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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 UniProt accession Q9HDX8 is specified (by the user-provided UniProt record) as Schizosaccharomyces pombe alo1 (ORF SPAPB1A10.12c), annotated as D-arabinono-1,4-lactone oxidase (ALO; EC 1.1.3.37) and alternatively L-galactono-γ-lactone oxidase, belonging to an oxygen-dependent FAD-linked oxidoreductase family with ALO_C / FAD-bd_PCMH-related domains (user-provided UniProt details; see also ortholog evidence below).
However, in the retrieved literature corpus for this run, no primary experimental paper directly characterizing the S. pombe SPAPB1A10.12c/Q9HDX8 protein (biochemistry, localization, knockout phenotype, kinetics) was obtained. Consequently, S. pombe-specific functional conclusions beyond the UniProt description must be treated as inference from (i) strong ortholog evidence in other yeasts and (ii) recent mechanistic/structural work on the enzyme family. This is critical because “ALO1” is a well-studied gene symbol in Saccharomyces cerevisiae (ORF YML086C) and can be confused with S. pombe alo1 (Q9HDX8). (huh1998d‐erythroascorbicacidis pages 1-2, huh1998d‐erythroascorbicacidis pages 2-3)
Aldonolactone oxidoreductases (including fungal/yeast ALO) catalyze the terminal oxidation step that generates vitamin C (L-ascorbate) or vitamin C analogs (e.g., D-erythroascorbate) by oxidizing an aldonolactone substrate at C2 to form the characteristic C2–C3 double bond of ascorbate-like molecules. In a broad mechanistic framework, the substrate is oxidized by a flavin (FAD) cofactor via hydride transfer to the flavin, followed by reoxidation of reduced flavin by an electron acceptor. (boverio2024structuremechanismand pages 3-5, boverio2024structuremechanismand pages 1-2)
A key definitional distinction is whether the enzyme behaves as an oxidase (uses O2 as electron acceptor) or a dehydrogenase (uses cytochrome c or other acceptors). Recent structural/functional synthesis explicitly states that “The reduced flavin will be re-oxidized by oxygen in GULO and ALO or cytochrome c in GalDH.” (boverio2024structuremechanismand pages 3-5).
Consistent with this, a yeast D-erythroascorbate biosynthetic pathway description specifies that the mitochondrial D-arabinono-1,4-lactone oxidase uses oxygen as an electron acceptor, producing D-erythroascorbate and hydrogen peroxide. (kim1998darabinosedehydrogenaseand pages 1-2)
Yeasts often produce D-erythroascorbate (EASC), a five-carbon ascorbate analog with antioxidant properties. In S. cerevisiae, EASC levels depend on genes encoding the terminal oxidase step (ALO1) and upstream dehydrogenase steps; disruption of these can abolish detectable EASC. (huh1998d‐erythroascorbicacidis pages 1-2, huh1998d‐erythroascorbicacidis pages 3-5)
The strongest direct experimental literature retrieved in this run concerns S. cerevisiae ALO1, experimentally identified as ORF YML086C, encoding a D-arabinono-1,4-lactone oxidase/lactone oxidase involved in EASC biosynthesis. (huh1998d‐erythroascorbicacidis pages 1-2, huh1998d‐erythroascorbicacidis pages 2-3)
This is not the same gene identifier as S. pombe SPAPB1A10.12c / Q9HDX8. Therefore, all S. cerevisiae “ALO1” evidence is used here only as ortholog-based functional inference, not as direct evidence for S. pombe Q9HDX8.
Given UniProt’s enzyme name (D-arabinono-1,4-lactone oxidase; EC 1.1.3.37) and the strong biochemical definition of yeast ALO enzymes, the most defensible functional model for S. pombe Alo1 (Q9HDX8) is:
A FAD-dependent aldonolactone oxidase that oxidizes D-arabinono-1,4-lactone to D-erythroascorbate, using O2 as the terminal electron acceptor (oxidase), thereby contributing to an ascorbate-like antioxidant system.
