Triose phosphate isomerase from the blood fluke Schistosoma mansoni: Biochemical characterisation of a potential drug and vaccine target

Veronika L. Zinsser; Edward Farnell; David W. Dunne; David J. Timson

doi:10.1016/j.febslet.2013.09.022

Triose phosphate isomerase from the blood fluke Schistosoma mansoni: Biochemical characterisation of a potential drug and vaccine target

Veronika L. Zinsser, Edward Farnell, David W. Dunne, David J. Timson

Research output: Contribution to journal › Article › peer-review

Abstract

The glycolytic enzyme triose phosphate isomerase from Schistosoma mansoni is a potential target for drugs and vaccines. Molecular modelling of the enzyme predicted that a Ser-Ala-Asp motif which is believed to be a helminth-specific epitope is exposed. The enzyme is dimeric (as judged by gel filtration and cross-linking), resistant to proteolysis and highly stable to thermal denaturation (melting temperature of 82.0 C). The steady-state kinetic parameters are high (K_m for dihydroxyacetone phosphate is 0.51 mM; K_m for glyceraldehyde 3-phosphate is 1.1 mM; k_cat for dihydroxyacetone phosphate is 7800 s^-1 and k_cat for glyceraldehyde 3-phosphate is 6.9 s^-1).

Original language	English
Pages (from-to)	3422-3427
Number of pages	6
Journal	Febs Letters
Volume	587
Issue number	21
DOIs	https://doi.org/10.1016/j.febslet.2013.09.022
Publication status	Published - 1 Nov 2013

Keywords

Bilharzia
Blood fluke
Glycolytic enzyme
Schistosomiasis
Vaccine target

Access to Document

10.1016/j.febslet.2013.09.022

Cite this

@article{51e8d715677a4b029ad58dd7c6e04998,

title = "Triose phosphate isomerase from the blood fluke Schistosoma mansoni: Biochemical characterisation of a potential drug and vaccine target",

abstract = "The glycolytic enzyme triose phosphate isomerase from Schistosoma mansoni is a potential target for drugs and vaccines. Molecular modelling of the enzyme predicted that a Ser-Ala-Asp motif which is believed to be a helminth-specific epitope is exposed. The enzyme is dimeric (as judged by gel filtration and cross-linking), resistant to proteolysis and highly stable to thermal denaturation (melting temperature of 82.0 C). The steady-state kinetic parameters are high (Km for dihydroxyacetone phosphate is 0.51 mM; Km for glyceraldehyde 3-phosphate is 1.1 mM; kcat for dihydroxyacetone phosphate is 7800 s-1 and kcat for glyceraldehyde 3-phosphate is 6.9 s-1).",

keywords = "Bilharzia, Blood fluke, Glycolytic enzyme, Schistosomiasis, Vaccine target",

author = "Zinsser, {Veronika L.} and Edward Farnell and Dunne, {David W.} and Timson, {David J.}",

year = "2013",

month = nov,

day = "1",

doi = "10.1016/j.febslet.2013.09.022",

language = "English",

volume = "587",

pages = "3422--3427",

journal = "Febs Letters",

issn = "0014-5793",

number = "21",

}

TY - JOUR

T1 - Triose phosphate isomerase from the blood fluke Schistosoma mansoni

T2 - Biochemical characterisation of a potential drug and vaccine target

AU - Zinsser, Veronika L.

AU - Farnell, Edward

AU - Dunne, David W.

AU - Timson, David J.

PY - 2013/11/1

Y1 - 2013/11/1

N2 - The glycolytic enzyme triose phosphate isomerase from Schistosoma mansoni is a potential target for drugs and vaccines. Molecular modelling of the enzyme predicted that a Ser-Ala-Asp motif which is believed to be a helminth-specific epitope is exposed. The enzyme is dimeric (as judged by gel filtration and cross-linking), resistant to proteolysis and highly stable to thermal denaturation (melting temperature of 82.0 C). The steady-state kinetic parameters are high (Km for dihydroxyacetone phosphate is 0.51 mM; Km for glyceraldehyde 3-phosphate is 1.1 mM; kcat for dihydroxyacetone phosphate is 7800 s-1 and kcat for glyceraldehyde 3-phosphate is 6.9 s-1).

AB - The glycolytic enzyme triose phosphate isomerase from Schistosoma mansoni is a potential target for drugs and vaccines. Molecular modelling of the enzyme predicted that a Ser-Ala-Asp motif which is believed to be a helminth-specific epitope is exposed. The enzyme is dimeric (as judged by gel filtration and cross-linking), resistant to proteolysis and highly stable to thermal denaturation (melting temperature of 82.0 C). The steady-state kinetic parameters are high (Km for dihydroxyacetone phosphate is 0.51 mM; Km for glyceraldehyde 3-phosphate is 1.1 mM; kcat for dihydroxyacetone phosphate is 7800 s-1 and kcat for glyceraldehyde 3-phosphate is 6.9 s-1).

KW - Bilharzia

KW - Blood fluke

KW - Glycolytic enzyme

KW - Schistosomiasis

KW - Vaccine target

UR - http://www.scopus.com/inward/record.url?scp=84886242037&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2013.09.022

DO - 10.1016/j.febslet.2013.09.022

M3 - Article

C2 - 24070897

AN - SCOPUS:84886242037

SN - 0014-5793

VL - 587

SP - 3422

EP - 3427

JO - Febs Letters

JF - Febs Letters

IS - 21

ER -

Triose phosphate isomerase from the blood fluke Schistosoma mansoni: Biochemical characterisation of a potential drug and vaccine target

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this