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. 1971 Dec;125(3):717–719. doi: 10.1042/bj1250717

β-Galactosidase-catalysed hydrolysis of β-d-galactopyranosyl azide

Michael L Sinnott 1
PMCID: PMC1178175  PMID: 4947657

Abstract

1. β-d-Galactopyranosyl azide is hydrolysed by the β-galactosidase of Escherichia coli to galactose and azide ion at a mechanistically significant rate. 2. Methyl 1-thio-β-d-galactopyranoside is a competitive inhibitor of the hydrolysis of the azide and of o-nitrophenyl β-d-galactopyranoside with Ki 1.8mm. 3. β-Galactosidase can thus hydrolyse a range of substrates of general structure β-d-galactopyranosyl-X(Y), where the atom X has a lone pair of electrons on which the enzyme may act as a Lewis or Brønsted acid, but in which the length of the bond cleaved varies significantly, which is inconsistent with the orbital steering hypothesis.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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