The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
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 mllF corresponds to locus META1p4135 in Methylorubrum (Methylobacterium) extorquens strain AM1 and is part of the mll/mlu biosynthetic gene cluster (BGC) responsible for production of the lanthanide-binding metallophore methylolanthanin (MLL). (zytnick2022discoveryandcharacterization pages 3-5, zytnick2022discoveryandcharacterization pages 5-8)
Direct experimental work to date establishes the cluster-level role of mll (including mllF) in improving growth under poorly soluble lanthanide conditions and in increasing cellular lanthanide bioaccumulation, but does not provide a single-gene biochemical characterization of the mllF enzyme product. (zytnick2022discoveryandcharacterization pages 8-10, zytnick2022discoveryandcharacterization pages 10-12)
Based on domain/family evidence and comparison to the closest well-characterized functional analog AsbF (Pfam PF01261, a TIM-barrel dehydroshikimate dehydratase used in petrobactin biosynthesis), mllF is most plausibly a divergent AsbF-like metalloenzyme supplying an aromatic acid building block for methylolanthanin, but this remains an inference because the authors explicitly report weak matching of mllF to the PF01261 model. (pfleger2008structuralandfunctional pages 2-4, zytnick2022discoveryandcharacterization pages 10-12)
Lanthanides (Ln) are cofactors for certain periplasmic alcohol dehydrogenases (e.g., XoxF-type methanol dehydrogenases) in diverse bacteria, but the mechanisms enabling uptake and utilization under environmentally low Ln bioavailability are incompletely understood. (zytnick2022discoveryandcharacterization pages 1-3)
Bacteria often deploy metallophores (small-molecule chelators) plus transport and regulatory systems (e.g., TonB-dependent receptors, ABC transporters, and cell-surface signaling modules) to solubilize and import metals. (zytnick2022discoveryandcharacterization pages 1-3)
Zytnick et al. report methylolanthanin as the first known biological lanthanide chelator (lanthanophore), discovered via transcriptional response of M. extorquens AM1 to a poorly soluble lanthanide source (Nd2O3). (zytnick2022discoveryandcharacterization pages 1-3)
The mll/mlu BGC is located at META1p4129–META1p4138, and mllF is explicitly assigned to locus META1p4135 within this BGC. (zytnick2022discoveryandcharacterization pages 3-5, zytnick2022discoveryandcharacterization pages 5-8)
AsbF is a Mn2+-dependent 3-dehydroshikimate (3-DHS) dehydratase that converts 3-DHS → 3,4-dihydroxybenzoic acid (3,4-DHBA; protocatechuate), providing an aromatic chelating subunit for the siderophore petrobactin. (pfleger2008structuralandfunctional pages 2-4, pfleger2008structuralandfunctional pages 1-2)
AsbF is an (α/β)8 TIM-barrel metalloenzyme; the structural family is described as related to the “xylose isomerase TIM-barrel family” and is annotated in the AP endonuclease 2 TIM-barrel protein family context. (pfleger2008structuralandfunctional pages 2-4, pfleger2008structuralandfunctional pages 1-2)
Within the methylolanthanin study, META1p4135 is annotated as mllF and is part of the methylolanthanin BGC, matching the requested organism/context (M. extorquens AM1). (zytnick2022discoveryandcharacterization pages 3-5, zytnick2022discoveryandcharacterization pages 5-8)
The same study explicitly discusses mllF in relation to the Pfam model PF01261, which is consistent with the UniProt-provided domain cue (PF01261). (zytnick2022discoveryandcharacterization pages 10-12)
Therefore, the literature retrieved supports that the user’s target (UniProt C5B1I7; locus MexAM1_META1p4135/META1p4135) corresponds to mllF in the methylolanthanin (mll) BGC context, and not a different “mllF” from another organism. (zytnick2022discoveryandcharacterization pages 3-5)
Zytnick et al. report that genes META1p4132–4135 (mllA, mllBC, mllDE, mllF) are homologous to the petrobactin biosynthetic locus asbABCDEF, and that the broader locus resembles BGCs for NRPS-independent siderophore biosynthesis (e.g., rhodopetrobactin/petrobactin/roseobactin). (zytnick2022discoveryandcharacterization pages 3-5)
