Structural characterization of Escherichia coli sialic acid synthase

Tzann Shun Hwang, Chih Hung Hung, Chin Fen Teo, Guan Ting Chen, Lee Shang Chang, Sung Fang Chen, Yu Ju Chen, Chun Hung Lin

Research output: Contribution to journalArticle

13 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)167-173
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume295
Issue number1
DOIs
Publication statusPublished - 2002 Jan 1

Fingerprint

Escherichia coli
Phosphoenolpyruvate
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
N-Acetylneuraminic Acid
Enzymes
Structural analysis
Condensation
Peptide Hydrolases
Genes
N-acetylneuraminate synthase
N-acetylmannosamine

Keywords

  • Circular dichroism (CD)
  • Matrix-assisted laser desorption (MALDI)/ionization-time-of-flight (TOF)
  • N-Acetylneuraminic acid (NeuAc)
  • Sialic acid synthase
  • Subunit cross-linking

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Structural characterization of Escherichia coli sialic acid synthase. / Hwang, Tzann Shun; Hung, Chih Hung; Teo, Chin Fen; Chen, Guan Ting; Chang, Lee Shang; Chen, Sung Fang; Chen, Yu Ju; Lin, Chun Hung.

In: Biochemical and Biophysical Research Communications, Vol. 295, No. 1, 01.01.2002, p. 167-173.

Research output: Contribution to journalArticle

Hwang, Tzann Shun ; Hung, Chih Hung ; Teo, Chin Fen ; Chen, Guan Ting ; Chang, Lee Shang ; Chen, Sung Fang ; Chen, Yu Ju ; Lin, Chun Hung. / Structural characterization of Escherichia coli sialic acid synthase. In: Biochemical and Biophysical Research Communications. 2002 ; Vol. 295, No. 1. pp. 167-173.
@article{0e41172caa1c42908f24c15d60a771bf,
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}",
year = "2002",
month = "1",
day = "1",
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 = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Structural characterization of Escherichia coli sialic acid synthase

AU - Hwang, Tzann Shun

AU - Hung, Chih Hung

AU - Teo, Chin Fen

AU - Chen, Guan Ting

AU - Chang, Lee Shang

AU - Chen, Sung Fang

AU - Chen, Yu Ju

AU - Lin, Chun Hung

PY - 2002/1/1

Y1 - 2002/1/1

N2 - 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.

AB - 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.

KW - Circular dichroism (CD)

KW - Matrix-assisted laser desorption (MALDI)/ionization-time-of-flight (TOF)

KW - N-Acetylneuraminic acid (NeuAc)

KW - Sialic acid synthase

KW - Subunit cross-linking

UR - http://www.scopus.com/inward/record.url?scp=0036305572&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036305572&partnerID=8YFLogxK

U2 - 10.1016/S0006-291X(02)00620-4

DO - 10.1016/S0006-291X(02)00620-4

M3 - Article

C2 - 12083785

AN - SCOPUS:0036305572

VL - 295

SP - 167

EP - 173

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -