EurekaMag.com logo
+ Translate

Specificity of the Escherichia coli proline transport system


, : Specificity of the Escherichia coli proline transport system. Journal of Bacteriology 123(3): 871-877

The presence of both the carbonyl portion of the carboxyl group at position 2 of the pyrrolidine ring and a secondary amine was essential for uptake of a compound by the proline permease of Escherichia coli. The permease possessed a high affinity for azetidine-2-carboxylic acid and for compounds with ring structures smaller than the pyrrolidine ring. Pipecolic acid, the higher homologue of proline, and its derivatives were not transported. Cis- and trans-3,4-methano-prolines, also six-membered ring structures, behaved anomolously in that they possessed a high affinity for the permease. The difference between the methano-prolines and other six-membered ring structures probably resides in the fact that the former exist in the "boat" configuration whereas the latter possess the "chair" configuration. In general, substituted prolines in the cis configuration displayed a higher affinity for the permease than did corresponding trans isomers, though the affinity for substituted prolines was influenced by the position, size, and polar or nonpolar nature of the substituent group. At O C many analogues with affinity for proline permease exchanged with intracellular proline, but some analogues, notably trans-3-methyl- and trans-4-methyl-L-prolines, though possessing high affinity for the permease, showed an almost complete inability to exchange with intracellular proline.

(PDF 0-2 workdays service)

Accession: 006459054

PMID: 1099081

Submit PDF Full Text: Here


Submit PDF Full Text

No spam - Every submission is manually reviewed

Due to poor quality, we do not accept files from Researchgate

Submitted PDF Full Texts will always be free for everyone
(We only charge for PDFs that we need to acquire)

Select a PDF file:
Close
Close

Related references

Mogi, T.; Anraku, Y., 1984: Mechanism of proline transport in Escherichia coli K12. III. Inhibition of membrane potential-driven proline transport by syn-coupled ions and evidence for symmetrical transition states of the 2H+/proline symport carrier. Specific inhibition of 2H+/proline symport by syn-coupled ions (Na+, Li+, and H+) was investigated using cytoplasmic membrane vesicles prepared from the proline carrier-overproducing strain MinS/ pLC4 -45 of Escherichia coli K12. The 2H+/proline s...

Mogi, T.; Anraku, Y., 1984: Mechanism of proline transport in Escherichia coli K12: inhibition of membrane potential-driven proline transport by syn-coupled ions and evidence for symmetrical transition states of the 2H+/proline symport carrier. The Journal of Biological Chemistry 259: 02-6

Mogi, T.; Anraku, Y., 1984: Mechanism of proline transport in escherichia coli k 12 3. inhibition of membrane potential driven proline transport by syn coupled ions and evidence for symmetrical transition states of the proton proline symport carrier. Specific inhibition of 2H+/proline symport by syn-coupled ions (Na+, Li+ and H+) was investigated using cytoplasmic membrane vesicles prepared from the proline carrier-overproducing strain MinS/pLC4-45 of E. coli K12. The 2H+/proline symport drive...

Wengender, P.A.; Miller, K.J., 1995: Identification of a PutP proline permease gene homolog from Staphylococcus aureus by expression cloning of the high-affinity proline transport system in Escherichia coli. The important food-borne pathogen Staphylococcus aureus is distinguished by its ability to grow at low water activity values. Previous work in our laboratory and by others has revealed that proline accumulation via transport is an important osmore...

Yazyu, H.; Shiota, S.; Futai, M.; Tsuchiya, T., 1985: Alteration in cation specificity of the melibiose transport carrier of Escherichia coli due to replacement of proline 122 with serine. The structural genes (melB) for the melibiose carrier of five mutants of Escherichia coli showing altered cation specificity for melibiose transport were cloned. The mutations were mapped in a 248-base-pair DNA fragment by a recombinational assay...

Mogi, T.; Anraku, Y., 1984: Mechanism of proline transport in Escherichia coli K12. II. Effect of alkaline cations on binding of proline to a H+/proline symport carrier in cytoplasmic membrane vesicles. The substrate binding reaction of the proline carrier was investigated in nonenergized conditions using cytoplasmic membrane vesicles prepared from the proline carrier-overproducing strain MinS/ pLC4 -45 of Escherichia coli K12. The binding activi...

Mogi, T.; Anraku, Y., 1984: Mechanism of proline transport in Escherichia coli K12: effect of alkaline cations on binding of proline to a H+/proline symport carrier in cytoplasmic membrane vesicles. The Journal of Biological Chemistry 259: 97-801

Yamato, I., 1990: Study of the major proline transport system in Escherichia coli. Seikagaku. Journal of Japanese Biochemical Society 62(8): 1020-1030

Mogi, T.; Anraku, Y., 1984: Mechanism of proline transport in escherichia coli k 12 2. effect of alkaline cations on binding of proline to a proton proline symport carrier in cytoplasmic membrane vesicles. The substrate binding reaction of the proline carrier was investigated in nonenergized conditions using cytoplasmic membrane vesicles prepared from the proline carrier-overproducing strain MinS/pLC4-45 of E. coli K12. The binding activity specific...

Chen, C.C.; Wilson, T.H., 1986: Solubilization and functional reconstitution of the proline transport system of Escherichia coli. The membrane carrier for L-proline (product of the putP gene) of Escherichia coli K12 was solubilized and functionally reconstituted with E. coli phospholipid by the cholate dilution method. The counterflow activity of the reconstituted system was...