JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wiley, W. R.
Right arrow Articles by Matchett, W. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wiley, W. R.
Right arrow Articles by Matchett, W. H.

 Previous Article  |  Next Article 

J Bacteriol. 1966 December; 92(6): 1698-1705
Copyright © 1966 American Society for Microbiology. All Rights Reserved.

Tryptophan Transport in Neurospora crassa I. Specificity and Kinetics

W. R. Wiley and W. H. Matchett

Biology Department, Battelle Memorial Institute, Pacific Northwest Laboratory, Richland, Washington

ABSTRACT

WILEY, W. R. (Battelle Memorial Institute, Richland, Wash.), AND W. H. MATCHETT. Tryptophan transport in Neurospora crassa. I. Specificity and kinetics. J. Bacteriol. 92:1698–1705. 1966.—The transport of tryptophan in Neurospora crassa is mediated by a distinct stereospecific system which is chemically specific for a family of neutral amino acids. The process shows typical saturation kinetics and a sharp decrease in the rate of tryptophan uptake at low temperatures. The Q10 for the process is approximately 2 between 20 and 30 C. The apparent Km for uptake is 5 x 10–5M. Leucine and phenylalanine competitively inhibit the rate of tryptophan transport; the Ki values are 1.1 x 10–4M and 4.0 x 10–5M, respectively. These data are interpreted as evidence that these amino acids are transported by the same transport site(s). Inhibition studies with amino acids and other compounds structurally related to leucine and phenylalanine suggest that an uncharged side chain and an {alpha} amino group, next to a carboxyl, represent three attachment points for the uptake site.


J Bacteriol. 1966 December; 92(6): 1698-1705
Copyright © 1966 American Society for Microbiology. All Rights Reserved.







Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 1966 by the American Society for Microbiology. All rights reserved.