@article{4b972854c0284a75832609a1f0f1b6ab,
title = "Structural characterization of Escherichia coli sialic acid synthase",
abstract = "Sialic acid synthase encoded by the neuB gene of Escherichia coli catalyzes the condensation of N-acetylmannosamine and phosphoenolpyruvate to form N-acetylneuraminic acid. This report demonstrates the first structural information on sialic acid synthase by CD MALDI-TOF and chemical cross-linking studies. Also a specific cleavage by endogenous protease(s) has been identified at Lys280 of the enzyme (40 kDa) by LC-MS and N-terminal sequencing analyses. The cleavage results in the formation of two inactive fragments of 33 and 7 kDa. The structural analysis indicates that the fragmentation is associated with a significant change of the enzyme from a tetrameric to trimeric form and alterations in both secondary and native quaternary structures.",
keywords = "Circular dichroism (CD), Matrix-assisted laser desorption (MALDI)/ionization-time-of-flight (TOF), N-Acetylneuraminic acid (NeuAc), Sialic acid synthase, Subunit cross-linking",
author = "Hwang, {Tzann Shun} and Hung, {Chih Hung} and Teo, {Chin Fen} and Chen, {Guan Ting} and Chang, {Lee Shang} and Chen, {Sung Fang} and Chen, {Yu Ju} and Lin, {Chun Hung}",
note = "Funding Information: The work was supported by National Science Council (NSC-90-2113-M-001-028), National Health Research Institute (NSC-90-2323-B-001-004), and Academia Sinica (Taipei, Taiwan). We are indebted to Prof. Shyh-Horng Chiou at the same institute for his critical reading of the manuscript and suggestions of CD and cross-linking experiments. We also thank Mr. Chuan-Fa Chang for graphic assistance.",
year = "2002",
doi = "10.1016/S0006-291X(02)00620-4",
language = "English",
volume = "295",
pages = "167--173",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier BV",
number = "1",
}