Comparative structural and enzymatic studies on Salmonella typhimurium diaminopropionate ammonia lyase reveal its unique features

Deka, G.; Bisht, S.; Savithri, H.S.; Murthy, M.R.N.

doi:10.1016/j.jsb.2017.12.012

Cited by 5 publications

(1 citation statement)

References 31 publications

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“…Tm is a pivotal component of this ATR system. 130 The enzyme consumes cytoplasmic protons in the process of L-arg degradation to agmatine. 86 Consequently, the arginine-agmatine antiporter (AdiC) exchanges the product agmatine for L-arg again.…”

Section: Bacterial Pathogensmentioning

confidence: 99%

L-arginine metabolism as pivotal interface of mutual host–microbe interactions in the gut

et al. 2023

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L-arginine (L-arg) is a versatile amino acid and a central intestinal metabolite in mammalian and microbial organisms. Thus, L-arg participates as precursor of multiple metabolic pathways in the regulation of cell division and growth. It also serves as a source of carbon, nitrogen, and energy or as a substrate for protein synthesis. Consequently, L-arg can simultaneously modify mammalian immune functions, intraluminal metabolism, intestinal microbiota, and microbial pathogenesis. While dietary intake, protein turnover or de novo synthesis usually supply L-arg in sufficient amounts, the expression of several key enzymes of L-arg metabolism can change rapidly and dramatically following inflammation, sepsis, or injury. Consequently, the availability of L-arg can be restricted due to increased catabolism, transforming L-arg into an essential amino acid. Here, we review the enzymatic pathways of L-arg metabolism in microbial and mammalian cells and their role in immune function, intraluminal metabolism, colonization resistance, and microbial pathogenesis in the gut.

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Section: Bacterial Pathogensmentioning

confidence: 99%