Abstract
Trans-sialidases catalyze the transfer of a sialic acid from one sialoside to an acceptor to form a new sialoside. α2,3-Trans-sialidase activity was initially discovered in the parasitic protozoan Trypanosoma cruzi, and more recently was found in a multifunctional Pasteurella multocida sialyltransferase PmST1. α2,8-Trans-sialidase activity was also described for a multifunctional Campylobacter jejuni sialyltransferase CstII. We report here the discovery of the α2,6-trans-sialidase activity of a previously reported recombinant truncated bacterial α2,6-sialyltransferase from Photobacterium damsela (Δ15Pd2,6ST). This is the first time that the α2,6-trans-sialidase activity has ever been identified. Kinetic studies indicate that Δ15Pd2,6ST-catalyzed trans-sialidase reaction follows a ping-pong bi-bi reaction mechanism. Cytidine 5′-monophosphate, the product of sialyltransferase reactions, is not required by the trans-sialidase activity of the enzyme but enhances the trans-sialidase activity modestly as a non-essential activator. Using chemically synthesized Neu5AcαpNP and LacβMU, α2,6-linked sialoside Neu5Acα2,6LacβMU has been obtained in one-step in high yield using the trans-sialidase activity of Δ15Pd2,6ST. In addition to the α2,6-trans-sialidase activity, Δ15Pd2,6ST also has α2,6-sialidase activity. The multifunctionality is thus a common feature of many bacterial sialyltransferases.
| Original language | English (US) |
|---|---|
| Article number | cwp172 |
| Pages (from-to) | 260-268 |
| Number of pages | 9 |
| Journal | Glycobiology |
| Volume | 20 |
| Issue number | 2 |
| DOIs | |
| State | Published - Oct 30 2009 |
Fingerprint
Keywords
- Enzyme
- Sialidase
- Sialoside
- Sialyltransferase
- Trans-sialidase
ASJC Scopus subject areas
- Biochemistry
Cite this
Trans-sialidase activity of Photobacterium damsela α2,6-sialyltransferase and its application in the synthesis of sialosides. / Cheng, Jiansong; Huang, Shengshu; Yu, Hai; Li, Yanhong; Lau, Kam; Chen, Xi.
In: Glycobiology, Vol. 20, No. 2, cwp172, 30.10.2009, p. 260-268.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Trans-sialidase activity of Photobacterium damsela α2,6-sialyltransferase and its application in the synthesis of sialosides
AU - Cheng, Jiansong
AU - Huang, Shengshu
AU - Yu, Hai
AU - Li, Yanhong
AU - Lau, Kam
AU - Chen, Xi
PY - 2009/10/30
Y1 - 2009/10/30
N2 - Trans-sialidases catalyze the transfer of a sialic acid from one sialoside to an acceptor to form a new sialoside. α2,3-Trans-sialidase activity was initially discovered in the parasitic protozoan Trypanosoma cruzi, and more recently was found in a multifunctional Pasteurella multocida sialyltransferase PmST1. α2,8-Trans-sialidase activity was also described for a multifunctional Campylobacter jejuni sialyltransferase CstII. We report here the discovery of the α2,6-trans-sialidase activity of a previously reported recombinant truncated bacterial α2,6-sialyltransferase from Photobacterium damsela (Δ15Pd2,6ST). This is the first time that the α2,6-trans-sialidase activity has ever been identified. Kinetic studies indicate that Δ15Pd2,6ST-catalyzed trans-sialidase reaction follows a ping-pong bi-bi reaction mechanism. Cytidine 5′-monophosphate, the product of sialyltransferase reactions, is not required by the trans-sialidase activity of the enzyme but enhances the trans-sialidase activity modestly as a non-essential activator. Using chemically synthesized Neu5AcαpNP and LacβMU, α2,6-linked sialoside Neu5Acα2,6LacβMU has been obtained in one-step in high yield using the trans-sialidase activity of Δ15Pd2,6ST. In addition to the α2,6-trans-sialidase activity, Δ15Pd2,6ST also has α2,6-sialidase activity. The multifunctionality is thus a common feature of many bacterial sialyltransferases.
AB - Trans-sialidases catalyze the transfer of a sialic acid from one sialoside to an acceptor to form a new sialoside. α2,3-Trans-sialidase activity was initially discovered in the parasitic protozoan Trypanosoma cruzi, and more recently was found in a multifunctional Pasteurella multocida sialyltransferase PmST1. α2,8-Trans-sialidase activity was also described for a multifunctional Campylobacter jejuni sialyltransferase CstII. We report here the discovery of the α2,6-trans-sialidase activity of a previously reported recombinant truncated bacterial α2,6-sialyltransferase from Photobacterium damsela (Δ15Pd2,6ST). This is the first time that the α2,6-trans-sialidase activity has ever been identified. Kinetic studies indicate that Δ15Pd2,6ST-catalyzed trans-sialidase reaction follows a ping-pong bi-bi reaction mechanism. Cytidine 5′-monophosphate, the product of sialyltransferase reactions, is not required by the trans-sialidase activity of the enzyme but enhances the trans-sialidase activity modestly as a non-essential activator. Using chemically synthesized Neu5AcαpNP and LacβMU, α2,6-linked sialoside Neu5Acα2,6LacβMU has been obtained in one-step in high yield using the trans-sialidase activity of Δ15Pd2,6ST. In addition to the α2,6-trans-sialidase activity, Δ15Pd2,6ST also has α2,6-sialidase activity. The multifunctionality is thus a common feature of many bacterial sialyltransferases.
KW - Enzyme
KW - Sialidase
KW - Sialoside
KW - Sialyltransferase
KW - Trans-sialidase
UR - http://www.scopus.com/inward/record.url?scp=77649221424&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77649221424&partnerID=8YFLogxK
U2 - 10.1093/glycob/cwp172
DO - 10.1093/glycob/cwp172
M3 - Article
C2 - 19880425
AN - SCOPUS:77649221424
VL - 20
SP - 260
EP - 268
JO - Glycobiology
JF - Glycobiology
SN - 0959-6658
IS - 2
M1 - cwp172
ER -