This comparative genomics context supports a role for mllF in biosynthesis of the lanthanophore methylolanthanin, rather than in downstream transport (which is typically carried by receptor/transport genes elsewhere in the locus). (zytnick2022discoveryandcharacterization pages 1-3)
Methylolanthanin’s structure contains two 4-hydroxybenzoate (4-HB) moieties, linked via homospermidine residues to a central citrate core. (zytnick2022discoveryandcharacterization pages 5-8)
This is a crucial clue: if mllF is functionally analogous to AsbF (which generates 3,4-DHBA), then mllF could (hypothetically) be involved in producing an aromatic acid precursor—potentially a hydroxybenzoate-related building block—used to assemble methylolanthanin’s 4-HB groups. However, the study does not directly assign that step to mllF. (zytnick2022discoveryandcharacterization pages 5-8, zytnick2022discoveryandcharacterization pages 10-12)
The mll locus is reported as highly induced under Nd2O3 (poorly soluble) compared with NdCl3 (soluble), with an average induction of approximately ~32-fold. (zytnick2022discoveryandcharacterization pages 3-5, zytnick2022discoveryandcharacterization pages 1-3)
This induction pattern supports a role in scavenging or solubilization of lanthanides when they are poorly bioavailable. (zytnick2022discoveryandcharacterization pages 1-3)
Zytnick et al. report that deletion of the mll cluster (ΔmxaFΔmll) results in reduced lanthanide bioaccumulation (noted as ~30% decrease in one discussion passage), while overexpression increases accumulation. (zytnick2022discoveryandcharacterization pages 10-12, zytnick2022discoveryandcharacterization pages 8-10)
Quantitatively, intracellular Nd (ICP-MS) showed:
- mll deletion decreased Nd bioaccumulation, notably by 1.8-fold in the NdCl3 condition
- mll overexpression increased Nd bioaccumulation by 3.5-fold on average
These are direct physiological readouts of the cluster’s function in lanthanide acquisition/handling. (zytnick2022discoveryandcharacterization pages 8-10)
Using UPLC-MS/MS and NMR, the authors identify methylolanthanin and establish its 4-HB-containing structure. (zytnick2022discoveryandcharacterization pages 5-8)
They further show by direct injection MS that methylolanthanin forms complexes with La(III), Nd(III), and Lu(III) (detected as [MLL-H+ + Ln3+]2+), supporting broad Ln-binding capability. (zytnick2022discoveryandcharacterization pages 8-10)
Overexpression of the mll cluster improved growth on poorly soluble Nd2O3, with a reported growth rate 0.026 hr−1, described as a nearly 50% increase relative to the ΔmxaF strain under Nd2O3 and closer to 0.037 hr−1 for ΔmxaF on NdCl3. (zytnick2022discoveryandcharacterization pages 8-10)
Addition of purified methylolanthanin (50 nM) increased growth yield (max OD) of both ΔmxaF and ΔmxaFΔmll cultures in NdCl3. (zytnick2022discoveryandcharacterization pages 8-10)
Important limitation: these experiments manipulate the entire mll cluster, so they do not isolate the specific contribution of mllF versus other biosynthetic genes. (zytnick2022discoveryandcharacterization pages 8-10, zytnick2022discoveryandcharacterization pages 3-5)
For comparative genomics detection of petrobactin-like BGCs, Zytnick et al. state that no asbF model was used because of a low bitscore between mllF and the expected Pfam model PF01261. (zytnick2022discoveryandcharacterization pages 10-12)
This implies that mllF is not confidently annotated by standard PF01261 HMM thresholds, but it is close enough to be considered in the same conceptual neighborhood (especially given the locus’ overall similarity to asb genes). (zytnick2022discoveryandcharacterization pages 3-5, zytnick2022discoveryandcharacterization pages 10-12)
AsbF catalyzes dehydration of 3-dehydroshikimate to 3,4-DHBA, and requires a divalent metal with Mn2+ preferred (Zn2+ inhibitory). (pfleger2008structuralandfunctional pages 2-4)
Reported kinetics (pH 7.5): Km ~290 µM, kcat ~80 min−1. (pfleger2008structuralandfunctional pages 2-4)