Ortholog evidence in S. cerevisiae shows that ALO1 encodes the terminal EASC biosynthetic oxidase, and that ALO activity is absent in alo1 mutants and increased upon ALO1 multicopy expression. (huh1998d‐erythroascorbicacidis pages 1-2, huh1998d‐erythroascorbicacidis pages 3-5)
A pathway-level description in yeast systems states: D-arabinose is converted (via a dehydrogenase) to D-arabinono lactones, culminating in D-arabinono-1,4-lactone oxidase catalyzing oxidation to D-erythroascorbate with oxygen as electron acceptor (and H2O2 production). (kim1998darabinosedehydrogenaseand pages 1-2)
Biochemical purification of the budding-yeast enzyme demonstrates that “ALO” can oxidize multiple related lactones: L-gulono-1,4-lactone, D-arabinono-1,4-lactone, and L-galactono-1,4-lactone. (huh1998d‐erythroascorbicacidis pages 2-3, huh1998d‐erythroascorbicacidis pages 1-2). This supports the plausibility of UniProt’s alternative name (“L-galactono-γ-lactone oxidase”) for Q9HDX8, but for S. pombe it remains inferred rather than experimentally demonstrated.
The S. cerevisiae ALO enzyme sequence contains a putative covalent FAD-binding site (PROSITE motif PS00862) in residues ~23–56, and the paper proposes a specific histidine (His-56) as the covalent flavin attachment site; the enzyme is described as a flavoenzyme with covalently bound FAD in yeast. (huh1998d‐erythroascorbicacidis pages 2-3)
Recent mechanistic synthesis of aldonolactone oxidoreductases reinforces that fungal/animal oxidase-type enzymes (ALO/GULO) commonly feature a covalent histidyl-FAD and use O2 as electron acceptor, in contrast to plant GalDH which uses cytochrome c and has dissociable flavin. (jamil2023biochemicalandstructurala pages 16-19)
For S. cerevisiae, ALO was purified from the mitochondrial fraction, and hydropathy analysis predicted an integral membrane protein with a transmembrane segment (residues 172–188), consistent with a mitochondrial membrane association. (huh1998d‐erythroascorbicacidis pages 1-2, huh1998d‐erythroascorbicacidis pages 2-3)
While UniProt’s domain/family assignments for S. pombe Q9HDX8 are consistent with an oxidase-type aldonolactone oxidoreductase, no direct localization data for the S. pombe protein were retrieved in this run.
In S. cerevisiae, genetic disruption of ALO1 eliminated detectable EASC and ALO activity; these mutants displayed increased sensitivity to oxidative stressors (H2O2 and menadione), while ALO1 overexpression increased resistance. (huh1998d‐erythroascorbicacidis pages 3-5, huh1998d‐erythroascorbicacidis pages 5-6)
A fission-yeast oxidative stress paper uses this budding-yeast ALO1/EASC system as an example of a gene important for resistance to acute peroxide stress, noting it “apparently plays no role in the adaptive response to H2O2.” (quinn2002distinctregulatoryproteins pages 9-10)
For S. pombe specifically, Quinn et al. (2002) characterize Sty1/Pap1/Atf1 peroxide signaling but do not provide direct experimental data for S. pombe alo1; their ALO1 statement is explicitly about S. cerevisiae (quinn2002distinctregulatoryproteins pages 9-10).
