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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.

Research Report: Functional Annotation of pqqE (UniProt P71517) in Methylorubrum extorquens AM1 (ATCC 14718; formerly Methylobacterium extorquens)

Executive summary

The target protein PqqE (gene pqqE, UniProt P71517) from Methylorubrum extorquens strain AM1 is a radical S-adenosyl-L-methionine (radical SAM) enzyme (SPASM subclass) that catalyzes the first committed chemical step in pyrroloquinoline quinone (PQQ) biosynthesis: installation of a C–C bond (crosslink) between the side chains of a conserved glutamate and tyrosine on the ribosomally produced precursor peptide PqqA, in a reaction that requires the peptide chaperone PqqD. (yao2026radicalenzymaticpeptide pages 6-7, martins2019atwocomponentprotease pages 2-3, kandy2025aromaticsidechaincrosslinking pages 4-6)

PQQ is a redox cofactor used by periplasmic dehydrogenases in methylotroph physiology; in M. extorquens AM1, genomic analyses explicitly connect pqq genes with methanol oxidation modules, consistent with the organism’s reliance on PQQ-dependent alcohol/methanol dehydrogenases. (chistoserdova2003methylotrophyinmethylobacterium pages 2-3, toyama2016pyrroloquinolinequinone(pqq) pages 11-13)

Recent applied research (2023–2024) leverages the pqq pathway in (i) industrial/bioprocess production of PQQ (where pqqE transcriptional upregulation is associated with improved titers) and (ii) using pqq gene clusters as functional genomic markers in phosphate-solubilizing bacteria due to PQQ-driven glucose oxidation and organic acid production. (ren2023adaptiveevolutionarystrategy pages 7-10, chen2024genomebasedidentificationof pages 7-9)

Target verification (mandatory identity checks)

1) Gene symbol ↔ protein function match. In M. extorquens AM1, PqqE is repeatedly described as the radical SAM enzyme responsible for the initial Glu–Tyr C–C crosslinking on PqqA during PQQ biosynthesis. (martins2019atwocomponentprotease pages 2-3, kandy2025aromaticsidechaincrosslinking pages 4-6)

2) Organism match. Multiple retrieved sources explicitly address PqqE in Methylorubrum/Methylobacterium extorquens AM1, including AM1-specific gene cluster/sequence characterization and pathway reconstruction. (martins2019atwocomponentprotease pages 10-11, ochsner2015methylobacteriumextorquensmethylotrophy pages 9-10)

3) Family/domain consistency. PqqE is described as a SPASM-domain radical SAM enzyme that binds the canonical radical SAM [4Fe–4S] cluster and additional auxiliary Fe–S clusters. (yao2026radicalenzymaticpeptide pages 6-7)

Ambiguity assessment. The symbol pqqE is used across bacteria to denote the same functional role (PQQ biosynthetic radical SAM enzyme). Within the retrieved materials, no evidence suggested a conflicting “pqqE” referring to an unrelated function; therefore the literature used aligns with UniProt P71517’s annotation context. (yao2026radicalenzymaticpeptide pages 6-7, martins2019atwocomponentprotease pages 10-11)

1. Key concepts and definitions (current understanding)

1.1. PQQ and the pqq pathway

Pyrroloquinoline quinone (PQQ) is a small redox-active cofactor used by multiple bacterial dehydrogenases. Genomic overview of M. extorquens AM1 treats PQQ biosynthesis as a distinct metabolic module because PQQ is a cofactor for dehydrogenases important to methylotrophy. (chistoserdova2003methylotrophyinmethylobacterium pages 5-6)

A pathway-centric framing in recent genomics literature describes PQQ as deriving from the PqqA peptide through a conserved set of enzymes including PqqE (radical SAM), PqqD (chaperone), PqqB (hydroxylase), and PqqC (multi-electron oxidase), with PqqF/G as an alternative/associated peptide processing route. (chen2024genomebasedidentificationof pages 7-9)