Structural and mechanistic features include a TIM-barrel fold, metal coordination in the active site, and an E1CB-like mechanism involving enolate stabilization by Mn2+. (pfleger2008structuralandfunctional pages 2-4, pfleger2008structuralandfunctional pages 4-5)
These details provide a concrete biochemical template for the kinds of reactions a PF01261-like enzyme can catalyze, and therefore what kinds of assays (e.g., UV at 290 nm, LC–MS for aromatic acid formation, metal dependence tests) would be appropriate to test mllF function. (pfleger2008structuralandfunctional pages 5-6, pfleger2008structuralandfunctional pages 2-2)
Best-supported hypothesis (not yet experimentally proven for mllF): mllF encodes a TIM-barrel metalloenzyme in the PF01261/AsbF-like functional space, contributing to production of an aromatic acid precursor used for methylolanthanin’s hydroxybenzoate moieties. (zytnick2022discoveryandcharacterization pages 5-8, pfleger2008structuralandfunctional pages 2-4)
Caveat: because methylolanthanin contains 4-hydroxybenzoate rather than 3,4-DHBA and because mllF’s match to PF01261 is weak, mllF may catalyze a non-canonical variant reaction relative to AsbF, or may have diverged substrate specificity/chemistry while retaining a related fold. (zytnick2022discoveryandcharacterization pages 5-8, zytnick2022discoveryandcharacterization pages 10-12)
No direct subcellular localization experiments for the mllF protein were found in the retrieved literature. (zytnick2022discoveryandcharacterization pages 10-12)
Given its placement in a small-molecule biosynthetic gene cluster (rather than a transporter/receptor gene), and by analogy to cytosolic steps in many NRPS-independent siderophore pathways, the most plausible localization for the mllF-encoded biosynthetic reaction is intracellular (cytosolic), with methylolanthanin subsequently functioning extracellularly/periplasmically in lanthanide acquisition (via transport systems encoded in/near the BGC). This remains an inference and should be validated experimentally. (zytnick2022discoveryandcharacterization pages 1-3, zytnick2022discoveryandcharacterization pages 8-10)
The primary body of evidence here comes from Zytnick et al.’s bioRxiv preprint (DOI: https://doi.org/10.1101/2022.01.19.476857), explicitly noted as posted Nov 10, 2023 in the retrieved text, describing methylolanthanin’s structure, lanthanide binding, the mll BGC organization, and phenotypes of deletion/overexpression. (zytnick2022discoveryandcharacterization pages 10-12, zytnick2022discoveryandcharacterization pages 5-8)
Valdés et al. (2024-11, Communications Biology; https://doi.org/10.1038/s42003-024-07258-3) studied LanM homologs and Ln preference in Hyphomicrobium, emphasizing the expanding toolkit of biological Ln-binding macromolecules and their potential relevance for sustainable Ln recovery; while this does not directly annotate mllF, it underscores increasing focus on Ln-binding strategies among methylotroph-adjacent taxa. (valdes2024anovelinsilico pages 1-2)
A 2024 PNAS article (“Identification and characterization of a small-molecule metallophore involved in lanthanide metabolism”, DOI https://doi.org/10.1073/pnas.2322096121) was flagged as unobtainable in the retrieval results, so its claims cannot be incorporated as evidence here. (retrieval log)
The methylolanthanin work frames M. extorquens AM1 as a candidate organism for selective bioaccumulation and recovery of lanthanides from waste streams (e.g., electronic waste, magnets), and demonstrates that manipulating the mll pathway can substantially alter intracellular Nd accumulation (up to 3.5-fold increase upon overexpression). (zytnick2022discoveryandcharacterization pages 8-10, zytnick2022discoveryandcharacterization pages 10-12)
These findings support a near-term application space: engineering of metallophore production pathways to improve biomining/bioleaching efficiency and selectivity, although scale-up and process-level validation are beyond the scope of the cited study. (zytnick2022discoveryandcharacterization pages 8-10)
