The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Ironing out siderophore biosynthesis: a review of non-ribosomal peptide synthetase (NRPS)-independent siderophore synthetases
Abstract
Iron is required for microbial growth and proliferation. To survive in low-iron environments, some microorganisms secrete ferric iron chelators called siderophores. Siderophore biosynthesis occurs via two pathways: the non-ribosomal peptide synthetase (NRPS) pathway and the NRPS-independent siderophore (NIS) synthetase pathway. NIS enzymes function by adenylating a carboxylic acid substrate, typically citrate, or a derivative, followed by nucleophilic capture of an amine or alcohol and displacement of a citryl intermediate. In this review, we summarize recent advances in NIS biochemistry with a particular focus on structural biology and confirm the classification of NIS enzymes into Types A, A', B, and C based on substrate specificity. Based on a phylogenetic analysis, we also propose a new subclass of NIS enzymes, Type C', responsible for dimerization and macrocyclization of complex and substituted amine or amide intermediates. Finally, we describe the role of NIS enzymes in virulence of pathogenic microbes and discuss NIS inhibitors as potential anti-microbial agents.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The Phyre2 web portal for protein modeling, prediction and analysis
Kelley, L. A., Mezulis, S., Yates, C. M., Wass, M. N., & Sternberg, M. J. E. (2015) · Nature Protocols · doi:10.1038/nprot.2015.053 · Cited by 9,652
LXXIII.—Oxidation of tartaric acid in presence of iron
Fenton, H. J. H. (1894) · J. Chem. Soc., Trans. · doi:10.1039/ct8946500899 · Cited by 3,179
Chemistry and biology of siderophores
Hider, R. C., & Kong, X. (2010) · Natural Product Reports · doi:10.1039/b906679a · Cited by 1,722
The Haber–Weiss reaction and mechanisms of toxicity
Kehrer, J. P. (2000) · Toxicology · doi:10.1016/s0300-483x(00)00231-6 · Cited by 1,418
Goetz, D. H., Holmes, M. A., Borregaard, N., Bluhm, M. E., Raymond, K. N., & Strong, R. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00708-6 · Cited by 1,355
Vandenesch, F., Lina, G., & Henry, T. (2012) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00012 · Cited by 405
Fungal siderophore metabolism with a focus on Aspergillus fumigatus
Haas, H. (2014) · Nat. Prod. Rep. · doi:10.1039/c4np00071d · Cited by 324
Russo, T. A., Olson, R., MacDonald, U., Beanan, J., & Davidson, B. A. (2015) · Infection and Immunity · doi:10.1128/iai.00430-15 · Cited by 305 · cited 1×
“Because K. pneumoniae secretes yersiniabactin, salmochelin, and enterobactin, Russo et al. (2015) created gene knockout strains for each siderophore (DentB was deficient in enterobactin and salmochelin, Dirp2 was deficient in yersiniabactin and DentBirp2 was deficient for yersiniabactin,…”
BackgroundMicrobial siderophore-mediated transport.
Winkelmann, G. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300691 · Cited by 301 · cited 1×
“A similar mechanism is employed by Gram-positive bacteria but without the OMT and periplasmic TonB proteins (Winkelmann 2002).”
MethodDale, S. E., Doherty-Kirby, A., Lajoie, G., & Heinrichs, D. E. (2004) · Infection and Immunity · doi:10.1128/iai.72.1.29-37.2004 · Cited by 232
Cited by
Bacterial siderophores in community and host interactions
Kramer, J., Özkaya, Ö., & Kümmerli, R. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-019-0284-4 · Cited by 998
Oleńska, E., Małek, W., Wójcik, M., Swiecicka, I., Thijs, S., & Vangronsveld, J. (2020) · Science of The Total Environment · doi:10.1016/j.scitotenv.2020.140682 · Cited by 555
Garber, A. I., Nealson, K. H., Okamoto, A., McAllister, S. M., Chan, C. S., Barco, R. A., & Merino, N. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00037 · Cited by 437
Biocontrol of Postharvest Fruit Fungal Diseases by Bacterial Antagonists: A Review
Carmona-Hernandez, S., Reyes-Pérez, J., Chiquito-Contreras, R., Rincon-Enriquez, G., Cerdan-Cabrera, C., & Hernandez-Montiel, L. (2019) · Agronomy · doi:10.3390/agronomy9030121 · Cited by 282
Expanding the Substrate Selectivity of the Fimsbactin Biosynthetic Adenylation Domain, FbsH
Ahmed, S. F., Balutowski, A., Yang, J., Wencewicz, T. A., & Gulick, A. M. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.4c00512 · Cited by 8
Metadata
- Authors
- Carroll, C. S., & Moore, M. M.
- Venue
- Critical Reviews in Biochemistry and Molecular Biology
- Publisher
- Informa UK Limited
- Published
- 2018-06-04
- Volume
- 53
- Issue
- 4
- Pages
- 356-381
- ISSN
- 0045-6411 (ISSN-L)
- 1040-9238
- 1549-7798
- OpenAlex
- W2806179485
- Cited by
- 168
- References
- 19
- FWCI
- 2.65
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Ironing out siderophore biosynthesis: a review of non-ribosomal peptide synthetase (NRPS)-independent siderophore synthetases. https://app.cochat.ai/papers/10.1080/10409238.2018.1476449
- The paper
- Carroll, C. S., & Moore, M. M. (2018). Ironing out siderophore biosynthesis: a review of non-ribosomal peptide synthetase (NRPS)-independent siderophore synthetases. Critical Reviews in Biochemistry and Molecular Biology. https://doi.org/10.1080/10409238.2018.1476449
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.