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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
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Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The gene symbol mllA in Methylorubrum extorquens AM1 (formerly Methylobacterium extorquens AM1) corresponds to locus META1p4132 (MexAM1_META1p4132) in the methylolanthanin (mll) biosynthetic gene cluster (BGC). This cluster produces methylolanthanin (MLL), a lanthanophore (lanthanide-binding metallophore) that improves lanthanide bioavailability and supports lanthanide-dependent methylotrophy and bioaccumulation. Evidence supports mllA’s role as an IucA/IucC-family NRPS-independent siderophore synthetase (NIS synthetase) component in MLL biosynthesis, but the specific catalytic step and substrate specificity of the mllA protein itself has not been directly biochemically reconstituted in the accessible sources; enzyme chemistry is therefore inferred from family mechanism plus cluster-level functional genetics and metabolite structure. (zytnick2022discoveryandcharacterization pages 3-5)
Gene symbol ambiguity check and mapping. In the lanthanophore study by Zytnick et al., the authors explicitly enumerate META1p4132–4135 as “mllA, mllBC, mllDE, and mllF”, establishing that META1p4132 is mllA in M. extorquens AM1. (zytnick2022discoveryandcharacterization pages 3-5)
Organism verification. The same work is performed in Methylobacterium/Methylorubrum extorquens AM1 and discusses the AM1 lanthanide uptake machinery (lut cluster) and the mll biosynthetic locus in this organism. (zytnick2022discoveryandcharacterization pages 1-3, zytnick2022discoveryandcharacterization pages 3-5)
Family/domain consistency. mllA is described as part of a BGC homologous to NRPS-independent siderophore systems (petrobactin/rhodopetrobactin/roseobactin-like) and is functionally interpreted as a siderophore synthetase component; mechanistic studies of IucA/IucC-family NIS synthetases provide a consistent biochemical framework (ATP-dependent carboxylate adenylation and amide formation) matching the user-provided UniProt family assignment. (zytnick2022discoveryandcharacterization pages 3-5, mydy2020thesiderophoresynthetase pages 7-10, gulick2024kineticanalysisof pages 1-2)
Metallophores are secreted small molecules that chelate metals to improve acquisition under low bioavailability. A lanthanophore is a metallophore specialized for lanthanides (Ln). In M. extorquens AM1, lanthanide-dependent methanol dehydrogenase systems are periplasmic, and lanthanide acquisition has been proposed to involve siderophore-like mechanisms (TonB-dependent uptake and ABC-type transport), motivating the search for lanthanide chelators. (zytnick2022discoveryandcharacterization pages 1-3, roszczenkojasinska2020geneproductsand pages 4-5)
Zytnick et al. report methylolanthanin (MLL) as the first characterized biological lanthanide chelator (lanthanophore) and show it forms lanthanide complexes detectable by mass spectrometry. (zytnick2022discoveryandcharacterization pages 1-3, zytnick2022discoveryandcharacterization pages 8-10)
NIS synthetases (including the IucA/IucC family) are ATP-dependent ligases that generate an amide bond between a carboxylate and an amine/hydroxamate via a two-step mechanism: (i) acyl-adenylate (acyl-AMP) formation with release of PPi, followed by (ii) nucleophilic attack by the amine/hydroxamate to displace AMP and form product. (gulick2024kineticanalysisof pages 1-2, mydy2020thesiderophoresynthetase pages 7-10)
Mechanistically, kinetic analyses support an ordered sequential substrate binding mechanism for IucA: ATP binds first, then citrate, then the hydroxamate donor. (mydy2020thesiderophoresynthetase pages 23-26, gulick2024kineticanalysisof pages 8-10)
Zytnick et al. identify a siderophore-like locus META1p4129–4138 and assign it as the mll (methylolanthanin) biosynthetic gene cluster, with associated uptake/regulatory elements. The cluster includes components consistent with coupling of metallophore biosynthesis to transport and transcriptional control, including a TonB-dependent outer membrane receptor plus cell-surface signaling (anti-sigma/sigma factor) features in the locus. (zytnick2022discoveryandcharacterization pages 3-5)