A 2024 Nature Communications study integrates molecular phylogeny, kinetics, mutagenesis, and crystallography to explain how aldonolactone oxidoreductases diversified across eukaryotes while maintaining an “overarching vitamin C-generating function.” It reports that a single flavin-interacting amino acid can modulate reactivity with electron acceptors (including oxygen), effectively distinguishing oxidase vs dehydrogenase behavior. It also shows that a small set of active-site side chains can switch substrate stereoselectivity and preference, and it explicitly notes that fungi produce D-erythroascorbate via oxidation of D-arabinono-1,4-lactone by ALO-type enzymes. (boverio2024structuremechanismand pages 1-2)
Quantitative data in this work include a reported flavin re-oxidation rate (kox) of ~6.4 s−1 at atmospheric oxygen for a representative oxidase-type enzyme context and strong differences in substrate preference among clades (GalDH up to ~1000-fold preference; GULO ≤10-fold). (boverio2024structuremechanismand pages 5-7)
A 2023 synthesis focused on ancestral GalDH emphasizes that fungal/animal oxidase-type enzymes (ALO/GULO) use molecular oxygen, frequently have covalent histidyl-FAD, and contrasts these with plant GalDH’s cytochrome c dependence and lack of covalent flavin attachment. It also highlights candidate residues affecting oxygen diffusion and substrate specificity (e.g., a conserved Glu-Arg pair and residues modulating oxygen access). (jamil2023biochemicalandstructurala pages 16-19)
A widely cited applied study (Applied and Environmental Microbiology; received 30 Dec 2003 / accepted 6 Jun 2004 / published Oct 2004) reports that although yeasts do not possess a native pathway to synthesize vitamin C from glucose, they can accumulate L-ascorbic acid intracellularly when incubated with pathway intermediates (e.g., L-galactose, L-galactono-1,4-lactone, L-gulono-1,4-lactone). Overexpression of S. cerevisiae enzymes including D-arabinono-1,4-lactone oxidase enhanced this ability, and strains overexpressing endogenous oxidase plus L-galactose dehydrogenase produced ~100 mg/L L-ascorbic acid converting ~40% (wt/vol) of starting L-galactose under the reported conditions. (sauer2004productionoflascorbic pages 1-2)
This demonstrates that ALO-class enzymes have practical utility as terminal oxidases in engineered biosynthetic routes, even though this application literature is primarily based on S. cerevisiae rather than S. pombe.
The following figure crops show the experimentally measured dependence of EASC and ALO activity on the ALO1 gene in S. cerevisiae (HPLC-electrochemical detection and enzymatic activity assay), supporting the core functional model for yeast ALO enzymes that underpins ortholog-based inference for S. pombe Q9HDX8. (huh1998d‐erythroascorbicacidis media 89a6d51f, huh1998d‐erythroascorbicacidis media eca5982c)
Despite targeted searches (by UniProt accession, ORF name, and organism), no direct S. pombe alo1/Q9HDX8 experimental characterization was retrieved in this run. Therefore:
- Reaction, substrate breadth, kinetics, localization, and phenotypes are not experimentally confirmed here for S. pombe.
- The report provides a cautious inferred annotation anchored by: (i) UniProt-provided identity; (ii) strong primary evidence for yeast ALO orthologs; and (iii) 2023–2024 enzyme-family mechanistic research.
To convert this inferred annotation into S. pombe-specific functional annotation, the most direct experiments would be: (i) purification/assay of S. pombe Alo1 with D-arabinono-1,4-lactone; (ii) gene deletion and measurement of intracellular D-erythroascorbate; and (iii) microscopy or fractionation for localization.