1.2. Radical SAM enzymes and the SPASM subclass

Radical SAM enzymes use a [4Fe–4S] cluster to reductively cleave S-adenosyl-L-methionine (SAM) to generate a highly reactive 5′-deoxyadenosyl radical (5′-dAdo•) or equivalent species that initiates substrate radical chemistry. In the PQQ pathway, PqqE is characterized as a SPASM-domain radical SAM enzyme that uses this chemistry to create a C–C crosslink in a peptide substrate. (yao2026radicalenzymaticpeptide pages 6-7)

The SPASM domain is a C-terminal auxiliary domain present in many peptide-modifying radical SAM enzymes, often binding additional Fe–S clusters implicated in substrate binding, electron transfer, or control of reactivity. PqqE contains two auxiliary Fe–S clusters in addition to the radical SAM cluster. (yao2026radicalenzymaticpeptide pages 6-7)

2. Primary function and catalytic reaction of PqqE

2.1. Biological role: initiating PQQ biosynthesis by PqqA crosslinking

PqqE catalyzes formation of the initial carbon–carbon bond between the conserved glutamate and tyrosine residues within the PqqA peptide, producing a crosslinked PqqA intermediate (often denoted PqqA). This step is described as occurring with the help of the peptide chaperone PqqD*. (martins2019atwocomponentprotease pages 2-3, martins2019atwocomponentprotease pages 1-2)

A broader RiPP crosslinking review similarly describes PqqE as the radical SAM enzyme that initiates PQQ biosynthesis by installing the Glu–Tyr C–C crosslink on PqqA in a PqqD-dependent reaction. (kandy2025aromaticsidechaincrosslinking pages 4-6)

2.2. Substrates and products (as supported by retrieved evidence)

Macromolecular substrate: the ribosomally produced peptide PqqA, containing conserved Glu and Tyr residues that become part of the PQQ backbone. (toyama2016pyrroloquinolinequinone(pqq) pages 11-13, martins2019atwocomponentprotease pages 1-2)

Cofactor substrate: SAM, which is cleaved by PqqE to generate 5′-deoxyadenosyl species used for H-abstraction chemistry. (yao2026radicalenzymaticpeptide pages 6-7, toyama2016pyrroloquinolinequinone(pqq) pages 11-13)

Product (enzyme step): a crosslinked PqqA species (PqqA*), representing an early, crosslinked di-amino-acid precursor that must be released/processed for subsequent enzymatic steps. (martins2019atwocomponentprotease pages 2-3, martins2019atwocomponentprotease pages 1-2)

Evidence limitation: the retrieved excerpts describe the PqqE reaction primarily at the level of peptide crosslinking; they do not provide a complete balanced small-molecule reaction equation for EC 1.21.98.4 (e.g., explicit stoichiometry of SAM-derived products besides 5′-dAdo formation). (yao2026radicalenzymaticpeptide pages 6-7, martins2019atwocomponentprotease pages 2-3)

3. Mechanism and cofactors: current evidence-based model

3.1. Hydrogen abstraction and regioselective coupling

Mechanistic synthesis in an authoritative review (based on experiments in the AM1 system) describes the following steps:
1) PqqE reductively cleaves SAM to generate a 5′-deoxyadenosyl species (5′-dAdo). (yao2026radicalenzymaticpeptide pages 6-7)
2) Isotope labeling with β-deuterated glutamate in PqqA shows a kinetic isotope effect and deuterium incorporation into 5′-dAdo, supporting β-H abstraction from glutamate by the 5′-dAdo radical and formation of a peptide-centered radical. (yao2026radicalenzymaticpeptide pages 6-7)
3) The resulting radical couples regioselectively to the ortho position of a tyrosine ring, forming the crosslink that constitutes the PQQ core scaffold. (yao2026radicalenzymaticpeptide pages 6-7)

3.2. Fe–S cluster architecture (SPASM auxiliary clusters)

PqqE contains the canonical radical SAM cluster and two auxiliary Fe–S clusters (AuxI and AuxII) in its C-terminal SPASM domain. Crystallographic interpretation summarized in the same review indicates:
- AuxII coordinates a canonical [4Fe–4S] cluster using three cysteines and Asp319.
- AuxI appeared as a [2Fe–2S] cluster in the crystal structure context.
Spectroscopic (EPR) evidence is described as enabling assignment of signals to the radical SAM cluster and the auxiliary clusters and indicating that access to some redox states requires low-potential reductants. (yao2026radicalenzymaticpeptide pages 6-7)