The locus architecture (including mllA/META1p4132) is shown in their gene-cluster schematic (Figure 2a). (zytnick2022discoveryandcharacterization media b0e60267)
MLL is structurally characterized as a citrate-containing molecule incorporating homospermidine-derived linkers and hydroxybenzoate moieties; MS/MS and NMR support incorporation of citrate and a para-hydroxybenzoate (4-HB) substitution pattern, with acetylated homospermidine features. (zytnick2022discoveryandcharacterization pages 5-8)
Given that (i) MLL incorporates citrate and amine-containing linkers and (ii) the mll locus is homologous to citrate-containing metallophore/siderophore BGCs, it is consistent that mllA functions as an ATP-dependent amide-forming enzyme in assembling citrate–amine linkages, as expected for an IucA/IucC-like NIS synthetase component. This is consistent with the IucA mechanistic model (citrate adenylation then nucleophilic attack by an amine/hydroxamate donor). (zytnick2022discoveryandcharacterization pages 3-5, mydy2020thesiderophoresynthetase pages 7-10, gulick2024kineticanalysisof pages 1-2)
Limitations: none of the accessible sources provide a purified mllA enzyme assay specifying its exact substrates or catalytic step; therefore, reaction and substrate specificity are inferred, not directly demonstrated for mllA. (zytnick2022discoveryandcharacterization pages 3-5, gulick2024kineticanalysisof pages 1-2)
In transcriptomics comparing growth with soluble vs poorly soluble lanthanide sources, Zytnick et al. report that the mll locus (META1p4129–4138) is highly induced (~32-fold) under Nd2O3 (poorly soluble) compared with NdCl3 (soluble), consistent with a role in mobilizing lanthanides when bioavailability is low. (zytnick2022discoveryandcharacterization pages 3-5)
The same low-bioavailability condition also shows increased expression of the lanthanide-dependent methanol dehydrogenase gene xoxF1 (5-fold), supporting the concept that lanthanide acquisition and lanthanide-dependent methylotrophy are coupled. (zytnick2022discoveryandcharacterization pages 3-5)
Lanthanide uptake in M. extorquens AM1 involves a dedicated lut (lanthanide utilization and transport) cluster proposed to function analogously to siderophore-mediated Fe(III) uptake, using TonB-dependent and ABC-type transport components. (roszczenkojasinska2020geneproductsand pages 4-5, roszczenkojasinska2019lanthanidetransportstorage pages 8-12)
Roszczenko-Jasińska et al. provide experimental evidence for this model: they report that a TonB–ABC transport system is required for lanthanide incorporation into the cytoplasm, that expression of the TonB receptor is repressed when lanthanides are in excess, and that lanthanides are stored as cytoplasmic inclusions resembling polyphosphate granules. (roszczenkojasinska2020geneproductsand pages 1-4, roszczenkojasinska2020geneproductsand pages 4-5)
Within this cell architecture:
- MLL biosynthesis (including mllA function) is most plausibly cytosolic (as a soluble biosynthetic enzyme), while
- MLL action is extracellular/periplasm-linked (chelation and delivery to uptake), and
- lanthanides ultimately can be stored intracellularly (cytoplasm) as phosphate-associated deposits/granules. (zytnick2022discoveryandcharacterization pages 1-3, roszczenkojasinska2020geneproductsand pages 4-5)
Zytnick et al. further note cluster components predicted for regulation/transport, including a DUF4142 (ferritin-like) protein predicted to be exported to the periplasm, supporting multi-compartment pathway organization even if mllA itself is not localized directly. (zytnick2022discoveryandcharacterization pages 3-5)
Zytnick et al. report multiple orthogonal lines of evidence that the mll cluster produces a functional lanthanophore:
