Studies on the N-acetyl-β-d-hexosaminidase B from germinating Lupinus luteus L. seeds II. Mechanism and inhibition with some 2-acetamido-2-deoxyaldono(1 å 4)lactones

I. Pócsi, L. Kiss, Virág Zsoldos-Mády, I. Pintér

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9 Citations (Scopus)

Abstract

The N-acetyl-β-d-hexosaminidase B of germinating yellow lupin seeds catalyzed the hydrolysis of both N-acetyl-β-d-glucosaminide and -galactosaminide substrates. The investigation of the pH dependence of the kinetic parameters (Vmax and Vmax/Km) demonstrated that two common ionizable groups (probably two carboxyl groups) play an essential role in the catalysis. That is, the enzyme has a lysozyme-like splitting mechanism, and the possibility of an anchimeric assistance provided by the acetamido group seems to be negligible. The presence of a deprotonated carboxyl group near the glycosidic linkage was also supported by inhibition with 1-thio substrate analogues. On the other hand, some 2-acetamido-2-deoxyaldono(1 å 4)lactones proved to be effective inhibitors of the hexosaminidase with the exception of the d-arabinose derivative, which can be explained by high stereospecificity in the binding.

Original languageEnglish
Pages (from-to)119-122
Number of pages4
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1039
Issue number1
DOIs
Publication statusPublished - May 31 1990

Fingerprint

Hexosaminidase B
Lupinus
Hexosaminidases
Arabinose
Lactones
Muramidase
Catalysis
Seed
Seeds
Hydrolysis
Substrates
Enzymes
Kinetic parameters
Derivatives

Keywords

  • Enzyme inhibition
  • Hexosaminidase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology

Cite this

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title = "Studies on the N-acetyl-β-d-hexosaminidase B from germinating Lupinus luteus L. seeds II. Mechanism and inhibition with some 2-acetamido-2-deoxyaldono(1 {\aa} 4)lactones",
abstract = "The N-acetyl-β-d-hexosaminidase B of germinating yellow lupin seeds catalyzed the hydrolysis of both N-acetyl-β-d-glucosaminide and -galactosaminide substrates. The investigation of the pH dependence of the kinetic parameters (Vmax and Vmax/Km) demonstrated that two common ionizable groups (probably two carboxyl groups) play an essential role in the catalysis. That is, the enzyme has a lysozyme-like splitting mechanism, and the possibility of an anchimeric assistance provided by the acetamido group seems to be negligible. The presence of a deprotonated carboxyl group near the glycosidic linkage was also supported by inhibition with 1-thio substrate analogues. On the other hand, some 2-acetamido-2-deoxyaldono(1 {\aa} 4)lactones proved to be effective inhibitors of the hexosaminidase with the exception of the d-arabinose derivative, which can be explained by high stereospecificity in the binding.",
keywords = "Enzyme inhibition, Hexosaminidase",
author = "I. P{\'o}csi and L. Kiss and Vir{\'a}g Zsoldos-M{\'a}dy and I. Pint{\'e}r",
year = "1990",
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AU - Pócsi, I.

AU - Kiss, L.

AU - Zsoldos-Mády, Virág

AU - Pintér, I.

PY - 1990/5/31

Y1 - 1990/5/31

N2 - The N-acetyl-β-d-hexosaminidase B of germinating yellow lupin seeds catalyzed the hydrolysis of both N-acetyl-β-d-glucosaminide and -galactosaminide substrates. The investigation of the pH dependence of the kinetic parameters (Vmax and Vmax/Km) demonstrated that two common ionizable groups (probably two carboxyl groups) play an essential role in the catalysis. That is, the enzyme has a lysozyme-like splitting mechanism, and the possibility of an anchimeric assistance provided by the acetamido group seems to be negligible. The presence of a deprotonated carboxyl group near the glycosidic linkage was also supported by inhibition with 1-thio substrate analogues. On the other hand, some 2-acetamido-2-deoxyaldono(1 å 4)lactones proved to be effective inhibitors of the hexosaminidase with the exception of the d-arabinose derivative, which can be explained by high stereospecificity in the binding.

AB - The N-acetyl-β-d-hexosaminidase B of germinating yellow lupin seeds catalyzed the hydrolysis of both N-acetyl-β-d-glucosaminide and -galactosaminide substrates. The investigation of the pH dependence of the kinetic parameters (Vmax and Vmax/Km) demonstrated that two common ionizable groups (probably two carboxyl groups) play an essential role in the catalysis. That is, the enzyme has a lysozyme-like splitting mechanism, and the possibility of an anchimeric assistance provided by the acetamido group seems to be negligible. The presence of a deprotonated carboxyl group near the glycosidic linkage was also supported by inhibition with 1-thio substrate analogues. On the other hand, some 2-acetamido-2-deoxyaldono(1 å 4)lactones proved to be effective inhibitors of the hexosaminidase with the exception of the d-arabinose derivative, which can be explained by high stereospecificity in the binding.

KW - Enzyme inhibition

KW - Hexosaminidase

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