Studying a cell division amidase using defined peptidoglycan substrates

Tania Lupoli, Tohru Taniguchi, Tsung Shing Wang, Deborah L. Perlstein, Suzanne Walker, Daniel E. Kahne

Research output: Contribution to journalArticle

Abstract

(Figure Presented) Three periplasmic N-acetylmuramoyl-L-alanine amidases are critical for hydrolysis of septal peptidoglycan, which enables cell separation. The amidases cleave the amide bond between the lactyl group of muramic acid and the amino group of L-alanine to release a peptide moiety. Cell division amidases remain largely uncharacterized because substrates suitable for studying them have not been available. Here we have used synthetic peptidoglycan fragments of defined composition to characterize the catalytic activity and substrate specificity of the important Escherichia coli cell division amidase AmiA. We show that AmiA is a zinc metalloprotease that requires at least a tetrasaccharide glycopeptide substrate for cleavage. The approach outlined here can be applied to many other cell wall hydrolases and should enable more detailed studies of accessory proteins proposed to regulate amidase activity in cells.

Original languageEnglish (US)
Pages (from-to)18230-18231
Number of pages2
JournalJournal of the American Chemical Society
Volume131
Issue number51
DOIs
StatePublished - Dec 30 2009

Fingerprint

amidase
Amidohydrolases
Peptidoglycan
Cell Division
Muramic Acids
Cells
N-Acetylmuramoyl-L-alanine Amidase
Glycopeptides
Cell Separation
Metalloproteases
Hydrolases
Substrates
Substrate Specificity
Amides
Alanine
Cell Wall
Zinc
Hydrolysis
Accessories
Escherichia coli

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Lupoli, T., Taniguchi, T., Wang, T. S., Perlstein, D. L., Walker, S., & Kahne, D. E. (2009). Studying a cell division amidase using defined peptidoglycan substrates. Journal of the American Chemical Society, 131(51), 18230-18231. https://doi.org/10.1021/ja908916z

Studying a cell division amidase using defined peptidoglycan substrates. / Lupoli, Tania; Taniguchi, Tohru; Wang, Tsung Shing; Perlstein, Deborah L.; Walker, Suzanne; Kahne, Daniel E.

In: Journal of the American Chemical Society, Vol. 131, No. 51, 30.12.2009, p. 18230-18231.

Research output: Contribution to journalArticle

Lupoli, T, Taniguchi, T, Wang, TS, Perlstein, DL, Walker, S & Kahne, DE 2009, 'Studying a cell division amidase using defined peptidoglycan substrates', Journal of the American Chemical Society, vol. 131, no. 51, pp. 18230-18231. https://doi.org/10.1021/ja908916z
Lupoli, Tania ; Taniguchi, Tohru ; Wang, Tsung Shing ; Perlstein, Deborah L. ; Walker, Suzanne ; Kahne, Daniel E. / Studying a cell division amidase using defined peptidoglycan substrates. In: Journal of the American Chemical Society. 2009 ; Vol. 131, No. 51. pp. 18230-18231.
@article{9e48a48b450347b1a16df954fe15d2a1,
title = "Studying a cell division amidase using defined peptidoglycan substrates",
abstract = "(Figure Presented) Three periplasmic N-acetylmuramoyl-L-alanine amidases are critical for hydrolysis of septal peptidoglycan, which enables cell separation. The amidases cleave the amide bond between the lactyl group of muramic acid and the amino group of L-alanine to release a peptide moiety. Cell division amidases remain largely uncharacterized because substrates suitable for studying them have not been available. Here we have used synthetic peptidoglycan fragments of defined composition to characterize the catalytic activity and substrate specificity of the important Escherichia coli cell division amidase AmiA. We show that AmiA is a zinc metalloprotease that requires at least a tetrasaccharide glycopeptide substrate for cleavage. The approach outlined here can be applied to many other cell wall hydrolases and should enable more detailed studies of accessory proteins proposed to regulate amidase activity in cells.",
author = "Tania Lupoli and Tohru Taniguchi and Wang, {Tsung Shing} and Perlstein, {Deborah L.} and Suzanne Walker and Kahne, {Daniel E.}",
year = "2009",
month = "12",
day = "30",
doi = "10.1021/ja908916z",
language = "English (US)",
volume = "131",
pages = "18230--18231",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "51",

}

TY - JOUR

T1 - Studying a cell division amidase using defined peptidoglycan substrates

AU - Lupoli, Tania

AU - Taniguchi, Tohru

AU - Wang, Tsung Shing

AU - Perlstein, Deborah L.

AU - Walker, Suzanne

AU - Kahne, Daniel E.

PY - 2009/12/30

Y1 - 2009/12/30

N2 - (Figure Presented) Three periplasmic N-acetylmuramoyl-L-alanine amidases are critical for hydrolysis of septal peptidoglycan, which enables cell separation. The amidases cleave the amide bond between the lactyl group of muramic acid and the amino group of L-alanine to release a peptide moiety. Cell division amidases remain largely uncharacterized because substrates suitable for studying them have not been available. Here we have used synthetic peptidoglycan fragments of defined composition to characterize the catalytic activity and substrate specificity of the important Escherichia coli cell division amidase AmiA. We show that AmiA is a zinc metalloprotease that requires at least a tetrasaccharide glycopeptide substrate for cleavage. The approach outlined here can be applied to many other cell wall hydrolases and should enable more detailed studies of accessory proteins proposed to regulate amidase activity in cells.

AB - (Figure Presented) Three periplasmic N-acetylmuramoyl-L-alanine amidases are critical for hydrolysis of septal peptidoglycan, which enables cell separation. The amidases cleave the amide bond between the lactyl group of muramic acid and the amino group of L-alanine to release a peptide moiety. Cell division amidases remain largely uncharacterized because substrates suitable for studying them have not been available. Here we have used synthetic peptidoglycan fragments of defined composition to characterize the catalytic activity and substrate specificity of the important Escherichia coli cell division amidase AmiA. We show that AmiA is a zinc metalloprotease that requires at least a tetrasaccharide glycopeptide substrate for cleavage. The approach outlined here can be applied to many other cell wall hydrolases and should enable more detailed studies of accessory proteins proposed to regulate amidase activity in cells.

UR - http://www.scopus.com/inward/record.url?scp=73249119525&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=73249119525&partnerID=8YFLogxK

U2 - 10.1021/ja908916z

DO - 10.1021/ja908916z

M3 - Article

C2 - 19957935

AN - SCOPUS:73249119525

VL - 131

SP - 18230

EP - 18231

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 51

ER -