- MLL detected in supernatants of strains with intact/overexpressed cluster and absent in deletion backgrounds, with a defined m/z consistent with the product family. (zytnick2022discoveryandcharacterization pages 5-8)
- MLL binds lanthanides, forming detectable complexes with La, Nd, and Lu. (zytnick2022discoveryandcharacterization pages 8-10)
- Exogenous MLL (50 nM) improves growth yield under lanthanide conditions. (zytnick2022discoveryandcharacterization pages 8-10)
- mll overexpression increases lanthanide bioaccumulation (~3.5-fold average) and rescues growth defects on poorly bioavailable Nd2O3. (zytnick2022discoveryandcharacterization pages 8-10)
- Deleting the cluster causes bioaccumulation defects, though the cluster is reported as not essential under some lab conditions, consistent with redundancy/alternative uptake routes. (zytnick2022discoveryandcharacterization pages 3-5, zytnick2022discoveryandcharacterization pages 10-12)
In Methylobacterium aquaticum strain 22A, Juma et al. show that an iucA/iucC-family-containing siderophore cluster (sbn) is involved in lanthanide handling and methylotrophy-related phenotypes:
- Wild-type spent medium solubilized ~24-fold more soluble La from La2O3 than spent medium from a siderophore mutant. (juma2022siderophoreforlanthanide pages 3-4)
- A siderophore biosynthesis mutant failed to grow on methanol unless supplemented with wild-type spent medium or citrate, supporting a causal connection between secreted chelators, lanthanide access, and methanol growth. (juma2022siderophoreforlanthanide pages 3-4)
These data reinforce that IucA/IucC-like NIS chemistry can be deployed in methylobacteria for lanthanide mobilization, supporting the inference for mllA as a biosynthetic component of a lanthanophore. (juma2022siderophoreforlanthanide pages 1-2, juma2022siderophoreforlanthanide pages 3-4)
Voutsinos et al. (BMC Biology; Feb 2024; https://doi.org/10.1186/s12915-024-01841-0) analyze 136 genomes from weathered granite/soil and report extensive secondary metabolism potential:
- ~1,900 biosynthetic gene clusters (BGCs) detected across genomes; 168 NRPS/PKS BGCs across 10 phyla. (voutsinos2024weatheredgranitesand pages 7-10)
- A metallophore-predictive TonB-dependent transporter co-occurred with 8 NRPS/PKS BGCs. (voutsinos2024weatheredgranitesand pages 7-10)
- The proportion of DNA encoding BGCs decreased from 0.53% (moderately weathered rock) to 0.34% (soil). (voutsinos2024weatheredgranitesand pages 7-10)
They argue that siderophore-like molecules may be required to solubilize lanthanides from minerals in situ and report co-occurrence of lanthanide methylotrophy genes with predicted metallophore systems in some genomes. (voutsinos2024weatheredgranitesand pages 1-2, voutsinos2024weatheredgranitesand pages 7-10)
Notably, they state they did not observe a system similar to the AM1 lanthanophore cluster in their reconstructed genomes, implying that lanthanide-chelation strategies may be diverse and not universal across lanthanide-methylotrophs in those environments. (voutsinos2024weatheredgranitesand pages 10-12, voutsinos2024weatheredgranitesand pages 7-10)
Gulick et al. (Methods in Enzymology; Jan 2024; https://doi.org/10.1016/bs.mie.2024.06.012) consolidate and extend mechanistic/kinetic frameworks for NIS synthetases, supporting more rigorous functional inference for IucA/IucC-like proteins such as mllA:
- NIS synthetases catalyze ATP-dependent amide formation through acyl-AMP intermediates; multiple carboxylates (often citrate) and amine donors are possible across the family. (gulick2024kineticanalysisof pages 1-2)
- For IucA, kinetic and structural analyses support an ordered binding mechanism: ATP first, then citrate, then hydroxamate donor. (gulick2024kineticanalysisof pages 8-10)
Good et al. (Environmental Science & Technology; Dec 2023; https://doi.org/10.1021/acs.est.3c06775) demonstrate a scalable, acid-free platform using M. extorquens AM1 to recover REEs from waste sources:
- Process demonstrated scalability up to 10 L with consistent yields, without harsh acids or high temperatures. (good2023scalableandconsolidated pages 1-2)
