A study of the effect on nucleophilic hydrolytic activity of pancreatic elastase, trypsin, chymotrypsin, and leucine aminopeptidase by boronic acids in the presence of arabinogalactan: A subsequent study on the hydrolytic activity of chymotrypsin by boronic acids in the presence of mono-, di-, and trisaccharides

Reem Smoum; Abraham Rubinstein; Morris Srebnik

doi:10.1016/j.bioorg.2003.08.004

A study of the effect on nucleophilic hydrolytic activity of pancreatic elastase, trypsin, chymotrypsin, and leucine aminopeptidase by boronic acids in the presence of arabinogalactan: A subsequent study on the hydrolytic activity of chymotrypsin by boronic acids in the presence of mono-, di-, and trisaccharides

Reem Smoum, Abraham Rubinstein^*, Morris Srebnik

^*Corresponding author for this work

School of Pharmacy

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19 Scopus citations

Abstract

The hydrolytic activity of trypsin, chymotrypsin, elastase, and leucine aminopeptidase, is inhibited by different boronic acids. However, all the enzymes are inhibited by the compound CbzAla(boro)Gly(OH)₂. Therefore, these additives can control the nucleophilic hydrolytic activity of these enzymes.

Original language	English
Pages (from-to)	464-474
Number of pages	11
Journal	Bioorganic Chemistry
Volume	31
Issue number	6
DOIs	https://doi.org/10.1016/j.bioorg.2003.08.004
State	Published - Dec 2003

Keywords

Boronic acids
Hydrolytic activity
Inhibition
Saccharides
Serine proteases

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Smoum, R., Rubinstein, A., & Srebnik, M. (2003). A study of the effect on nucleophilic hydrolytic activity of pancreatic elastase, trypsin, chymotrypsin, and leucine aminopeptidase by boronic acids in the presence of arabinogalactan: A subsequent study on the hydrolytic activity of chymotrypsin by boronic acids in the presence of mono-, di-, and trisaccharides. Bioorganic Chemistry, 31(6), 464-474. https://doi.org/10.1016/j.bioorg.2003.08.004

Smoum, Reem ; Rubinstein, Abraham ; Srebnik, Morris. / A study of the effect on nucleophilic hydrolytic activity of pancreatic elastase, trypsin, chymotrypsin, and leucine aminopeptidase by boronic acids in the presence of arabinogalactan : A subsequent study on the hydrolytic activity of chymotrypsin by boronic acids in the presence of mono-, di-, and trisaccharides. In: Bioorganic Chemistry. 2003 ; Vol. 31, No. 6. pp. 464-474.

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abstract = "The hydrolytic activity of trypsin, chymotrypsin, elastase, and leucine aminopeptidase, is inhibited by different boronic acids. However, all the enzymes are inhibited by the compound CbzAla(boro)Gly(OH)2. Therefore, these additives can control the nucleophilic hydrolytic activity of these enzymes.",

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Smoum, R , Rubinstein, A & Srebnik, M 2003, 'A study of the effect on nucleophilic hydrolytic activity of pancreatic elastase, trypsin, chymotrypsin, and leucine aminopeptidase by boronic acids in the presence of arabinogalactan: A subsequent study on the hydrolytic activity of chymotrypsin by boronic acids in the presence of mono-, di-, and trisaccharides', Bioorganic Chemistry, vol. 31, no. 6, pp. 464-474. https://doi.org/10.1016/j.bioorg.2003.08.004

A study of the effect on nucleophilic hydrolytic activity of pancreatic elastase, trypsin, chymotrypsin, and leucine aminopeptidase by boronic acids in the presence of arabinogalactan: A subsequent study on the hydrolytic activity of chymotrypsin by boronic acids in the presence of mono-, di-, and trisaccharides. / Smoum, Reem ; Rubinstein, Abraham; Srebnik, Morris.
In: Bioorganic Chemistry, Vol. 31, No. 6, 12.2003, p. 464-474.

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

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Smoum R , Rubinstein A, Srebnik M. A study of the effect on nucleophilic hydrolytic activity of pancreatic elastase, trypsin, chymotrypsin, and leucine aminopeptidase by boronic acids in the presence of arabinogalactan: A subsequent study on the hydrolytic activity of chymotrypsin by boronic acids in the presence of mono-, di-, and trisaccharides. Bioorganic Chemistry. 2003 Dec;31(6):464-474. doi: 10.1016/j.bioorg.2003.08.004

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