Zytnick et al. argue that methylolanthanin’s narrow distribution and similarity to Fe-siderophore systems suggests the pathway may have entered Methylorubrum via horizontal gene transfer and subsequently evolved toward Ln chelation, though they emphasize that further study is needed to confirm this hypothesis. (zytnick2022discoveryandcharacterization pages 8-10)
They further propose an evolutionary rationale for methylolanthanin’s unusual 4-HB moiety (relative to typical bidentate catecholates), suggesting selection may balance Ln acquisition with avoidance of toxic Fe overaccumulation; they note Fe bioaccumulation was unaffected by mll overexpression in their system. (zytnick2022discoveryandcharacterization pages 10-12)
Key quantitative results relevant to the mll locus (including mllF) include:
- ~32-fold induction of the mll locus under Nd2O3 vs NdCl3 conditions (RNA-seq). (zytnick2022discoveryandcharacterization pages 3-5)
- Growth-rate changes under Nd2O3 and NdCl3 upon mll overexpression: 0.026 hr−1 (Nd2O3, ΔmxaF/pAZ1) and 0.037 hr−1 (NdCl3, ΔmxaF reference). (zytnick2022discoveryandcharacterization pages 8-10)
- Intracellular Nd accumulation changes by ICP-MS: 1.8-fold decrease upon mll deletion (NdCl3 condition) and 3.5-fold increase on average upon overexpression. (zytnick2022discoveryandcharacterization pages 8-10)
- Reference enzymology for PF01261 analog AsbF: Km ~290 µM and kcat ~80 min−1 (pH 7.5). (pfleger2008structuralandfunctional pages 2-4)
The following table distinguishes experimentally established facts from inference for mllF.
| Claim / annotation item | Evidence type | Key supporting details / quantitative values | Confidence | Primary citation(s) |
|---|---|---|---|---|
| mllF identity and membership in the methylolanthanin BGC | Direct experiment in M. extorquens AM1; comparative genomics | META1p4135 is explicitly annotated as mllF within the mll/mlu biosynthetic gene cluster spanning META1p4129–META1p4138; the cluster is described as homologous in part to the petrobactin asb locus, placing mllF in a metallophore-biosynthetic context. | High | (zytnick2022discoveryandcharacterization pages 3-5, zytnick2022discoveryandcharacterization pages 5-8) |
| mll locus is induced under poorly soluble lanthanide conditions | Direct experiment in M. extorquens AM1 (RNA-seq) | The entire mll locus was reported as highly upregulated, with an average of ~32-fold higher expression during growth with Nd2O3 versus NdCl3, consistent with a role in scavenging poorly bioavailable lanthanides. | High | (zytnick2022discoveryandcharacterization pages 3-5, zytnick2022discoveryandcharacterization pages 1-3) |
| Pathway role: methylolanthanin biosynthesis / lanthanophore system | Direct experiment in M. extorquens AM1; comparative genomics | The cluster was identified as producing methylolanthanin, the first reported biological lanthanide chelator; the BGC also includes predicted uptake/signaling functions such as a TonB-dependent outer membrane receptor, supporting a dedicated lanthanide acquisition pathway. | High | (zytnick2022discoveryandcharacterization pages 3-5, zytnick2022discoveryandcharacterization pages 1-3) |
| Methylolanthanin chemical structure | Direct experiment in M. extorquens AM1 | UPLC-MS/MS and NMR established methylolanthanin as a citrate-centered molecule linked to two 4-hydroxybenzoate (4-HB) moieties via homospermidine residues; this distinguishes it from rhodopetrobactin, which uses 3,4-DHBA. | High | (zytnick2022discoveryandcharacterization pages 5-8) |
| Methylolanthanin binds lanthanides | Direct experiment in M. extorquens AM1 | Direct-injection MS showed complexes with La(III), Nd(III), and Lu(III), observed as [MLL-H+ + Ln3+]2+ species with matching isotopic patterns, demonstrating binding across lanthanides of different ionic radii. | High | (zytnick2022discoveryandcharacterization pages 8-10) |
| Physiological effect of deleting/overexpressing the mll cluster | Direct experiment in M. extorquens AM1 | Overexpression (ΔmxaF/pAZ1) improved growth with poorly soluble Nd2O3 to 0.026 hr^-1, described as a nearly 50% increase over ΔmxaF under the same condition and closer to 0.037 hr^-1 observed for ΔmxaF with soluble NdCl3. Exogenous methylolanthanin (50 nM) significantly increased growth yield of both ΔmxaF and ΔmxaFΔmll cultures. | High | (zytnick2022discoveryandcharacterization pages 8-10) |
