Arginine inhibition of the argininosuccinate lyases is conserved among three orders in cyanobacteria

Katayama, Noriaki; Osanai, Takashi

doi:10.1007/s11103-022-01280-x

Cited by 2 publications

(3 citation statements)

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“…These results indicate that Sy ArgG is more sensitively regulated by feedback inhibition than Pp ASSY. This arginine inhibition is similar to that of previously reported arginine biosynthesis enzymes (NAGK and Sy ArgH) in cyanobacteria (Hoare and Hoare 1966 ; Bolay et al 2021 ; Katayama and Osanai 2022 ). Under physiological conditions, the intracellular arginine concentration in Synechocystis 6803 is 0.6 mM (Zhang et al 2018 ).…”

Section: Discussionsupporting

confidence: 91%

“…Synechocystis 6803 cell crude extract experiments also show that N -acetylornithine aminotransferase activity is 2-fold higher than argininosuccinate synthetase activity (Liu and Yang 2014 ). The k cat / K m of Sy ArgG for the substrate (citrulline: 1.97 s − 1 mM − 1 , aspartate: 2.16 s − 1 mM − 1 ) was lower than that of the last-step enzyme in arginine biosynthesis ( Sy ArgH: 37.3 s − 1 mM − 1 ) (Katayama and Osanai 2022 ). These results indicate that Sy ArgG is the rate-limiting enzyme in arginine biosynthesis.…”

Section: Discussionmentioning

confidence: 99%

“…In cyanobacteria, N -acetyl-glutamate kinase (NAGK) is a second-step enzyme that is primarily subject to feedback inhibition by arginine during its biosynthesis (Hoare and Hoare 1966 ). Cyanobacterial argininosuccinate lyase (ArgH), the last step of arginine biosynthesis, is also inhibited by arginine, and this inhibition for cyanobacterial ArgH changes with pH (Katayama and Osanai 2022 ). Arginine biosynthesis is also regulated by P II proteins that are widely distributed in bacteria, eukaryotic algae, and plants, and are involved in the regulation of nitrogen assimilation and metabolism (Forchhammer 2004 ).…”

Section: Introductionmentioning

confidence: 99%

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Arginine inhibits the arginine biosynthesis rate-limiting enzyme and leads to the accumulation of intracellular aspartate in Synechocystis sp. PCC 6803

Katayama,

Osanai

2024

Plant Mol Biol

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Cyanobacteria are oxygen-evolving photosynthetic prokaryotes that affect the global carbon and nitrogen turnover. Synechocystis sp. PCC 6803 (Synechocystis 6803) is a model cyanobacterium that has been widely studied and can utilize and uptake various nitrogen sources and amino acids from the outer environment and media. l-arginine is a nitrogen-rich amino acid used as a nitrogen reservoir in Synechocystis 6803, and its biosynthesis is strictly regulated by feedback inhibition. Argininosuccinate synthetase (ArgG; EC 6.3.4.5) is the rate-limiting enzyme in arginine biosynthesis and catalyzes the condensation of citrulline and aspartate using ATP to produce argininosuccinate, which is converted to l-arginine and fumarate through argininosuccinate lyase (ArgH). We performed a biochemical analysis of Synechocystis 6803 ArgG (SyArgG) and obtained a Synechocystis 6803 mutant overexpressing SyArgG and ArgH of Synechocystis 6803 (SyArgH). The specific activity of SyArgG was lower than that of other arginine biosynthesis enzymes and SyArgG was inhibited by arginine, especially among amino acids and organic acids. Both arginine biosynthesis enzyme-overexpressing strains grew faster than the wild-type Synechocystis 6803. Based on previous reports and our results, we suggest that SyArgG is the rate-limiting enzyme in the arginine biosynthesis pathway in cyanobacteria and that arginine biosynthesis enzymes are similarly regulated by arginine in this cyanobacterium. Our results contribute to elucidating the regulation of arginine biosynthesis during nitrogen metabolism.

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Section: Discussionsupporting

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Arginine inhibits the arginine biosynthesis rate-limiting enzyme and leads to the accumulation of intracellular aspartate in Synechocystis sp. PCC 6803

Katayama,

Osanai

2024

Plant Mol Biol

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Elucidating the Mechanisms of Acquired Palbociclib Resistance via Comprehensive Metabolomics Profiling

Yang,

Yue,

Wang

et al. 2025

CIMB

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Palbociclib is a cyclin-dependent kinase 4/6 inhibitor and a commonly used antitumor drug. Many cancers are susceptible to palbociclib resistance, however, the underlying metabolism mechanism and extent of resistance to palbociclib are unknown. In this study, LC-MS metabolomics was used to investigate the metabolite changes of colorectal cancer SW620 cells that were resistant to palbociclib. The study indicated that there were 76 metabolite expression differences between SW620 cells with palbociclib resistance and the parental SW620 cells involving amino acids, glutathione, ABC transporters, and so on. MetaboAnalyst 6.0 metabolic pathway analysis showed that arginine synthesis, β-alanine metabolism, and purine metabolism were disrupted. These results may provide potential clues to the metabolism mechanism of drug resistance in cancer cells that are resistant to palbociclib. Our study has the potential to contribute to the study of anti-palbociclib resistance.

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Arginine inhibition of the argininosuccinate lyases is conserved among three orders in cyanobacteria

Cited by 2 publications

References 44 publications

Arginine inhibits the arginine biosynthesis rate-limiting enzyme and leads to the accumulation of intracellular aspartate in Synechocystis sp. PCC 6803

Arginine inhibits the arginine biosynthesis rate-limiting enzyme and leads to the accumulation of intracellular aspartate in Synechocystis sp. PCC 6803

Elucidating the Mechanisms of Acquired Palbociclib Resistance via Comprehensive Metabolomics Profiling

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