Relation between the Oligomerization State and the Transport and Phosphorylation Function of the Escherichia coli Mannitol Transport Protein: Interaction between Mannitol-Specific Enzyme II Monomers Studied by Complementation of Inactive Site-Directed Mutants-Reference-Cited by-同舟云学术

Relation between the Oligomerization State and the Transport and Phosphorylation Function of the Escherichia coli Mannitol Transport Protein: Interaction between Mannitol-Specific Enzyme II Monomers Studied by Complementation of Inactive Site-Directed Mutants

Published:1996-01-01 Issue:39 Volume:35 Page:12901-12908
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Boer Harry¹,ten Hoeve-Duurkens Ria H.¹,Robillard G. T.¹

Affiliation:

1. The Groningen Biomolecular Science and Biotechnology Institute (GBB) and the Department of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9611016

Reference47 articles.

1. Expression, purification, and kinetic characterization of the mannitol transport domain of the phosphoenolpyruvate-dependent mannitol phosphotransferase system of Escherichia coli. Kinetic evidence that the E. coli mannitol transport protein is a functional dimer.

2. The glucose transporter of Escherichia coli. Mutants with impaired translocation activity that retain phosphorylation activity.

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