| Effect on intracellular neodymium accumulation | Direct experiment in M. extorquens AM1 | Δmll reduced Nd bioaccumulation with both lanthanide sources, notably by 1.8-fold in the NdCl3 condition, whereas overexpression of mll increased Nd bioaccumulation by 3.5-fold on average. | High | (zytnick2022discoveryandcharacterization pages 8-10) |
| Predicted enzymatic activity of mllF: divergent AsbF-like PF01261 enzyme | Comparative genomics; characterized homolog inference | The study grouped mllF with genes resembling the petrobactin asb biosynthetic locus, but specifically noted that no asbF model was used in genome mining because mllF had a low bitscore to Pfam PF01261, implying it is PF01261-related but divergent. This supports cautious inference rather than definitive assignment. | Medium | (zytnick2022discoveryandcharacterization pages 3-5, zytnick2022discoveryandcharacterization pages 10-12) |
| Reference reaction for the closest characterized homolog AsbF | Characterized homolog | AsbF is a Mn2+-dependent 3-dehydroshikimate dehydratase that converts 3-dehydroshikimate (3-DHS) to 3,4-dihydroxybenzoic acid (3,4-DHBA / protocatechuate), a precursor for petrobactin biosynthesis. | High | (pfleger2008structuralandfunctional pages 2-4, pfleger2008structuralandfunctional pages 1-2, pfleger2008structuralandfunctional pages 4-5) |
| Reference kinetics and structural family for AsbF | Characterized homolog | Reported AsbF parameters at pH 7.5: Km ~290 µM, kcat ~80 min^-1. Structurally, AsbF adopts an (α/β)8 TIM-barrel fold within the AP endonuclease 2 / xylose-isomerase-like family and uses a divalent metal, with Mn2+ preferred and Zn2+ inhibitory. | High | (pfleger2008structuralandfunctional pages 2-4, pfleger2008structuralandfunctional pages 1-2) |
| Most likely subcellular localization for mllF function | Inference from pathway chemistry and homolog class | Because methylolanthanin is a small-molecule biosynthetic product and mllF is not described as a membrane or secreted protein, the most plausible localization is intracellular (cytosolic) biosynthesis, with the lanthanophore subsequently functioning in extracellular/periplasm-associated metal acquisition. This localization has not been directly tested for mllF alone. | Low | (zytnick2022discoveryandcharacterization pages 1-3, zytnick2022discoveryandcharacterization pages 8-10) |
Table: This table summarizes the strongest available evidence for functional annotation of mllF/META1p4135 in Methylorubrum extorquens AM1, separating direct AM1 experiments from inference based on the characterized homolog AsbF. It is useful for distinguishing what is experimentally established from what remains a domain-based prediction.
A biosynthetic gene cluster map including mllF and the growth/bioaccumulation phenotypes associated with manipulating the mll cluster are shown in extracted figure regions. (zytnick2022discoveryandcharacterization media d423bf82, zytnick2022discoveryandcharacterization media 924bdd07)
Because mllF has not been individually characterized, the primary function (substrate specificity and reaction) remains unresolved. (zytnick2022discoveryandcharacterization pages 10-12)
High-value next steps, guided by AsbF assays, would include: heterologous expression/purification of mllF; testing for metal dependence (Mn2+ vs other divalent ions); LC–MS detection of candidate aromatic acid products (including 4-hydroxybenzoate-related chemistry); and genetic complementation within Δmll background to attribute specific steps to mllF. (pfleger2008structuralandfunctional pages 2-4, pfleger2008structuralandfunctional pages 2-2)
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 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.
(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.
(zytnick2022discoveryandcharacterization pages 10-12): 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.