3.3. Protein–protein interactions and substrate presentation

PqqE operates in a multicomponent context with PqqD as a peptide chaperone that interacts with PqqA and PqqE and supports productive PqqA modification. (martins2019atwocomponentprotease pages 2-3, toyama2016pyrroloquinolinequinone(pqq) pages 11-13)

4. Pathway placement, gene context, and cellular localization

4.1. Genomic organization in M. extorquens AM1

Genome-based analyses indicate PQQ biosynthesis genes can occur in multiple loci/modules in AM1, with pqqABC/DE in a methylotrophy island and pqqFG in a separate cluster in at least one genomic overview. (chistoserdova2003methylotrophyinmethylobacterium pages 5-6)

A later AM1-focused study figure description maps a local neighborhood including (order shown in that excerpt) pqqE, pqqC/D, pqqB, pqqA, pqqF, pqqG, and additional pqqA annotations in the region. (martins2019atwocomponentprotease pages 14-16)

4.2. Downstream processing: proteolysis and release of the crosslinked intermediate

A major gap historically was identification of the protease/peptidase steps needed to excise the crosslinked di-amino-acid precursor. In M. extorquens, Martins et al. characterize a two-component protease (PqqF/PqqG) and hypothesize it initially cleaves between the PqqE/PqqD-generated crosslinked form of PqqA, with other proteases completing release of a substrate for PqqB. (martins2019atwocomponentprotease pages 1-2)

4.3. Cellular localization (evidence and inference)

Direct subcellular localization experiments for PqqE in AM1 were not found in the retrieved text excerpts. However:
- The PqqE substrate is a ribosomally produced peptide (PqqA) and PqqE is a cytosolic radical SAM enzyme by biochemical class, consistent with activity in the cytosol.
- Mature PQQ accumulates in the periplasmic space in M. extorquens, consistent with downstream use by periplasmic dehydrogenases and/or export/trafficking after synthesis. (martins2019atwocomponentprotease pages 1-2)
Thus, localization is best described as: PqqE likely acts in the cytosol on PqqA prior to downstream processing and subsequent periplasmic accumulation/use of PQQ, with the caveat that explicit imaging/fractionation data were not retrieved here. (martins2019atwocomponentprotease pages 1-2, toyama2016pyrroloquinolinequinone(pqq) pages 11-13)

5. Recent developments (prioritizing 2023–2024)

5.1. 2023: strain/process engineering for high-titer PQQ production (bioprocess relevance to pqqE)

Ren et al. (published Jan 2023, Biotechnology for Biofuels and Bioproducts, URL: https://doi.org/10.1186/s13068-023-02261-y) developed a high-titer PQQ-producing methylotroph (Hyphomicrobium denitrificans FJNU-A26) through ARTP mutagenesis + adaptive laboratory evolution + fermentation strategy optimization. (ren2023adaptiveevolutionarystrategy pages 1-2)

Key quantitative outcomes (industrial relevance):
- Fed-batch (5-L) achieved 1.52 g/L PQQ in 144 h, with 40.3 mg PQQ/g DCW and ~10.5 mg/L·h productivity; biomass reached 37.7 g/L. (ren2023adaptiveevolutionarystrategy pages 10-11)
- Growth/production kinetics included μx ~0.169 h−1 under two-stage pH control and maximum μp 5.37×10−4 h−1 (at 88 h). (ren2023adaptiveevolutionarystrategy pages 10-11)

Critically for pqqE relevance, transcript analysis showed that pqqE expression from pqqABCDE increased most strongly, reaching approximately ~6× higher than wild type at later times in the mutant background, supporting the view that pqqE can be rate-influencing or at least highly responsive in high-production states. (ren2023adaptiveevolutionarystrategy pages 7-10)

