期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 137, 期 46, 页码 14570-14573出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.5b08968
关键词
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资金
- National Institutes of Health [U54GM093342]
- DOE Office of Science by Argonne National Laboratory [DE-AC02-06CH11357]
We describe a general integrated bioinformatic and experimental strategy to discover the in vitro enzymatic activities and in vivo functions (metabolic pathways) of uncharacterized enzymes discovered in microbial genome projects using the ligand specificities of the solute binding proteins (SBPs) for ABC transporters. Using differential scanning fluorimetry, we determined that the SBP for an ABC transporter encoded by the genome of Mycobacterium smegmatis is stabilized by d-threitol. Using sequence similarity networks and genome neighborhood networks to guide selection of target proteins for pathway enzymes, we applied both in vitro and in vivo experimental approaches to discover novel pathways for catabolism of d-threitol, l-threitol, and erythritol.
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