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Article

Identification of a single amino acid substitution in the diphtheria toxin A chain of CRM 228 responsible for the loss of enzymatic activity.

Journal of bacteriology - 1 Aug 1994

Johnson V G, Nicholls P J

Abstract excerpt

CRM 228 (T. Uchida, A. M. Pappenheimer, and R. Greany, J. Biol. Chem. 248:3838-3844, 1973), a mutant form of diphtheria toxin which completely lacks ADP-ribosyltransferase activity, contains five amino acid substitutions. The two amino acid changes that fall within the A chain of the toxin (G79D and E162K) were separately analyzed by substituting a variety of other amino acids at these sites. The substitution at...

Topics

Corynebacterium diphtheriae
Cross Reactions
Diphtheria Toxin
Mutation
Poly(ADP-ribose) Polymerases
Structure-Activity Relationship

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 8045910
DOI: 10.1128/jb.176.15.4766-4769.1994
PMCID: PMC196302

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8045910-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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