5.2. 2024: pqq gene clusters as functional markers (genome-based implementations)

Chen et al. (published Jul 2024, AMB Express, URL: https://doi.org/10.1186/s13568-024-01745-w) analyzed 76 phosphate-solubilizing bacterial isolates and concluded that pqq gene clusters—particularly pqqC—are useful genomic markers for phosphate-solubilization capacity, explicitly describing the biosynthetic steps and noting PqqE as the radical SAM enzyme in the pathway. (chen2024genomebasedidentificationof pages 7-9, chen2024genomebasedidentificationof pages 1-2)

The work provides strain-level quantitative phosphate solubilization values spanning low to high solubilizers (e.g., 159.48 µg/mL P release for one Bacillus megaterium isolate in their dataset) and gives examples where complete pqq clusters associate with higher P release and lower pH (e.g., 92.03 µg/mL P release at pH 5.00 for Burkholderia cepacia 51-Y1415). (chen2024genomebasedidentificationof pages 3-5, chen2024genomebasedidentificationof pages 2-3)

It also reports correlation statistics that connect pqq genes to biochemical outputs linked to P solubilization (2-keto-D-gluconic acid and P release). For example, Table-level correlations include P release vs pqqA = 0.946 and P release vs pqqC = 0.940, and extremely strong correlations between 2-keto-D-gluconic acid and pqqA–pqqE (0.988–0.995) with significance indicated (P < 0.05, P** < 0.01). (chen2024genomebasedidentificationof pages 7-9, chen2024genomebasedidentificationof pages 5-7)

6. Current applications and real-world implementations

1) Biomanufacturing of PQQ: Adaptive evolution and fermentation control strategies can yield gram-per-liter titers of PQQ in methylotrophs, and gene expression analyses implicate increased transcription of pqq pathway genes including pqqE in improved production phenotypes. (ren2023adaptiveevolutionarystrategy pages 7-10, ren2023adaptiveevolutionarystrategy pages 10-11)

2) Agriculture/environmental microbiology (phosphate solubilization): pqq genes are used as genomic predictors of PQQ-dependent glucose oxidation leading to gluconic/2-ketogluconic acid formation and phosphate solubilization, with reported quantitative P release and strong correlations between pqq gene metrics and solubilization-related outputs. (chen2024genomebasedidentificationof pages 7-9, chen2024genomebasedidentificationof pages 2-3)

3) Methylotrophy and lanthanide-linked alcohol oxidation ecosystems: Although not directly measuring PqqE, M. extorquens AM1 genomic context links pqq loci with methanol oxidation systems, consistent with PQQ’s essential cofactor role for periplasmic dehydrogenases in methylotrophic growth. (chistoserdova2003methylotrophyinmethylobacterium pages 2-3, chistoserdova2003methylotrophyinmethylobacterium pages 5-6)

7. Expert opinions and analysis (from authoritative sources)

• A high-authority mechanistic review synthesizes multiple lines of evidence (isotope labeling, crystallography, EPR) to position PqqE as a SPASM-domain radical SAM enzyme whose auxiliary clusters are integral to its redox behavior and peptide-crosslinking chemistry, highlighting the need for strong reductants to access relevant redox states. (yao2026radicalenzymaticpeptide pages 6-7)

• A leading enzyme/pathway study in M. extorquens emphasizes that a “full description” of the PQQ biosynthetic pathway required identifying proteolytic processing steps beyond PqqE/PqqD chemistry, and proposes a biologically plausible division of labor where PqqE/PqqD make the crosslink and PqqF/PqqG initiate cleavage to release a substrate for downstream enzymes. (martins2019atwocomponentprotease pages 1-2)

8. Summary of key evidence sources (with URLs)

The following table summarizes the evidence extracted in this report, including organism match, mechanism, gene context, and application statistics:

Table: This table compiles the most relevant evidence-supported sources on PqqE in Methylorubrum extorquens AM1 and the broader PQQ biosynthetic pathway. It highlights identity verification, mechanism, gene organization, physiological context, and recent application-oriented studies with quantitative results where available.

