PURIFICATION AND CHARACTERIZATION OF THE RECOMBINANT CMP-SIALIC ACID SYNTHETASE FROM NEISSERIA-MENINGITIDIS

Authors
GILBERT M WATSON DC WAKARCHUK WW
Citation
M. Gilbert et al., PURIFICATION AND CHARACTERIZATION OF THE RECOMBINANT CMP-SIALIC ACID SYNTHETASE FROM NEISSERIA-MENINGITIDIS, Biotechnology letters, 19(5), 1997, pp. 417-420
Citations number
11
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
Biotechnology letters → ACNP
ISSN journal
01415492
Volume
19
Issue
5
Year of publication
1997
Pages
417 - 420
Database
ISI
SICI code
0141-5492(1997)19:5<417:PACOTR>2.0.ZU;2-2
Abstract
CMP-Sialic acid synthetase from Neisseria meningitidis 406Y was expres sed in Escherichia coli K113 pLysS and produced at 360 U/L. The purifi ed CMP-sialic acid synthetase used both N-acetyl-neuraminic acid (K-m = 0.34 mM) and N-glycolyl-neuraminic acid (K-m = 2.6 mM) as substrates . The recombinant synthetase could be used in a coupled reaction with an alpha-2,3-sialyltransferase to sialylate a lactose derivative in a one-reactor synthesis.