| Claim | Species/gene | Evidence type | Key details/values | Source (URL, year) |
|---|---|---|---|---|
| Target identity to research | Schizosaccharomyces pombe alo1 / SPAPB1A10.12c / UniProt Q9HDX8 | Database-defined target identity from prompt; direct primary-literature evidence not retrieved in available contexts | Target protein is specified as D-arabinono-1,4-lactone oxidase / L-galactono-γ-lactone oxidase (EC 1.1.3.37), distinct from budding-yeast ALO1/YML086C; available paper contexts did not provide a direct biochemical characterization for the S. pombe locus, so S. pombe-specific functional claims must be treated cautiously | UniProt accession supplied in user prompt; comparative caution supported by available literature context showing most direct biochemical data are from S. cerevisiae rather than S. pombe (huh1998d‐erythroascorbicacidis pages 1-2, huh1998d‐erythroascorbicacidis pages 2-3) |
| Symbol ambiguity warning: “ALO1” is well characterized in budding yeast and can be confused with S. pombe alo1 | Saccharomyces cerevisiae ALO1 / YML086C vs. S. pombe alo1 / SPAPB1A10.12c | Direct experimental evidence for S. cerevisiae; cross-species comparison/inference for S. pombe | In S. cerevisiae, ALO1 was identified experimentally as ORF YML086C encoding the lactone oxidase; this is not the same locus designation as S. pombe SPAPB1A10.12c. Therefore, literature on YML086C should not be conflated with Q9HDX8 without explicit orthology support | Huh et al. identified S. cerevisiae ALO1 = YML086C (https://doi.org/10.1046/j.1365-2958.1998.01133.x, 1998) (huh1998d‐erythroascorbicacidis pages 1-2, huh1998d‐erythroascorbicacidis pages 2-3) |
| Core enzymatic function of yeast ALO1 enzymes | S. cerevisiae ALO1; inference to S. pombe alo1/Q9HDX8 | Direct biochemical/genetic evidence in ortholog; inference to target based on annotation/name | ALO catalyzes the terminal oxidation step in D-erythroascorbic acid (EASC) biosynthesis: D-arabinono-1,4-lactone → D-erythroascorbic acid | https://doi.org/10.1046/j.1365-2958.1998.01133.x (1998); pathway context https://doi.org/10.1016/S0167-4838(98)00217-9 (1998) (huh1998d‐erythroascorbicacidis pages 1-2, kim1998darabinosedehydrogenaseand pages 1-2) |
| Substrate range is broader than the canonical name implies | S. cerevisiae ALO1; inference to S. pombe alo1/Q9HDX8 | Direct enzymology in ortholog | Purified budding-yeast ALO oxidized D-arabinono-1,4-lactone, L-gulono-1,4-lactone, and L-galactono-1,4-lactone; this supports the alternate name L-galactono-γ-lactone oxidase and suggests relaxed substrate specificity within aldonolactones | https://doi.org/10.1046/j.1365-2958.1998.01133.x (1998) (huh1998d‐erythroascorbicacidis pages 2-3, huh1998d‐erythroascorbicacidis pages 1-2) |
| Electron acceptor is molecular oxygen | Yeast D-arabinono-1,4-lactone oxidase (directly discussed for yeast pathway; species example includes S. cerevisiae/Candida) | Direct pathway/biochemical evidence | Oxidase step uses O2 as electron acceptor; pathway produces D-erythroascorbic acid from D-arabinono-1,4-lactone via an oxygen-dependent reaction | https://doi.org/10.1016/S0167-4838(98)00217-9 (1998) (kim1998darabinosedehydrogenaseand pages 1-2) |
| Cofactor/family assignment | S. cerevisiae ALO1; inference to S. pombe alo1/Q9HDX8 | Direct sequence/biochemical evidence in ortholog; target-family inference from UniProt/domain naming | ALO is a flavoenzyme with covalently bound FAD; a putative covalent FAD-binding region was mapped to residues 23–56, with His56 proposed as the FAD-linked histidine. This is consistent with the oxygen-dependent FAD-linked oxidoreductase family assigned to Q9HDX8 | https://doi.org/10.1046/j.1365-2958.1998.01133.x (1998) (huh1998d‐erythroascorbicacidis pages 2-3, huh1998d‐erythroascorbicacidis pages 1-2) |
