ArticleApplied and environmental microbiology2022
Regulation of l- and d-Aspartate Transport and Metabolism in Acinetobacter baylyi ADP1.
Article in Applied and environmental microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- Recent progress in microbial production of D-aspartate.World journal of microbiology & biotechnology · 2026Review
- Effects of cultivation conditions on D-aspartate production by the lactic acid bacterium Latilactobacillus curvatus strain WDN19.Biotechnology letters · 2025Article
- Rewiring Aromatic Compound Consumption: Chromosomal Amplification and Evolution of a Foreign Pathway inACS synthetic biology · 2025Article
- Fundamentals and Exceptions of the LysR-type Transcriptional Regulators.ACS synthetic biology · 2024Review
- Survival and virulence of Acinetobacter baumannii in microbial mixtures.BMC microbiology · 2024Article
- Aspartate aminotransferase ofMicrobiology (Reading, England) · 2024Article
- Regulation of tricarboxylate transport and metabolism inApplied and environmental microbiology · 2024Article
- Acinetobacter Metabolism in Infection and Antimicrobial Resistance.Infection and immunity · 2023Review
Corrections and comments
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Authors and funding
14 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The regulated uptake and consumption of d-amino acids by bacteria remain largely unexplored, despite the physiological importance of these compounds. Unlike other characterized bacteria, such as Escherichia coli, which utilizes only l-Asp, Acinetobacter baylyi ADP1 can consume both d-Asp and l-Asp as the sole carbon or nitrogen source. As described here, two LysR-type transcriptional regulators (LTTRs), DarR and AalR, control d- and l-Asp metabolism in strain ADP1. Heterologous expression of A. baylyi proteins enabled E. coli to use d-Asp as the carbon source when either of two transporters (AspT or AspY) and a racemase (RacD) were coexpressed. A third transporter, designated AspS, was also discovered to transport Asp in ADP1. DarR and/or AalR controlled the transcription of
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