- REEs are stored intracellularly as polyphosphate granules, and deletion of exopolyphosphatase (ppx) improves accumulation, linking phosphate metabolism to REE handling. (good2023scalableandconsolidated pages 2-3)
- Overexpressing the lanthanophore pathway (mll) increased bioaccumulation >3-fold, reaching 80 mg Nd/g dry weight, 15 mg Pr/g, and 8 mg Dy/g under the tested conditions. (good2023scalableandconsolidated pages 6-7)
- Deleting ppx increased Nd bioaccumulation to 202 mg Nd/g dry weight (~5.5-fold), and engineering reduced granule deconstruction can increase Nd storage capacity >50-fold. (good2023scalableandconsolidated pages 6-7)
- With a 0.75 L bioreactor at OD ~20, they estimate 1.3–2.1 g Nd/L recovery (65–100% recovery in one run with 1% Nd swarf pulp, per their estimate). (good2023scalableandconsolidated pages 6-7)
These outcomes represent a direct application leveraging the lanthanide uptake/chelation biology that mllA supports as part of the lanthanophore pathway. (good2023scalableandconsolidated pages 6-7)
The following figure panel depicts the mll BGC including mllA (META1p4132) and neighboring transport/regulatory genes, supporting gene identity and pathway association. (zytnick2022discoveryandcharacterization media b0e60267)
| Item | Evidence summary | Primary source(s) with year and URL |
|---|---|---|
| Identity | Target protein is mllA in Methylorubrum extorquens AM1, corresponding to locus META1p4132 / MexAM1_META1p4132; it is part of the methylolanthanin (mll) biosynthetic gene cluster and is annotated as a siderophore synthetase component consistent with an IucA/IucC-like NRPS-independent siderophore synthetase. (zytnick2022discoveryandcharacterization pages 3-5) | Zytnick et al. 2022, bioRxiv, https://doi.org/10.1101/2022.01.19.476857 |
| Gene/locus mapping | Zytnick et al. explicitly list META1p4132-4135 as mllA, mllBC, mllDE, and mllF, establishing that META1p4132 maps to mllA in the mll locus. The same source places the cluster within META1p4129-4138. (zytnick2022discoveryandcharacterization pages 3-5) | Zytnick et al. 2022, bioRxiv, https://doi.org/10.1101/2022.01.19.476857 |
| Protein family/domains | Direct domain architecture for C5B1I4 is provided by UniProt in the user prompt, and the literature-supported family-level assignment is IucA/IucC-like / NIS synthetase. Mechanistic work on IucA/IucC-family enzymes supports interpreting mllA as an ATP-dependent amide-bond-forming carboxylate:amine ligase in siderophore/metallophore assembly. (mydy2020thesiderophoresynthetase pages 1-5, gulick2024kineticanalysisof pages 1-2) | Mydy et al. 2020, Biochemistry, https://doi.org/10.1021/acs.biochem.0c00250; Gulick et al. 2024, Methods in Enzymology, https://doi.org/10.1016/bs.mie.2024.06.012 |
| Reaction class | IucA/IucC-family NIS synthetases catalyze ATP-dependent amide formation between a carboxylate and an amine/hydroxamate via an acyl-adenylate intermediate, releasing PPi then AMP. For homologs such as mllA, this supports annotation as an adenylating amide-bond-forming siderophore/metallophore synthetase rather than a transporter or redox enzyme. (mydy2020thesiderophoresynthetase pages 7-10, gulick2024kineticanalysisof pages 1-2, mydy2020thesiderophoresynthetase pages 23-26) | Mydy et al. 2020, Biochemistry, https://doi.org/10.1021/acs.biochem.0c00250; Gulick et al. 2024, Methods in Enzymology, https://doi.org/10.1016/bs.mie.2024.06.012 |
| Likely substrates | The exact mllA substrates were not directly measured in the provided snippets. By homology to IucA/IucC-family enzymes and to the mll cluster’s similarity to rhodopetrobactin/petrobactin/roseobactin pathways, mllA likely uses ATP plus a carboxylate acceptor such as citrate and an amine-containing donor in methylolanthanin assembly; the cluster is proposed to use citrate and 3,4-dihydroxybenzoate-derived chelating features. Family-wide substrate ranges include citrate, α-ketoglutarate, succinate or derivatives as carboxylates and hydroxamate/amine donors derived from lysine/ornithine or decarboxylated amines. (zytnick2022discoveryandcharacterization pages 3-5, gulick2024kineticanalysisof pages 1-2) | Zytnick et al. 2022, bioRxiv, https://doi.org/10.1101/2022.01.19.476857; Gulick et al. 2024, Methods in Enzymology, https://doi.org/10.1016/bs.mie.2024.06.012 |