| Subcellular localization | S. cerevisiae ALO1; inference to S. pombe alo1/Q9HDX8 | Direct biochemical/fractionation and sequence inference in ortholog | ALO was purified from the mitochondrial fraction; enzyme activity was assayed in mitochondrial preparations; sequence analysis predicted an integral membrane protein with a transmembrane segment (aa 172–188), supporting a mitochondrial membrane localization in budding yeast | https://doi.org/10.1046/j.1365-2958.1998.01133.x (1998) (huh1998d‐erythroascorbicacidis pages 1-2, huh1998d‐erythroascorbicacidis pages 3-5, huh1998d‐erythroascorbicacidis pages 2-3) |
| Genetic evidence linking ALO1 to EASC production | S. cerevisiae ALO1 | Direct gene disruption/overexpression evidence | alo1 deletion abolished detectable EASC and ALO activity; multicopy ALO1 increased intracellular EASC ~6.9-fold and ALO activity ~7.3-fold | https://doi.org/10.1046/j.1365-2958.1998.01133.x (1998) (huh1998d‐erythroascorbicacidis pages 3-5, huh1998d‐erythroascorbicacidis media 89a6d51f) |
| Oxidative-stress phenotype | S. cerevisiae ALO1; used comparatively in S. pombe stress literature | Direct phenotype in ortholog; comparative citation in fission-yeast paper | alo1 mutants were hypersensitive to H2O2 and menadione; ALO1 overexpression increased survival. Quinn et al. cite budding-yeast ALO1 as an example of a gene needed for acute H2O2 resistance but not apparently for adaptive response | https://doi.org/10.1046/j.1365-2958.1998.01133.x (1998); comparative mention in https://doi.org/10.1091/mbc.01-06-0288 (2002) (huh1998d‐erythroascorbicacidis pages 5-6, huh1998d‐erythroascorbicacidis pages 3-5, quinn2002distinctregulatoryproteins pages 9-10) |
| Biotechnological application of ALO1 enzyme class | S. cerevisiae ALO1 | Direct application/engineering evidence | Overexpression of S. cerevisiae ALO1 enhanced conversion of exogenous lactone precursors toward L-ascorbic acid; engineered yeast strains coexpressing pathway enzymes produced about 100 mg/L L-ascorbic acid from L-galactose, illustrating real-world use of ALO enzymes in vitamin C bioproduction | https://doi.org/10.1128/AEM.70.10.6086-6091.2004 (2004) (sauer2004productionoflascorbic pages 1-2) |
| What is directly evidenced for the S. pombe target in available sources | S. pombe alo1 / SPAPB1A10.12c / Q9HDX8 | Limited direct evidence in retrieved contexts | In the available paper contexts, no direct biochemical characterization, localization experiment, knockout phenotype, or kinetic data were retrieved specifically for S. pombe SPAPB1A10.12c/Q9HDX8. Therefore, specific functional annotation for the target relies mainly on UniProt naming/domain assignment plus ortholog-based inference from yeast ALO1 enzymes | Lack of direct target-specific evidence in retrieved contexts; contrast with direct S. cerevisiae evidence (huh1998d‐erythroascorbicacidis pages 1-2, huh1998d‐erythroascorbicacidis pages 2-3, quinn2002distinctregulatoryproteins pages 9-10) |
| Best-supported annotation strategy for Q9HDX8 | S. pombe alo1 / Q9HDX8 | Evidence synthesis | The most defensible annotation is: probable mitochondrial, membrane-associated FAD-dependent aldonolactone oxidase participating in D-erythroascorbate/vitamin-C-like biosynthesis, with likely activity on D-arabinono-1,4-lactone and possibly L-galactono-/L-gulono-1,4-lactones; however, these mechanistic details are inferred from orthologs, not directly demonstrated here for S. pombe | Supported by direct budding-yeast enzymology/genetics and comparative oxidative-stress literature: https://doi.org/10.1046/j.1365-2958.1998.01133.x (1998), https://doi.org/10.1016/S0167-4838(98)00217-9 (1998), https://doi.org/10.1128/AEM.70.10.6086-6091.2004 (2004), https://doi.org/10.1091/mbc.01-06-0288 (2002) (huh1998d‐erythroascorbicacidis pages 2-3, kim1998darabinosedehydrogenaseand pages 1-2, sauer2004productionoflascorbic pages 1-2, quinn2002distinctregulatoryproteins pages 9-10) |
Table: This table separates what is directly demonstrated for yeast ALO1 enzymes from what can be cautiously inferred for the target S. pombe protein Q9HDX8. It is useful for avoiding symbol confusion and for tracing each functional claim to specific primary sources.
