Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme
H Cho JE Cronan Jr 1993 Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme J. Biol. Chem. 268 9238 9245
Characterization of cpsF and its product CMP-N-acetylneuraminic acid synthetase, a group B streptococcal enzyme that can function in K1 capsular polysaccharide biosynthesis in Escherichia coli
RF Haft MR Wessels MF Mebane N Conaty CE Rubens 1996 Characterization of cpsF and its product CMP-N-acetylneuraminic acid synthetase, a group B streptococcal enzyme that can function in K1 capsular polysaccharide biosynthesis in Escherichia coli Mol. Microbiol. 19 555 563
The thioesterase I of Escherichia coli has arylesterase activity and shows stereospecificity for protease substrates
YL Lee JC Chen JF Shaw 1997 The thioesterase I of Escherichia coli has arylesterase activity and shows stereospecificity for protease substrates Biochem. Biophys. Res. Commun. 231 452 456
Discovery and characterization of sialic acid O-acetylation in group B Streptococcus
AL Lewis V Nizet A Varki 2004 Discovery and characterization of sialic acid O-acetylation in group B Streptococcus Proc. Natl. Acad. Sci. USA 101 11123 11128
CMP-N-acetylneuraminic acid synthetase from Escherichia coli K1 is a bifunctional enzyme: Identification of minimal catalytic domain for synthetase activity and novel functional domain for platelet-activating factor acetylhydrolase activity
G Liu C Jin C Jin 2004 CMP-N-acetylneuraminic acid synthetase from Escherichia coli K1 is a bifunctional enzyme: identification of minimal catalytic domain for synthetase activity and novel functional domain for platelet-activating factor acetylhydrolase activity J. Biol. Chem. 279 17738 17749
Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases
A Molgaard S Kauppinen S Larsen 2000 Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases Structure Fold. Des. 8 373 383
Chemoenzymatic synthesis of CMP-sialic acid derivatives by a one-pot two-enzyme system: Comparison of substrate flexibility of three microbial CMP-sialic acid synthetases
H Yu H Yu R Karpel X Chen 2004 Chemoenzymatic synthesis of CMP-sialic acid derivatives by a one-pot two-enzyme system: comparison of substrate flexibility of three microbial CMP-sialic acid synthetases Bioorg. Med. Chem. 12 6427 6435