| Pathway role | mllA is a biosynthetic component of the methylolanthanin pathway, which produces a lanthanide-binding metallophore (lanthanophore). The mll locus is proposed to synthesize methylolanthanin, and pathway perturbation changes lanthanide bioaccumulation and growth under low-bioavailability lanthanide conditions. (zytnick2022discoveryandcharacterization pages 3-5, zytnick2022discoveryandcharacterization pages 1-3) | Zytnick et al. 2022, bioRxiv, https://doi.org/10.1101/2022.01.19.476857 |
| Cellular localization/compartment | mllA itself is a biosynthetic enzyme and is therefore most plausibly intracellular/cytosolic, but the provided snippets do not directly localize the protein. The broader lanthanide acquisition pathway spans extracellular chelation by methylolanthanin, outer-membrane uptake via TonB-dependent systems, periplasmic trafficking, and cytoplasmic storage as phosphate-containing deposits. A ferritin-like DUF4142 protein in the mll cluster is predicted to be exported to the periplasm, indicating compartmentalized pathway components. (zytnick2022discoveryandcharacterization pages 3-5, roszczenkojasinska2020geneproductsand pages 4-5, roszczenkojasinska2019lanthanidetransportstorage pages 8-12, zytnick2022discoveryandcharacterization pages 1-3) | Zytnick et al. 2022, bioRxiv, https://doi.org/10.1101/2022.01.19.476857; Roszczenko-Jasińska et al. 2020, Scientific Reports, https://doi.org/10.1038/s41598-020-69401-4 |
| Genomic context/neighbor genes | The mll biosynthetic region includes nearby uptake/regulatory genes META1p4129-4131 encoding a TonB-dependent outer-membrane receptor, anti-sigma factor, and sigma factor, followed by biosynthetic genes including mllA (META1p4132), mllBC, mllDE, mllF, mllG, mllH, and mllJ. This organization supports coupling of biosynthesis to export/import and transcriptional control. (zytnick2022discoveryandcharacterization pages 3-5, zytnick2022discoveryandcharacterization media b0e60267) | Zytnick et al. 2022, bioRxiv, https://doi.org/10.1101/2022.01.19.476857 |
| Regulation/induction conditions | The mll locus is induced when lanthanide bioavailability is poor: expression is ~32-fold higher with poorly soluble Nd2O3 than with soluble NdCl3. In the same low-solubility condition, xoxF1 is upregulated 5-fold, linking lanthanophore production to lanthanide-dependent methanol oxidation. More generally, lanthanide uptake genes in the lut system are repressed by excess lanthanides. (zytnick2022discoveryandcharacterization pages 3-5, roszczenkojasinska2020geneproductsand pages 4-5) | Zytnick et al. 2022, bioRxiv, https://doi.org/10.1101/2022.01.19.476857; Roszczenko-Jasińska et al. 2020, Scientific Reports, https://doi.org/10.1038/s41598-020-69401-4 |
| Key experimental evidence/phenotypes | Evidence for the pathway containing mllA is strong at the cluster/product level: overexpression of MLL biosynthetic genes increases growth and lanthanide bioaccumulation; deletion causes severe defects; purified methylolanthanin binds lanthanides; exogenous MLL rescues growth of a biosynthesis mutant. Analogous evidence from Methylobacterium aquaticum 22A shows that IucA/IucC-containing siderophore clusters can solubilize lanthanide oxide and are required for methanol growth in specific genetic backgrounds, supporting the plausibility of mllA as a lanthanide-mobilizing metallophore synthetase. (zytnick2022discoveryandcharacterization pages 3-5, juma2022siderophoreforlanthanide pages 1-2, juma2022siderophoreforlanthanide pages 3-4) | Zytnick et al. 2022, bioRxiv, https://doi.org/10.1101/2022.01.19.476857; Juma et al. 2022, Frontiers in Microbiology, https://doi.org/10.3389/fmicb.2022.921635 |