References
(huh1998d‐erythroascorbicacidis pages 1-2): Won‐Ki Huh, Byung‐Hoon Lee, Seong‐Tae Kim, Yeon‐Ran Kim, Gi‐Eun Rhie, Yong‐Woon Baek, Cheol‐Sang Hwang, Jung‐Shin Lee, and Sa‐Ouk Kang. D‐erythroascorbic acid is an important antioxidant molecule in saccharomyces cerevisiae. Molecular Microbiology, 30:895-903, Nov 1998. URL: https://doi.org/10.1046/j.1365-2958.1998.01133.x, doi:10.1046/j.1365-2958.1998.01133.x. This article has 152 citations and is from a domain leading peer-reviewed journal.
(huh1998d‐erythroascorbicacidis pages 2-3): Won‐Ki Huh, Byung‐Hoon Lee, Seong‐Tae Kim, Yeon‐Ran Kim, Gi‐Eun Rhie, Yong‐Woon Baek, Cheol‐Sang Hwang, Jung‐Shin Lee, and Sa‐Ouk Kang. D‐erythroascorbic acid is an important antioxidant molecule in saccharomyces cerevisiae. Molecular Microbiology, 30:895-903, Nov 1998. URL: https://doi.org/10.1046/j.1365-2958.1998.01133.x, doi:10.1046/j.1365-2958.1998.01133.x. This article has 152 citations and is from a domain leading peer-reviewed journal.
(boverio2024structuremechanismand pages 3-5): Alessandro Boverio, Neelam Jamil, Barbara Mannucci, Maria Laura Mascotti, Marco W. Fraaije, and Andrea Mattevi. Structure, mechanism, and evolution of the last step in vitamin c biosynthesis. Nature Communications, May 2024. URL: https://doi.org/10.1038/s41467-024-48410-1, doi:10.1038/s41467-024-48410-1. This article has 16 citations and is from a highest quality peer-reviewed journal.
(boverio2024structuremechanismand pages 1-2): Alessandro Boverio, Neelam Jamil, Barbara Mannucci, Maria Laura Mascotti, Marco W. Fraaije, and Andrea Mattevi. Structure, mechanism, and evolution of the last step in vitamin c biosynthesis. Nature Communications, May 2024. URL: https://doi.org/10.1038/s41467-024-48410-1, doi:10.1038/s41467-024-48410-1. This article has 16 citations and is from a highest quality peer-reviewed journal.
(kim1998darabinosedehydrogenaseand pages 1-2): Seong-Tae Kim, Won-Ki Huh, Byung-Hoon Lee, and Sa-Ouk Kang. D-arabinose dehydrogenase and its gene from saccharomyces cerevisiae. Biochimica et biophysica acta, 1429 1:29-39, Dec 1998. URL: https://doi.org/10.1016/s0167-4838(98)00217-9, doi:10.1016/s0167-4838(98)00217-9. This article has 95 citations.
(huh1998d‐erythroascorbicacidis pages 3-5): Won‐Ki Huh, Byung‐Hoon Lee, Seong‐Tae Kim, Yeon‐Ran Kim, Gi‐Eun Rhie, Yong‐Woon Baek, Cheol‐Sang Hwang, Jung‐Shin Lee, and Sa‐Ouk Kang. D‐erythroascorbic acid is an important antioxidant molecule in saccharomyces cerevisiae. Molecular Microbiology, 30:895-903, Nov 1998. URL: https://doi.org/10.1046/j.1365-2958.1998.01133.x, doi:10.1046/j.1365-2958.1998.01133.x. This article has 152 citations and is from a domain leading peer-reviewed journal.