9. Knowledge gaps and confidence assessment (specific to AM1 PqqE / UniProt P71517)

• High confidence: PqqE’s primary biochemical function in AM1 (PqqD-dependent radical SAM Glu–Tyr C–C crosslinking on PqqA) and its placement as the first committed step in PQQ biosynthesis. (yao2026radicalenzymaticpeptide pages 6-7, martins2019atwocomponentprotease pages 2-3)
• Moderate confidence (supported but not exhaustively detailed in retrieved excerpts): specific auxiliary cluster composition in AM1 PqqE and its mechanistic roles beyond general cluster presence/assignment. (yao2026radicalenzymaticpeptide pages 6-7)
• Lower confidence / not directly evidenced here: direct subcellular localization of PqqE by fractionation/microscopy in AM1; current localization statements are inferred from enzyme class (cytosolic radical SAM acting on ribosomal peptide) and from explicit mention that mature PQQ accumulates in the periplasm. (martins2019atwocomponentprotease pages 1-2)

References (retrieved in-tool; include publication dates and URLs)

• Chistoserdova L. et al. May 2003. Journal of Bacteriology. “Methylotrophy in Methylobacterium extorquens AM1 from a Genomic Point of View.” https://doi.org/10.1128/jb.185.10.2980-2987.2003 (chistoserdova2003methylotrophyinmethylobacterium pages 2-3, chistoserdova2003methylotrophyinmethylobacterium pages 5-6)
• Martins A.M. et al. Oct 2019. Journal of Biological Chemistry. “A two-component protease in Methylorubrum extorquens with high activity toward the peptide precursor of the redox cofactor pyrroloquinoline quinone.” https://doi.org/10.1074/jbc.ra119.009684 (martins2019atwocomponentprotease pages 1-2, martins2019atwocomponentprotease pages 14-16)
• Ren Y. et al. Jan 2023. Biotechnology for Biofuels and Bioproducts. “Adaptive evolutionary strategy coupled with an optimized biosynthesis process for the efficient production of pyrroloquinoline quinone from methanol.” https://doi.org/10.1186/s13068-023-02261-y (ren2023adaptiveevolutionarystrategy pages 7-10, ren2023adaptiveevolutionarystrategy pages 10-11)
• Chen X. et al. Jul 2024. AMB Express. “Genome-based identification of phosphate-solubilizing capacities of soil bacterial isolates.” https://doi.org/10.1186/s13568-024-01745-w (chen2024genomebasedidentificationof pages 7-9, chen2024genomebasedidentificationof pages 2-3)
• Toyama H. Apr 2016. (Book chapter via DOI; deposited as arXiv text in retrieval). “Pyrroloquinoline Quinone (PQQ).” https://doi.org/10.1002/9783527681754.ch13 (toyama2016pyrroloquinolinequinone(pqq) pages 11-13)
• Yao Z., Morinaka B.I. Feb 2026. Chemical Society Reviews. “Radical enzymatic peptide cyclization in natural product biosynthesis.” https://doi.org/10.1039/d5cs00585j (includes synthesis of PqqE mechanistic/structural evidence). (yao2026radicalenzymaticpeptide pages 6-7)

References

1. (yao2026radicalenzymaticpeptide pages 6-7): Ziwei Yao and Brandon I. Morinaka. Radical enzymatic peptide cyclization in natural product biosynthesis. Chemical Society reviews, Feb 2026. URL: https://doi.org/10.1039/d5cs00585j, doi:10.1039/d5cs00585j. This article has 3 citations and is from a highest quality peer-reviewed journal.

2. (martins2019atwocomponentprotease pages 2-3): Ana M. Martins, John A. Latham, Paulo J. Martel, Ian Barr, Anthony T. Iavarone, and Judith P. Klinman. A two-component protease in methylorubrum extorquens with high activity toward the peptide precursor of the redox cofactor pyrroloquinoline quinone. Journal of Biological Chemistry, 294:15025-15036, Oct 2019. URL: https://doi.org/10.1074/jbc.ra119.009684, doi:10.1074/jbc.ra119.009684. This article has 38 citations and is from a domain leading peer-reviewed journal.