| Key quantitative stats | mll/locus response: ~32-fold higher expression under Nd2O3 vs NdCl3; xoxF1 upregulated 5-fold under low-solubility lanthanide conditions. IucA-family benchmark kinetics: for hvKP IucA with ahLys, apparent KM = 0.79 ± 0.02 mM, kcat = 51.2 ± 0.5 min⁻¹, kcat/KM = 1,100 M⁻¹ s⁻¹; wild-type IucA shows ~100-fold preference for ahLys over N6-acetyllysine and a ~4-fold activity decrease with tricarballylic acid relative to citrate. Ecological prevalence/statistics from weathered rock metagenomes: ~1,900 BGCs identified across 136 genomes; 168 NRPS/PKS BGCs; metallophore-predictive TonB transporters co-occurred with 8 NRPS/PKS BGCs; three Acidobacteria had co-localized XoxF3-plus-putative metallophore systems and three more had non-colocalized combinations; no system similar to the AM1 lanthanophore cluster was observed. (voutsinos2024weatheredgranitesand pages 7-10, mydy2020thesiderophoresynthetase pages 10-12, mydy2020thesiderophoresynthetase pages 23-26, zytnick2022discoveryandcharacterization pages 3-5) | Zytnick et al. 2022, bioRxiv, https://doi.org/10.1101/2022.01.19.476857; Mydy et al. 2020, Biochemistry, https://doi.org/10.1021/acs.biochem.0c00250; Voutsinos et al. 2024, BMC Biology, https://doi.org/10.1186/s12915-024-01841-0 |
| Current interpretation / confidence | mllA can be annotated with moderate-to-high confidence as an IucA/IucC-family NRPS-independent siderophore/metallophore synthetase component in methylolanthanin biosynthesis, but the exact reaction step and substrate specificity of the mllA protein itself have not been directly biochemically demonstrated in the provided evidence. Thus, pathway membership is experimentally supported, while enzyme-level chemistry remains inferred from family homology and related systems. (zytnick2022discoveryandcharacterization pages 3-5, mydy2020thesiderophoresynthetase pages 1-5, gulick2024kineticanalysisof pages 1-2) | Zytnick et al. 2022, bioRxiv, https://doi.org/10.1101/2022.01.19.476857; Mydy et al. 2020, Biochemistry, https://doi.org/10.1021/acs.biochem.0c00250; Gulick et al. 2024, Methods in Enzymology, https://doi.org/10.1016/bs.mie.2024.06.012 |
Table: This table summarizes the evidence-supported functional annotation of mllA (META1p4132; UniProt C5B1I4) in Methylorubrum extorquens AM1, integrating direct cluster-level evidence with mechanistic inference from IucA/IucC-family enzymes. It is useful for distinguishing experimentally supported conclusions from homology-based inferences.
References
(zytnick2022discoveryandcharacterization pages 3-5): Alexa M. Zytnick, Sophie M. Gutenthaler-Tietze, Allegra T. Aron, Zachary L. Reitz, Manh Tri Phi, Nathan M. Good, Daniel Petras, Lena J. Daumann, and N. Cecilia Martinez-Gomez. Discovery and characterization of the first known biological lanthanide chelator. bioRxiv, Jan 2022. URL: https://doi.org/10.1101/2022.01.19.476857, doi:10.1101/2022.01.19.476857. This article has 20 citations.
(zytnick2022discoveryandcharacterization pages 1-3): Alexa M. Zytnick, Sophie M. Gutenthaler-Tietze, Allegra T. Aron, Zachary L. Reitz, Manh Tri Phi, Nathan M. Good, Daniel Petras, Lena J. Daumann, and N. Cecilia Martinez-Gomez. Discovery and characterization of the first known biological lanthanide chelator. bioRxiv, Jan 2022. URL: https://doi.org/10.1101/2022.01.19.476857, doi:10.1101/2022.01.19.476857. This article has 20 citations.
(mydy2020thesiderophoresynthetase pages 7-10): Lisa S. Mydy, Daniel C. Bailey, Ketan D. Patel, Matthew R. Rice, and Andrew M. Gulick. The siderophore synthetase iuca of the aerobactin biosynthetic pathway uses an ordered mechanism. Biochemistry, 59:2143-2153, May 2020. URL: https://doi.org/10.1021/acs.biochem.0c00250, doi:10.1021/acs.biochem.0c00250. This article has 34 citations and is from a peer-reviewed journal.
(gulick2024kineticanalysisof pages 1-2): Andrew M. Gulick, Lisa S. Mydy, and Ketan D. Patel. Kinetic analysis of the three-substrate reaction mechanism of an nrps-independent siderophore (nis) synthetase. Methods in enzymology, 702:1-19, Jan 2024. URL: https://doi.org/10.1016/bs.mie.2024.06.012, doi:10.1016/bs.mie.2024.06.012. This article has 4 citations and is from a peer-reviewed journal.
