ArticleNature communications2016
A distinct holoenzyme organization for two-subunit pyruvate carboxylase.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
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- Development and Application of a High-Throughput Method for the Purification and Analysis of Surface Carbohydrates fromBiology · 2024Article
- Sample optimizations to enable the structure determination of biotin-dependent carboxylases.Methods in enzymology · 2024Article
- The opportunistic pathogen Pseudomonas aeruginosa exploits bacterial biotin synthesis pathway to benefit its infectivity.PLoS pathogens · 2023Article
- Article
- Crystal structure of a thermophilic fungal cyanase and its implications on the catalytic mechanism for bioremediation.Scientific reports · 2021Article
- Kinetic, Structural, and Mutational Analysis of Acyl-CoA Carboxylase FromFrontiers in molecular biosciences · 2020Article
- Role of the malic enzyme in metabolism of the halotolerant methanotroph Methylotuvimicrobium alcaliphilum 20Z.PloS one · 2019Article
- Structural and functional studies of pyruvate carboxylase regulation by cyclic di-AMP in lactic acid bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Pyruvate carboxylase (PC) has important roles in metabolism and is crucial for virulence for some pathogenic bacteria. PC contains biotin carboxylase (BC), carboxyltransferase (CT) and biotin carboxyl carrier protein (BCCP) components. It is a single-chain enzyme in eukaryotes and most bacteria, and functions as a 500 kD homo-tetramer. In contrast, PC is a two-subunit enzyme in a collection of Gram-negative bacteria, with the α subunit containing the BC and the β subunit the CT and BCCP domains, and it is believed that the holoenzyme has α
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Registered trials
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