3. (kandy2025aromaticsidechaincrosslinking pages 4-6): Sanath K. Kandy, Michael A. Pasquale, and Jonathan R. Chekan. Aromatic side-chain crosslinking in ripp biosynthesis. Nature chemical biology, 21:168-181, Jan 2025. URL: https://doi.org/10.1038/s41589-024-01795-y, doi:10.1038/s41589-024-01795-y. This article has 38 citations and is from a highest quality peer-reviewed journal.

4. (chistoserdova2003methylotrophyinmethylobacterium pages 2-3): Ludmila Chistoserdova, Sung-Wei Chen, Alla Lapidus, and Mary E. Lidstrom. Methylotrophy in methylobacterium extorquens am1 from a genomic point of view. Journal of Bacteriology, 185:2980-2987, May 2003. URL: https://doi.org/10.1128/jb.185.10.2980-2987.2003, doi:10.1128/jb.185.10.2980-2987.2003. This article has 402 citations and is from a peer-reviewed journal.

5. (toyama2016pyrroloquinolinequinone(pqq) pages 11-13): Hirohide Toyama. Pyrroloquinoline quinone (pqq). ArXiv, pages 367-388, Apr 2016. URL: https://doi.org/10.1002/9783527681754.ch13, doi:10.1002/9783527681754.ch13. This article has 5 citations.

6. (ren2023adaptiveevolutionarystrategy pages 7-10): Yang Ren, Xinwei Yang, Lingtao Ding, Dongfang Liu, Yong Tao, Jianzhong Huang, and Chongrong Ke. Adaptive evolutionary strategy coupled with an optimized biosynthesis process for the efficient production of pyrroloquinoline quinone from methanol. Biotechnology for Biofuels and Bioproducts, Jan 2023. URL: https://doi.org/10.1186/s13068-023-02261-y, doi:10.1186/s13068-023-02261-y. This article has 12 citations and is from a domain leading peer-reviewed journal.

7. (chen2024genomebasedidentificationof pages 7-9): Xiaoqing Chen, Yiting Zhao, Shasha Huang, Josep Peñuelas, Jordi Sardans, Lei Wang, and Bangxiao Zheng. Genome-based identification of phosphate-solubilizing capacities of soil bacterial isolates. AMB Express, Jul 2024. URL: https://doi.org/10.1186/s13568-024-01745-w, doi:10.1186/s13568-024-01745-w. This article has 21 citations and is from a peer-reviewed journal.

8. (martins2019atwocomponentprotease pages 10-11): Ana M. Martins, John A. Latham, Paulo J. Martel, Ian Barr, Anthony T. Iavarone, and Judith P. Klinman. A two-component protease in methylorubrum extorquens with high activity toward the peptide precursor of the redox cofactor pyrroloquinoline quinone. Journal of Biological Chemistry, 294:15025-15036, Oct 2019. URL: https://doi.org/10.1074/jbc.ra119.009684, doi:10.1074/jbc.ra119.009684. This article has 38 citations and is from a domain leading peer-reviewed journal.

9. (ochsner2015methylobacteriumextorquensmethylotrophy pages 9-10): Andrea M. Ochsner, Frank Sonntag, Markus Buchhaupt, Jens Schrader, and Julia A. Vorholt. Methylobacterium extorquens: methylotrophy and biotechnological applications. Applied Microbiology and Biotechnology, 99:517-534, Nov 2015. URL: https://doi.org/10.1007/s00253-014-6240-3, doi:10.1007/s00253-014-6240-3. This article has 229 citations and is from a domain leading peer-reviewed journal.

10. (chistoserdova2003methylotrophyinmethylobacterium pages 5-6): Ludmila Chistoserdova, Sung-Wei Chen, Alla Lapidus, and Mary E. Lidstrom. Methylotrophy in methylobacterium extorquens am1 from a genomic point of view. Journal of Bacteriology, 185:2980-2987, May 2003. URL: https://doi.org/10.1128/jb.185.10.2980-2987.2003, doi:10.1128/jb.185.10.2980-2987.2003. This article has 402 citations and is from a peer-reviewed journal.

