ArticleThe Journal of biological chemistry2020
Crystal structures and biochemical analyses of the bacterial arginine dihydrolase ArgZ suggests a "bond rotation" catalytic mechanism.
Article in The Journal of biological chemistry, 2020. 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.
- The ornithine-arginine cycle supported a toxic, metalimnic Planktothrix rubescens bloom.Harmful algae · 2026Article
- Molecular dynamics simulation-driven focused virtual screening and experimental validation of Fisetin as an inhibitor of Helicobacter pylori HtrA protease.Molecular diversity · 2025Article
- Structural insights into the enzymatic breakdown of azomycin-derived antibiotics by 2-nitroimdazole hydrolase (NnhA).Communications biology · 2024Article
- Structure and function of the pseudouridine 5'-monophosphate glycosylase PUMY fromRNA biology · 2024Article
- Functional annotation of uncharacterized proteins from Fusobacterium nucleatum: identification of virulence factors.Genomics & informatics · 2023Article
- Molecular Relationships in Biofilm Formation and the Biosynthesis of Exoproducts in Pseudoalteromonas spp.Marine biotechnology (New York, N.Y.) · 2022Review
- Structural and mutational analyses of the bifunctional arginine dihydrolase and ornithine cyclodeaminase AgrE from the cyanobacteriumThe Journal of biological chemistry · 2020Article
- Arginine catabolism enzyme AgrE/ArgZ likely involves a cyanobacterial specific factor.The Journal of biological chemistry · 2020Article
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6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
A recently discovered ornithine-ammonia cycle (OAC) serves as a conduit in the nitrogen storage and remobilization machinery in cyanobacteria. The OAC involves an arginine catabolic reaction catalyzed by the arginine dihydrolase ArgZ whose catalytic mechanism is unknown. Here we determined the crystal structures at 1.2-3.0 Å of unliganded ArgZ from the cyanobacterium
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