(roszczenkojasinska2020geneproductsand pages 4-5): Paula Roszczenko-Jasińska, Huong N. Vu, Gabriel A. Subuyuj, Ralph Valentine Crisostomo, James Cai, Nicholas F. Lien, Erik J. Clippard, Elena M. Ayala, Richard T. Ngo, Fauna Yarza, Justin P. Wingett, Charumathi Raghuraman, Caitlin A. Hoeber, Norma C. Martinez-Gomez, and Elizabeth Skovran. Gene products and processes contributing to lanthanide homeostasis and methanol metabolism in methylorubrum extorquens am1. Scientific Reports, Jul 2020. URL: https://doi.org/10.1038/s41598-020-69401-4, doi:10.1038/s41598-020-69401-4. This article has 98 citations and is from a peer-reviewed journal.
(zytnick2022discoveryandcharacterization pages 8-10): Alexa M. Zytnick, Sophie M. Gutenthaler-Tietze, Allegra T. Aron, Zachary L. Reitz, Manh Tri Phi, Nathan M. Good, Daniel Petras, Lena J. Daumann, and N. Cecilia Martinez-Gomez. Discovery and characterization of the first known biological lanthanide chelator. bioRxiv, Jan 2022. URL: https://doi.org/10.1101/2022.01.19.476857, doi:10.1101/2022.01.19.476857. This article has 20 citations.
(mydy2020thesiderophoresynthetase pages 23-26): Lisa S. Mydy, Daniel C. Bailey, Ketan D. Patel, Matthew R. Rice, and Andrew M. Gulick. The siderophore synthetase iuca of the aerobactin biosynthetic pathway uses an ordered mechanism. Biochemistry, 59:2143-2153, May 2020. URL: https://doi.org/10.1021/acs.biochem.0c00250, doi:10.1021/acs.biochem.0c00250. This article has 34 citations and is from a peer-reviewed journal.
(gulick2024kineticanalysisof pages 8-10): Andrew M. Gulick, Lisa S. Mydy, and Ketan D. Patel. Kinetic analysis of the three-substrate reaction mechanism of an nrps-independent siderophore (nis) synthetase. Methods in enzymology, 702:1-19, Jan 2024. URL: https://doi.org/10.1016/bs.mie.2024.06.012, doi:10.1016/bs.mie.2024.06.012. This article has 4 citations and is from a peer-reviewed journal.
(zytnick2022discoveryandcharacterization media b0e60267): Alexa M. Zytnick, Sophie M. Gutenthaler-Tietze, Allegra T. Aron, Zachary L. Reitz, Manh Tri Phi, Nathan M. Good, Daniel Petras, Lena J. Daumann, and N. Cecilia Martinez-Gomez. Discovery and characterization of the first known biological lanthanide chelator. bioRxiv, Jan 2022. URL: https://doi.org/10.1101/2022.01.19.476857, doi:10.1101/2022.01.19.476857. This article has 20 citations.
(zytnick2022discoveryandcharacterization pages 5-8): Alexa M. Zytnick, Sophie M. Gutenthaler-Tietze, Allegra T. Aron, Zachary L. Reitz, Manh Tri Phi, Nathan M. Good, Daniel Petras, Lena J. Daumann, and N. Cecilia Martinez-Gomez. Discovery and characterization of the first known biological lanthanide chelator. bioRxiv, Jan 2022. URL: https://doi.org/10.1101/2022.01.19.476857, doi:10.1101/2022.01.19.476857. This article has 20 citations.
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(mydy2020thesiderophoresynthetase pages 10-12): Lisa S. Mydy, Daniel C. Bailey, Ketan D. Patel, Matthew R. Rice, and Andrew M. Gulick. The siderophore synthetase iuca of the aerobactin biosynthetic pathway uses an ordered mechanism. Biochemistry, 59:2143-2153, May 2020. URL: https://doi.org/10.1021/acs.biochem.0c00250, doi:10.1021/acs.biochem.0c00250. This article has 34 citations and is from a peer-reviewed journal.
(mydy2020thesiderophoresynthetase pages 1-5): Lisa S. Mydy, Daniel C. Bailey, Ketan D. Patel, Matthew R. Rice, and Andrew M. Gulick. The siderophore synthetase iuca of the aerobactin biosynthetic pathway uses an ordered mechanism. Biochemistry, 59:2143-2153, May 2020. URL: https://doi.org/10.1021/acs.biochem.0c00250, doi:10.1021/acs.biochem.0c00250. This article has 34 citations and is from a peer-reviewed journal.