11. (martins2019atwocomponentprotease pages 1-2): Ana M. Martins, John A. Latham, Paulo J. Martel, Ian Barr, Anthony T. Iavarone, and Judith P. Klinman. A two-component protease in methylorubrum extorquens with high activity toward the peptide precursor of the redox cofactor pyrroloquinoline quinone. Journal of Biological Chemistry, 294:15025-15036, Oct 2019. URL: https://doi.org/10.1074/jbc.ra119.009684, doi:10.1074/jbc.ra119.009684. This article has 38 citations and is from a domain leading peer-reviewed journal.

12. (martins2019atwocomponentprotease pages 14-16): Ana M. Martins, John A. Latham, Paulo J. Martel, Ian Barr, Anthony T. Iavarone, and Judith P. Klinman. A two-component protease in methylorubrum extorquens with high activity toward the peptide precursor of the redox cofactor pyrroloquinoline quinone. Journal of Biological Chemistry, 294:15025-15036, Oct 2019. URL: https://doi.org/10.1074/jbc.ra119.009684, doi:10.1074/jbc.ra119.009684. This article has 38 citations and is from a domain leading peer-reviewed journal.

13. (ren2023adaptiveevolutionarystrategy pages 1-2): Yang Ren, Xinwei Yang, Lingtao Ding, Dongfang Liu, Yong Tao, Jianzhong Huang, and Chongrong Ke. Adaptive evolutionary strategy coupled with an optimized biosynthesis process for the efficient production of pyrroloquinoline quinone from methanol. Biotechnology for Biofuels and Bioproducts, Jan 2023. URL: https://doi.org/10.1186/s13068-023-02261-y, doi:10.1186/s13068-023-02261-y. This article has 12 citations and is from a domain leading peer-reviewed journal.

14. (ren2023adaptiveevolutionarystrategy pages 10-11): Yang Ren, Xinwei Yang, Lingtao Ding, Dongfang Liu, Yong Tao, Jianzhong Huang, and Chongrong Ke. Adaptive evolutionary strategy coupled with an optimized biosynthesis process for the efficient production of pyrroloquinoline quinone from methanol. Biotechnology for Biofuels and Bioproducts, Jan 2023. URL: https://doi.org/10.1186/s13068-023-02261-y, doi:10.1186/s13068-023-02261-y. This article has 12 citations and is from a domain leading peer-reviewed journal.

15. (chen2024genomebasedidentificationof pages 1-2): Xiaoqing Chen, Yiting Zhao, Shasha Huang, Josep Peñuelas, Jordi Sardans, Lei Wang, and Bangxiao Zheng. Genome-based identification of phosphate-solubilizing capacities of soil bacterial isolates. AMB Express, Jul 2024. URL: https://doi.org/10.1186/s13568-024-01745-w, doi:10.1186/s13568-024-01745-w. This article has 21 citations and is from a peer-reviewed journal.

16. (chen2024genomebasedidentificationof pages 3-5): Xiaoqing Chen, Yiting Zhao, Shasha Huang, Josep Peñuelas, Jordi Sardans, Lei Wang, and Bangxiao Zheng. Genome-based identification of phosphate-solubilizing capacities of soil bacterial isolates. AMB Express, Jul 2024. URL: https://doi.org/10.1186/s13568-024-01745-w, doi:10.1186/s13568-024-01745-w. This article has 21 citations and is from a peer-reviewed journal.

17. (chen2024genomebasedidentificationof pages 2-3): Xiaoqing Chen, Yiting Zhao, Shasha Huang, Josep Peñuelas, Jordi Sardans, Lei Wang, and Bangxiao Zheng. Genome-based identification of phosphate-solubilizing capacities of soil bacterial isolates. AMB Express, Jul 2024. URL: https://doi.org/10.1186/s13568-024-01745-w, doi:10.1186/s13568-024-01745-w. This article has 21 citations and is from a peer-reviewed journal.

