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Article

Interaction between the cytoplasmic and membrane-bound domains of enzyme IImtl of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system.

Biochemistry - 9 Jul 1991

Lolkema J S, Dijkstra D S, ten Hoeve-Duurkens R H, Robillard G T

Abstract excerpt

Sulfhydryl reagents affected the binding properties of the translocator domain, NIII, of enzyme IImtl in two ways: (i) the affinity for mannitol was reduced, and (ii) the exchange rate of bound and free mannitol was increased. The effect on the affinity was very much reduced after solubilization of enzyme IImtl in the detergent decylPEG. The effects were caused exclusively by reaction of the sulfhydryl reagents...

Topics

Cytoplasm
Escherichia coli
Escherichia coli Proteins
Membrane Proteins
Monosaccharide Transport Proteins
Mutation
Phosphoenolpyruvate Sugar Phosphotransferase System
Phosphorylation
Substrate Specificity
Sulfhydryl Compounds

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Identifiers

PMID: 2065056
DOI: 10.1021/bi00241a013

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2065056-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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