Identification and Characterization of a Bacterial Periplasmic Solute Binding Protein That Binds <scp>l</scp>-Amino Acid Amides-Reference-Cited by-同舟云学术

Identification and Characterization of a Bacterial Periplasmic Solute Binding Protein That Binds l-Amino Acid Amides

Published:2024-05-02 Issue:10 Volume:63 Page:1322-1334
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Smith Oliver B.¹²^ORCID,Frkic Rebecca L.¹³,Rahman Marina G.²⁴,Jackson Colin J.¹²³⁴^ORCID,Kaczmarski Joe A.²⁴

Affiliation:

1. Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory 2601, Australia

2. ARC Centre of Excellence in Synthetic Biology, Australian National University, Canberra, Australian Capital Territory 2601, Australia

3. ARC Centre of Excellence for Innovations in Peptide & Protein Science, Australian National University, Canberra, Australian Capital Territory 2601, Australia

4. Research School of Biology, Australian National University, Canberra, Australian Capital Territory 2601, Australia

Funder

Australian Research Council

Australian Government

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.4c00096

Reference83 articles.

1. Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems

2. Maltose/Maltodextrin System of Escherichia coli : Transport, Metabolism, and Regulation

3. An ATP Binding Cassette Transporter Mediates the Uptake of α-(1,6)-Linked Dietary Oligosaccharides in Bifidobacterium and Correlates with Competitive Growth on These Substrates

4. Two Closely Related ABC Transporters in Streptococcus mutans Are Involved in Disaccharide and/or Oligosaccharide Uptake

5. Carbohydrate-Binding Capability and Functional Conformational Changes of AbnE, an Arabino-oligosaccharide Binding Protein