Characterization of site-directed mutants in the lac permease of Escherichia coli. 2. Glutamate-325 replacements-Reference-Cited by-同舟云学术

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Characterization of site-directed mutants in the lac permease of Escherichia coli. 2. Glutamate-325 replacements

Published:1989-03 Issue:6 Volume:28 Page:2533-2539
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Carrasco Nancy,Puttner Irene B.,Antes Lisa M.,Lee Jonathan A.,Larigan J. Douglas,Lolkema Julius S.,Roepe Paul D.,Kaback H. Ronald

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00432a028

Reference39 articles.

1. Topological Studies of Lactose Permease of Escherichia coli by Protein Sequence Analysis

2. Sequence of the lactose permease gene

3. Monoclonal antibodies against the lac carrier protein from Escherichia coli. 1. Functional studies

4. Lac permease of Escherichia: histidine-322 and glutamic acid-325 may be components of a charge-relay system

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1. Mechanisms of long-distance allosteric couplings in proton-binding membrane transporters;Membrane Proteins;2022

2. It's Better To Be Lucky Than Smart;Annual Review of Biochemistry;2021-06-20

3. Monoclonal antibody 4B1 influences the p K a of Glu325 in lactose permease (LacY) from Escherichia coli : evidence from SEIRAS;FEBS Letters;2020-08-30

4. The proton electrochemical gradient induces a kinetic asymmetry in the symport cycle of LacY;Proceedings of the National Academy of Sciences;2019-12-30

5. It takes two to tango: The dance of the permease;Journal of General Physiology;2019-05-30

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