2,6-sialyltransferase activity but affect the solubility of the recombinant protein expressed in Escherichia coli Photobacterium damselae

Protein Variants

Protein Variants Comment Organism
additional information cloned as N- and C-His-tagged fusion proteins with different lengths (16-497 aa or 113-497 aa). Expression and activity assays indicate that the N-terminal 112 amino acid residues of the protein are not required for its alpha2,6-sialyltransferase activity. Among four truncated forms tested, N-His-tagged ELTA15Pd2,6ST(N) containing 16-497 amino acid residues has the highest expression level. Similar to the DELTA15Pd2,6ST(N), the shorter DELTA112Pd2,6ST(N) is active in a wide pH range of 7.5-10.0 Photobacterium damselae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.6
-
4-methylumbelliferyl beta-D-lactoside pH 8.5, 37°C, enzyme form DELTA112Pd2,6ST(N) Photobacterium damselae
0.8
-
4-methylumbelliferyl beta-D-lactoside pH 8.5, 37°C, enzyme form DELTA15Pd2,6ST(N) Photobacterium damselae
0.9
-
CMP-N-acetylneuraminate pH 8.5, 37°C, enzyme form DELTA112Pd2,6ST(N) Photobacterium damselae
0.9
-
CMP-N-acetylneuraminate pH 8.5, 37°C, enzyme form DELTA15Pd2,6ST(N) Photobacterium damselae

Metals/Ions

Metals/Ions Comment Organism Structure
additional information a metal ion is not required for the activity Photobacterium damselae

Organism

Organism UniProt Comment Textmining
Photobacterium damselae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
truncated enzyme forms Photobacterium damselae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CMP-N-acetylneuraminate + 4-methylumbelliferyl beta-D-lactoside
-
Photobacterium damselae ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1
-
4-methylumbelliferyl beta-D-lactoside pH 8.5, 37°C, enzyme form DELTA112Pd2,6ST(N) Photobacterium damselae
1.4
-
CMP-N-acetylneuraminate pH 8.5, 37°C, enzyme form DELTA112Pd2,6ST(N) Photobacterium damselae
2.3
-
4-methylumbelliferyl beta-D-lactoside pH 8.5, 37°C, enzyme form DELTA15Pd2,6ST(N) Photobacterium damselae
2.7
-
CMP-N-acetylneuraminate pH 8.5, 37°C, enzyme form DELTA15Pd2,6ST(N) Photobacterium damselae

pH Range

pH Minimum pH Maximum Comment Organism
7.5 10 pH-profile of truncated enzyme forms DELTA15Pd2,6ST(N) and DELTA112Pd2,6ST(N). Similar to the DELTA15Pd2,6ST(N), the shorter DELTA112Pd2,6ST(N) is active in a wide pH range of 7.5-10.0 Photobacterium damselae