(jamil2023biochemicalandstructurala pages 16-19): N JAMIL. Biochemical and structural characterization of ancestral l-galactono-1, 4-lactone dehydrogenase. Unknown journal, 2023.
(huh1998d‐erythroascorbicacidis pages 5-6): Won‐Ki Huh, Byung‐Hoon Lee, Seong‐Tae Kim, Yeon‐Ran Kim, Gi‐Eun Rhie, Yong‐Woon Baek, Cheol‐Sang Hwang, Jung‐Shin Lee, and Sa‐Ouk Kang. D‐erythroascorbic acid is an important antioxidant molecule in saccharomyces cerevisiae. Molecular Microbiology, 30:895-903, Nov 1998. URL: https://doi.org/10.1046/j.1365-2958.1998.01133.x, doi:10.1046/j.1365-2958.1998.01133.x. This article has 152 citations and is from a domain leading peer-reviewed journal.
(quinn2002distinctregulatoryproteins pages 9-10): Janet Quinn, Victoria J. Findlay, Keren Dawson, Jonathan B.A. Millar, Nic Jones, Brian A. Morgan, and W. Mark Toone. Distinct regulatory proteins control the graded transcriptional response to increasing h(2)o(2) levels in fission yeast schizosaccharomyces pombe. Molecular biology of the cell, 13 3:805-16, Mar 2002. URL: https://doi.org/10.1091/mbc.01-06-0288, doi:10.1091/mbc.01-06-0288. This article has 168 citations and is from a domain leading peer-reviewed journal.
(boverio2024structuremechanismand pages 5-7): Alessandro Boverio, Neelam Jamil, Barbara Mannucci, Maria Laura Mascotti, Marco W. Fraaije, and Andrea Mattevi. Structure, mechanism, and evolution of the last step in vitamin c biosynthesis. Nature Communications, May 2024. URL: https://doi.org/10.1038/s41467-024-48410-1, doi:10.1038/s41467-024-48410-1. This article has 16 citations and is from a highest quality peer-reviewed journal.
(sauer2004productionoflascorbic pages 1-2): Michael Sauer, Paola Branduardi, Minoska Valli, and Danilo Porro. Production of l-ascorbic acid by metabolically engineered saccharomyces cerevisiae and zygosaccharomyces bailii. Applied and Environmental Microbiology, 70:6086-6091, Oct 2004. URL: https://doi.org/10.1128/aem.70.10.6086-6091.2004, doi:10.1128/aem.70.10.6086-6091.2004. This article has 134 citations and is from a peer-reviewed journal.
(huh1998d‐erythroascorbicacidis media 89a6d51f): Won‐Ki Huh, Byung‐Hoon Lee, Seong‐Tae Kim, Yeon‐Ran Kim, Gi‐Eun Rhie, Yong‐Woon Baek, Cheol‐Sang Hwang, Jung‐Shin Lee, and Sa‐Ouk Kang. D‐erythroascorbic acid is an important antioxidant molecule in saccharomyces cerevisiae. Molecular Microbiology, 30:895-903, Nov 1998. URL: https://doi.org/10.1046/j.1365-2958.1998.01133.x, doi:10.1046/j.1365-2958.1998.01133.x. This article has 152 citations and is from a domain leading peer-reviewed journal.
(huh1998d‐erythroascorbicacidis media eca5982c): Won‐Ki Huh, Byung‐Hoon Lee, Seong‐Tae Kim, Yeon‐Ran Kim, Gi‐Eun Rhie, Yong‐Woon Baek, Cheol‐Sang Hwang, Jung‐Shin Lee, and Sa‐Ouk Kang. D‐erythroascorbic acid is an important antioxidant molecule in saccharomyces cerevisiae. Molecular Microbiology, 30:895-903, Nov 1998. URL: https://doi.org/10.1046/j.1365-2958.1998.01133.x, doi:10.1046/j.1365-2958.1998.01133.x. This article has 152 citations and is from a domain leading peer-reviewed journal.