18. (chen2024genomebasedidentificationof pages 5-7): Xiaoqing Chen, Yiting Zhao, Shasha Huang, Josep Peñuelas, Jordi Sardans, Lei Wang, and Bangxiao Zheng. Genome-based identification of phosphate-solubilizing capacities of soil bacterial isolates. AMB Express, Jul 2024. URL: https://doi.org/10.1186/s13568-024-01745-w, doi:10.1186/s13568-024-01745-w. This article has 21 citations and is from a peer-reviewed journal.

19. (martins2019atwocomponentprotease pages 5-6): Ana M. Martins, John A. Latham, Paulo J. Martel, Ian Barr, Anthony T. Iavarone, and Judith P. Klinman. A two-component protease in methylorubrum extorquens with high activity toward the peptide precursor of the redox cofactor pyrroloquinoline quinone. Journal of Biological Chemistry, 294:15025-15036, Oct 2019. URL: https://doi.org/10.1074/jbc.ra119.009684, doi:10.1074/jbc.ra119.009684. This article has 38 citations and is from a domain leading peer-reviewed journal.

20. (ren2023adaptiveevolutionarystrategy pages 2-4): Yang Ren, Xinwei Yang, Lingtao Ding, Dongfang Liu, Yong Tao, Jianzhong Huang, and Chongrong Ke. Adaptive evolutionary strategy coupled with an optimized biosynthesis process for the efficient production of pyrroloquinoline quinone from methanol. Biotechnology for Biofuels and Bioproducts, Jan 2023. URL: https://doi.org/10.1186/s13068-023-02261-y, doi:10.1186/s13068-023-02261-y. This article has 12 citations and is from a domain leading peer-reviewed journal.

Artifacts

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Citations

1. yao2026radicalenzymaticpeptide pages 6-7
2. chistoserdova2003methylotrophyinmethylobacterium pages 5-6
3. chen2024genomebasedidentificationof pages 7-9
4. kandy2025aromaticsidechaincrosslinking pages 4-6
5. martins2019atwocomponentprotease pages 14-16
6. martins2019atwocomponentprotease pages 1-2
7. ren2023adaptiveevolutionarystrategy pages 1-2
8. ren2023adaptiveevolutionarystrategy pages 10-11
9. ren2023adaptiveevolutionarystrategy pages 7-10
10. martins2019atwocomponentprotease pages 2-3
11. chistoserdova2003methylotrophyinmethylobacterium pages 2-3
12. martins2019atwocomponentprotease pages 10-11
13. ochsner2015methylobacteriumextorquensmethylotrophy pages 9-10
14. chen2024genomebasedidentificationof pages 1-2
15. chen2024genomebasedidentificationof pages 3-5
16. chen2024genomebasedidentificationof pages 2-3
17. chen2024genomebasedidentificationof pages 5-7
18. martins2019atwocomponentprotease pages 5-6
19. ren2023adaptiveevolutionarystrategy pages 2-4
20. 4Fe–4S
21. 2Fe–2S
22. https://doi.org/10.1186/s13068-023-02261-y
23. https://doi.org/10.1186/s13568-024-01745-w
24. https://doi.org/10.1039/d5cs00585j
25. https://doi.org/10.1074/jbc.ra119.009684
26. https://doi.org/10.1128/jb.185.10.2980-2987.2003;
27. https://doi.org/10.1002/9783527681754.ch13;
28. https://doi.org/10.1074/jbc.ra119.009684;
29. https://doi.org/10.1007/s00253-014-6240-3
30. https://doi.org/10.1128/jb.185.10.2980-2987.2003
31. https://doi.org/10.1002/9783527681754.ch13
32. https://doi.org/10.1039/d5cs00585j,
33. https://doi.org/10.1074/jbc.ra119.009684,
34. https://doi.org/10.1038/s41589-024-01795-y,
35. https://doi.org/10.1128/jb.185.10.2980-2987.2003,
36. https://doi.org/10.1002/9783527681754.ch13,
37. https://doi.org/10.1186/s13068-023-02261-y,
38. https://doi.org/10.1186/s13568-024-01745-w,
39. https://doi.org/10.1007/s00253-014-6240-3,