(pfleger2008structuralandfunctional pages 2-4): Brian F. Pfleger, Youngchang Kim, Tyler D. Nusca, Natalia Maltseva, Jung Yeop Lee, Christopher M. Rath, Jamie B. Scaglione, Brian K. Janes, Erica C. Anderson, Nicholas H. Bergman, Philip C. Hanna, Andrzej Joachimiak, and David H. Sherman. Structural and functional analysis of asbf: origin of the stealth 3,4-dihydroxybenzoic acid subunit for petrobactin biosynthesis. Proceedings of the National Academy of Sciences, 105:17133-17138, Nov 2008. URL: https://doi.org/10.1073/pnas.0808118105, doi:10.1073/pnas.0808118105. This article has 84 citations and is from a highest quality peer-reviewed journal.
(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.
(pfleger2008structuralandfunctional pages 1-2): Brian F. Pfleger, Youngchang Kim, Tyler D. Nusca, Natalia Maltseva, Jung Yeop Lee, Christopher M. Rath, Jamie B. Scaglione, Brian K. Janes, Erica C. Anderson, Nicholas H. Bergman, Philip C. Hanna, Andrzej Joachimiak, and David H. Sherman. Structural and functional analysis of asbf: origin of the stealth 3,4-dihydroxybenzoic acid subunit for petrobactin biosynthesis. Proceedings of the National Academy of Sciences, 105:17133-17138, Nov 2008. URL: https://doi.org/10.1073/pnas.0808118105, doi:10.1073/pnas.0808118105. This article has 84 citations and is from a highest quality peer-reviewed journal.
(pfleger2008structuralandfunctional pages 4-5): Brian F. Pfleger, Youngchang Kim, Tyler D. Nusca, Natalia Maltseva, Jung Yeop Lee, Christopher M. Rath, Jamie B. Scaglione, Brian K. Janes, Erica C. Anderson, Nicholas H. Bergman, Philip C. Hanna, Andrzej Joachimiak, and David H. Sherman. Structural and functional analysis of asbf: origin of the stealth 3,4-dihydroxybenzoic acid subunit for petrobactin biosynthesis. Proceedings of the National Academy of Sciences, 105:17133-17138, Nov 2008. URL: https://doi.org/10.1073/pnas.0808118105, doi:10.1073/pnas.0808118105. This article has 84 citations and is from a highest quality peer-reviewed journal.
(pfleger2008structuralandfunctional pages 5-6): Brian F. Pfleger, Youngchang Kim, Tyler D. Nusca, Natalia Maltseva, Jung Yeop Lee, Christopher M. Rath, Jamie B. Scaglione, Brian K. Janes, Erica C. Anderson, Nicholas H. Bergman, Philip C. Hanna, Andrzej Joachimiak, and David H. Sherman. Structural and functional analysis of asbf: origin of the stealth 3,4-dihydroxybenzoic acid subunit for petrobactin biosynthesis. Proceedings of the National Academy of Sciences, 105:17133-17138, Nov 2008. URL: https://doi.org/10.1073/pnas.0808118105, doi:10.1073/pnas.0808118105. This article has 84 citations and is from a highest quality peer-reviewed journal.
(pfleger2008structuralandfunctional pages 2-2): Brian F. Pfleger, Youngchang Kim, Tyler D. Nusca, Natalia Maltseva, Jung Yeop Lee, Christopher M. Rath, Jamie B. Scaglione, Brian K. Janes, Erica C. Anderson, Nicholas H. Bergman, Philip C. Hanna, Andrzej Joachimiak, and David H. Sherman. Structural and functional analysis of asbf: origin of the stealth 3,4-dihydroxybenzoic acid subunit for petrobactin biosynthesis. Proceedings of the National Academy of Sciences, 105:17133-17138, Nov 2008. URL: https://doi.org/10.1073/pnas.0808118105, doi:10.1073/pnas.0808118105. This article has 84 citations and is from a highest quality peer-reviewed journal.
(zytnick2022discoveryandcharacterization media d423bf82): 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 media 924bdd07): 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.
(peek2017structurallydiversedehydroshikimate pages 9-12): James Peek, Joseph Roman, Graham R. Moran, and Dinesh Christendat. Structurally diverse dehydroshikimate dehydratase variants participate in microbial quinate catabolism. Molecular Microbiology, 103:39-54, Jan 2017. URL: https://doi.org/10.1111/mmi.13542, doi:10.1111/mmi.13542. This article has 25 citations and is from a domain leading peer-reviewed journal.