A new T677C mutation of the aspartoacylase gene encodes for a protein with no enzymatic activity

Barbara Tavazzi; Valentina Di Pietro; Angela Maria Amorini; Bruno Giardina; Giuseppe Lazzarino

A new T677C mutation of the aspartoacylase gene encodes for a protein with no enzymatic activity

Barbara Tavazzi, Valentina Di Pietro, Angela Maria Amorini, Bruno Giardina, Giuseppe Lazzarino

Università Cattolica del Sacro Cuore

Risultato della ricerca: Contributo in rivista › Articolo in rivista › peer review

5 Citazioni (Scopus)

Abstract

OBJECTIVE: To verify the effect of and to date the unknown T677C mutation of the human N-acetylaspartoacylase (hASPA) gene on the function of the mutated enzyme. DESIGN AND METHODS: Wild type and I226T-mutated proteins were expressed and purified from a transformed Escherichia coli colony. Enzymatic activities were measured in the presence of varying substrate concentrations. RESULTS: Whilst kinetic parameters of wild type hASPA were in line with data in literature, I226T-mutated hASPA showed no enzymatic activity. CONCLUSION: Data indicated that this new mutation might be responsible in homozygosis for the phenotype corresponding to Canavan disease.

Lingua originale	English
pagine (da-a)	611-615
Numero di pagine	5
Rivista	Clinical Biochemistry
Stato di pubblicazione	Pubblicato - 2008

Keywords

Aspartoacylase
Canavan desease
NAA

OSS delle Nazioni Unite

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title = "A new T677C mutation of the aspartoacylase gene encodes for a protein with no enzymatic activity",

abstract = "OBJECTIVE: To verify the effect of and to date the unknown T677C mutation of the human N-acetylaspartoacylase (hASPA) gene on the function of the mutated enzyme. DESIGN AND METHODS: Wild type and I226T-mutated proteins were expressed and purified from a transformed Escherichia coli colony. Enzymatic activities were measured in the presence of varying substrate concentrations. RESULTS: Whilst kinetic parameters of wild type hASPA were in line with data in literature, I226T-mutated hASPA showed no enzymatic activity. CONCLUSION: Data indicated that this new mutation might be responsible in homozygosis for the phenotype corresponding to Canavan disease.",

keywords = "Aspartoacylase, Canavan desease, NAA, Aspartoacylase, Canavan desease, NAA",

author = "Barbara Tavazzi and {Di Pietro}, Valentina and Amorini, {Angela Maria} and Bruno Giardina and Giuseppe Lazzarino",

year = "2008",

language = "English",

pages = "611--615",

journal = "Clinical Biochemistry",

issn = "0009-9120",

publisher = "Elsevier Science Limited: Oxford Fulfillment Center, PO Box 800, Kidlington Oxford OX5 1DX United Kingdom:011 44 1865 843000, 011 44 1865 843699, EMAIL: [email protected], [email protected], INTERNET: http://www.elsevier.com, http://www.elsevier.com/locate/shpsa/, Fax: 011 44 1865 843010",

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TY - JOUR

T1 - A new T677C mutation of the aspartoacylase gene encodes for a protein with no enzymatic activity

AU - Tavazzi, Barbara

AU - Di Pietro, Valentina

AU - Amorini, Angela Maria

AU - Giardina, Bruno

AU - Lazzarino, Giuseppe

PY - 2008

Y1 - 2008

N2 - OBJECTIVE: To verify the effect of and to date the unknown T677C mutation of the human N-acetylaspartoacylase (hASPA) gene on the function of the mutated enzyme. DESIGN AND METHODS: Wild type and I226T-mutated proteins were expressed and purified from a transformed Escherichia coli colony. Enzymatic activities were measured in the presence of varying substrate concentrations. RESULTS: Whilst kinetic parameters of wild type hASPA were in line with data in literature, I226T-mutated hASPA showed no enzymatic activity. CONCLUSION: Data indicated that this new mutation might be responsible in homozygosis for the phenotype corresponding to Canavan disease.

AB - OBJECTIVE: To verify the effect of and to date the unknown T677C mutation of the human N-acetylaspartoacylase (hASPA) gene on the function of the mutated enzyme. DESIGN AND METHODS: Wild type and I226T-mutated proteins were expressed and purified from a transformed Escherichia coli colony. Enzymatic activities were measured in the presence of varying substrate concentrations. RESULTS: Whilst kinetic parameters of wild type hASPA were in line with data in literature, I226T-mutated hASPA showed no enzymatic activity. CONCLUSION: Data indicated that this new mutation might be responsible in homozygosis for the phenotype corresponding to Canavan disease.

KW - Aspartoacylase

KW - Canavan desease

KW - NAA

KW - Aspartoacylase

KW - Canavan desease

KW - NAA

UR - http://hdl.handle.net/10807/16383

M3 - Article

SN - 0009-9120

SP - 611

EP - 615

JO - Clinical Biochemistry

JF - Clinical Biochemistry

ER -

A new T677C mutation of the aspartoacylase gene encodes for a protein with no enzymatic activity

Abstract

Keywords

OSS delle Nazioni Unite

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