Evidence for a single catalytic and two binding sites in the almond emulsin β-D-glucosidase molecule

L. Kiss, Lili K. Berki, Pál Nánási

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

An isoenzyme of glucosidase- isolated from sweet almond emulsin - and composed of a β-D-glucosidase, a β-D-galactosidase and a β-D-fucosidase, has been shown to possess β-D-xylosidase activity, as well. On the basis of the following results it has been concluded that the β-D-glucosidase and β-D-galactosidase activities reside in one catalytic site, but there are two kinetically distinst binding sites in the active center: 1./D-Glucono-1,5-lactone is shown to excert competitive inhibition on the hydrolysis of β-D-glucopyranoside and non-competitive inhibition on the hydrolysis of β-D-galactopyranoside. 2./ D-galactono-1,5-lactone competitively inhibits the hydrolysis of β-D-galactopyranoside, but possesses non-competitive inhibition on the hydrolysis of β-D-glucopyranoside. 3./ When the enzyme is incubated with two p-nitrophenyl glycoside substrates at or above their respective Km values, the rate of p-nitrophenol formation is not additive but rather it is equal to the value calculated from the individual Km values and relative maximum rates.

Original languageEnglish
Pages (from-to)792-799
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume98
Issue number3
DOIs
Publication statusPublished - Feb 12 1981

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Glucosidases
Hydrolysis
Binding Sites
Galactosidases
Molecules
Lactones
Galactose
Xylosidases
alpha-L-Fucosidase
Glycosides
Isoenzymes
Catalytic Domain
Prunus dulcis
Substrates
Enzymes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Evidence for a single catalytic and two binding sites in the almond emulsin β-D-glucosidase molecule. / Kiss, L.; Berki, Lili K.; Nánási, Pál.

In: Biochemical and Biophysical Research Communications, Vol. 98, No. 3, 12.02.1981, p. 792-799.

Research output: Contribution to journalArticle

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