EC Number | Cloned (Comment) | Organism |
---|---|---|
2.4.3.1 | 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 |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.4.3.1 | 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 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.4.3.1 | 0.6 | - |
4-methylumbelliferyl beta-D-lactoside | pH 8.5, 37°C, enzyme form DELTA112Pd2,6ST(N) | Photobacterium damselae | |
2.4.3.1 | 0.8 | - |
4-methylumbelliferyl beta-D-lactoside | pH 8.5, 37°C, enzyme form DELTA15Pd2,6ST(N) | Photobacterium damselae | |
2.4.3.1 | 0.9 | - |
CMP-N-acetylneuraminate | pH 8.5, 37°C, enzyme form DELTA112Pd2,6ST(N) | Photobacterium damselae | |
2.4.3.1 | 0.9 | - |
CMP-N-acetylneuraminate | pH 8.5, 37°C, enzyme form DELTA15Pd2,6ST(N) | Photobacterium damselae |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.4.3.1 | additional information | a metal ion is not required for the activity | Photobacterium damselae |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.3.1 | Photobacterium damselae | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.4.3.1 | truncated enzyme forms | Photobacterium damselae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.3.1 | CMP-N-acetylneuraminate + 4-methylumbelliferyl beta-D-lactoside | - |
Photobacterium damselae | ? | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.4.3.1 | 1.1 | - |
4-methylumbelliferyl beta-D-lactoside | pH 8.5, 37°C, enzyme form DELTA112Pd2,6ST(N) | Photobacterium damselae | |
2.4.3.1 | 1.4 | - |
CMP-N-acetylneuraminate | pH 8.5, 37°C, enzyme form DELTA112Pd2,6ST(N) | Photobacterium damselae | |
2.4.3.1 | 2.3 | - |
4-methylumbelliferyl beta-D-lactoside | pH 8.5, 37°C, enzyme form DELTA15Pd2,6ST(N) | Photobacterium damselae | |
2.4.3.1 | 2.7 | - |
CMP-N-acetylneuraminate | pH 8.5, 37°C, enzyme form DELTA15Pd2,6ST(N) | Photobacterium damselae |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
2.4.3.1 | 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 |