Journal article
Lac permease of Escherichia coli: histidine-322 and glutamic acid-325 may be components of a charge-relay system
Biochemistry (Easton), Vol.25(16), pp.4486-4488
1986
DOI: 10.1021/bi00364a004
PMID: 2876725
Abstract
When Glu-325 in the lac permease of Escherichia coli is replaced with Ala, lactose/H+ symport is abolished. Thus, the altered permease catalyzes neither uphill lactose accumulation nor efflux. Remarkably, however, permease with Ala-325 catalyzes exchange and counterflow at completely normal rates. Taken together with the results presented in the accompanying paper [Püttner, I. B., Sarkar, H. K., Poonian, M. S., & Kaback, H. R. (1986) Biochemistry (preceding paper in this issue)], the findings suggest that the His-322 and Glu-325 may be components of a charge-relay system that plays an important role in the coupled translocation of lactose and H+.
Details
- Title: Subtitle
- Lac permease of Escherichia coli: histidine-322 and glutamic acid-325 may be components of a charge-relay system
- Creators
- Nancy Carrasco - Hoffmann-La Roche inc., Nutley NJ 07110, United StatesLisa M Antes - Hoffmann-La Roche inc., Nutley NJ 07110, United StatesMohindar S Poonian - Hoffmann-La Roche inc., Nutley NJ 07110, United StatesH. Ronald Kaback - Hoffmann-La Roche inc., Nutley NJ 07110, United States
- Resource Type
- Journal article
- Publication Details
- Biochemistry (Easton), Vol.25(16), pp.4486-4488
- Publisher
- American Chemical Society
- DOI
- 10.1021/bi00364a004
- PMID
- 2876725
- ISSN
- 0006-2960
- eISSN
- 1520-4995
- Language
- English
- Date published
- 1986
- Academic Unit
- Nephrology; Internal Medicine
- Record Identifier
- 9984094771302771
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