ArticleFrontiers in plant science2020
The Neighboring Subunit Is Engaged to Stabilize the Substrate in the Active Site of Plant Arginases.
Article in Frontiers in plant science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Polyamine-Related Gene Families Identification and Regulatory Effects on Early Somatic Embryogenesis via Modulating Gene Expressions and Hormone Levels inPlants (Basel, Switzerland) · 2026Article
- Polyamines: pleiotropic molecules regulating plant development and enhancing crop yield and quality.Plant biotechnology journal · 2024Review
- Characterization of a novel 4-guanidinobutyrase from Candida parapsilosis.FEMS yeast research · 2024Article
- Structural analysis and molecular substrate recognition properties ofFrontiers in plant science · 2023Article
- Discovery of a NiNature · 2022Article
- Crystal Structure ofInternational journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Arginine acts as a precursor of polyamines in plants in two known pathways, agmatine and ornithine routes. It is decarboxylated to agmatine by arginine decarboxylase, and then transformed to putrescine by the consecutive action of agmatine iminohydrolase and N-carbamoylputrescine amidohydrolase. Alternatively, it can be hydrolyzed to ornithine by arginase and then decarboxylated by ornithine decarboxylase to putrescine. Some plants lack a functional ornithine pathway, but all have one or two arginases that can have dual cellular localization, in mitochondria and plastids. It was recently shown that arginases from
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