The Y430F mutant of Salmonella d-ornithine/d-lysine decarboxylase has altered stereospecificity and a putrescine allosteric activation site

Phillips, Robert S.; Hoang, Kim-Ngoc Nguyen

doi:10.1016/j.abb.2022.109429

Cited by 1 publication

(2 citation statements)

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“…For instance, putrescine is generated from decarboxylation of l-ornithine via ODC, l-arginine can be converted to agmatine by ADC, and l-lysine can be decarboxylated by LDC to yield cadaverine. 10 Typically, these amino acid decarboxylases exhibit substrate insensitivity under normal conditions. 11 For instance, Michael's research 8 revealed that ADC enzymes derived from Bacillus subtilis can facilitate the decarboxylation of l-arginine and l-lysine, resulting in the production of agmatine and cadaverine.…”

Section: Introductionmentioning

confidence: 99%

“…In cells, polyamines primarily are produced from amino acids. For instance, putrescine is generated from decarboxylation of l ‐ornithine via ODC, l ‐arginine can be converted to agmatine by ADC, and l ‐lysine can be decarboxylated by LDC to yield cadaverine 10 . Typically, these amino acid decarboxylases exhibit substrate insensitivity under normal conditions 11 .…”

Section: Introductionmentioning

confidence: 99%

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Enzymatic properties of ornithine decarboxylase from Clostridium aceticum DSM1496

Tan,

Gou,

Fan

et al. 2024

Biotech and App Biochem

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Clostridium aceticum DSM1496 is an acid‐resistant strain in which ornithine decarboxylase (ODC) plays a crucial role in acid resistance. In this study, we expressed ODC derived from C. aceticum DSM1496 in Escherichia coli BL21 (DE3) and thoroughly examined its enzymatic properties. The enzyme has a molecular weight of 55.27 kDa and uses pyridoxal‐5′‐phosphate (PLP) as a coenzyme with a Km = 0.31 mM. ODC exhibits optimal activity at pH 7.5, and it maintains high stability even at pH 4.5. The peak reaction temperature for ODC is 30°C. Besides, it can be influenced by certain metal ions such as Mn2+. Although l‐ornithine serves as the preferred substrate for ODC, the enzyme also decarboxylates l‐arginine and l‐lysine simultaneously. The results indicate that ODC derived from C. aceticum DSM1496 exhibits the ability to produce putrescine, cadaverine, and agmatine through decarboxylation. These polyamines have the potential to neutralize acid in an acidic environment, facilitating the growth of microorganisms. These significant findings provide a strong basis for further investigation into the acid‐resistant mechanisms contributed by ODC.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%