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Article

Substitution of aspartic acid-217 of Citrobacter freundii cephalosporinase and properties of the mutant enzymes.

FEBS letters - 21 May 1990

Tsukamoto K, Kikura R, Ohno R, Sawai T

Abstract excerpt

On the assumption that Asp-217 of a Citrobacter freundii cephalosporinase forms a salt-bridge with the conserved Lys-67, Asp-217 was changed to glutamic acid, threonine or lysine. The mutant enzymes retained about the same level of activity as that of the wild-type enzyme, and the participation of Asp-217 in the salt-bridge was ruled out. However, the mutations resulted in an increase in hydrolytic activity...

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Source

Identifiers

PMID: 1972682
DOI: 10.1016/0014-5793(90)80250-m

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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