Commichau, Fabian M.

[["dc.bibliographiccitation.artnumber","758"],["dc.bibliographiccitation.journal","Frontiers in Microbiology"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Stannek, Lorena"],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Care, Rachel A."],["dc.contributor.author","Gerth, Ulf"],["dc.contributor.author","Commichau, Fabian M."],["dc.date.accessioned","2018-11-07T10:02:18Z"],["dc.date.available","2018-11-07T10:02:18Z"],["dc.date.issued","2015"],["dc.description.abstract","The Gram-positive model bacterium Bacillus subtilis contains two glutamate dehydrogenase-encoding genes, rocG and gudB. While the rocG gene encodes the functional GDH, the gudB gene is cryptic (gudB(CR)) in the laboratory strain 168 due to a perfect 18 bp-long direct repeat that renders the GudB enzyme inactive and unstable. Although constitutively expressed the GudB(CR) protein can hardly be detected in B. subtilis as it is rapidly degraded within stationary growth phase. Its high instability qualifies GudB(CR) as a model substrate for studying protein turnover in B. subtilis. Recently, we have developed a visual screen to monitor the GudB(CR) stability in the cell using a GFP-GudB(CR) fusion. Using fluorescent microscopy we found that the G FP protein is simultaneously degraded together with GudB(CR). This allows us to analyze the stability of GudB(CR) in living cells. By combining the visual screen with a transposon mutagenesis approach we looked for mutants that show an increased fluorescence signal compared to the wild type indicating a stabilized GFP-GudB(CR) fusion. We observed, that disruption of the arginine kinase encoding gene mcsB upon transposon insertion leads to increased amounts of the GFP-GudB(CR) fusion in this mutant. Deletion of the cognate arginine phosphatase YwIE in contrast results in reduced levels of the GFP-GudB(CR) fusion. Recently, it was shown that the kinase McsB is involved in phosphorylation of GudB(CR) on arginine residues. Here we show that selected arginine-lysine point mutations of GudB(CR) exhibit no influence on degradation. The activity of McsB and YwIE, however, are crucial for the activation and inhibition, respectively, of a proteolytic machinery that efficiently degrades the unstable GudB(CR) protein in B. subtilis."],["dc.identifier.doi","10.3389/fmicb.2014.00758"],["dc.identifier.isi","000348706900001"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11795"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38197"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Frontiers Media Sa"],["dc.relation.issn","1664-302X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Factors that mediate and prevent degradation of the inactive and unstable GudB protein in Bacillus subtilis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Microbiology"],["dc.bibliographiccitation.volume","13"],["dc.contributor.affiliation","Stecker, Daniela; 1Faculty of Biology, Philipps-University Marburg, Marburg, Germany"],["dc.contributor.affiliation","Hoffmann, Tamara; 1Faculty of Biology, Philipps-University Marburg, Marburg, Germany"],["dc.contributor.affiliation","Link, Hannes; 2SYNMIKRO Research Center, Philipps-University Marburg, Marburg, Germany"],["dc.contributor.affiliation","Commichau, Fabian M.; 4Insitute of Microbiology and Genetics, Georg-August-University Göttingen, Göttingen, Germany"],["dc.contributor.affiliation","Bremer, Erhard; 1Faculty of Biology, Philipps-University Marburg, Marburg, Germany"],["dc.contributor.author","Stecker, Daniela"],["dc.contributor.author","Hoffmann, Tamara"],["dc.contributor.author","Link, Hannes"],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Bremer, Erhard"],["dc.date.accessioned","2022-07-01T06:45:49Z"],["dc.date.available","2022-07-01T06:45:49Z"],["dc.date.issued","2022-06-16"],["dc.date.updated","2022-06-30T17:13:09Z"],["dc.description.abstract","The accumulation of the compatible solute L-proline by Bacillus subtilis via synthesis is a cornerstone in the cell’s defense against high salinity as the genetic disruption of this biosynthetic process causes osmotic sensitivity. To understand how B. subtilis could potentially cope with high osmolarity surroundings without the functioning of its natural osmostress adaptive L-proline biosynthetic route (ProJ-ProA-ProH), we isolated suppressor strains of proA mutants under high-salinity growth conditions. These osmostress-tolerant strains carried mutations affecting either the AhrC transcriptional regulator or its operator positioned in front of the argCJBD-carAB-argF L-ornithine/L-citrulline/L-arginine biosynthetic operon. Osmostress protection assays, molecular analysis and targeted metabolomics showed that these mutations, in conjunction with regulatory mutations affecting rocR-rocDEF expression, connect and re-purpose three different physiological processes: (i) the biosynthetic pathway for L-arginine, (ii) the RocD-dependent degradation route for L-ornithine, and (iii) the last step in L-proline biosynthesis. Hence, osmostress adaptation without a functional ProJ-ProA-ProH route is made possible through a naturally existing, but inefficient, metabolic shunt that allows to substitute the enzyme activity of ProA by feeding the RocD-formed metabolite γ-glutamate-semialdehyde/Δ1-pyrroline-5-carboxylate into the biosynthetic route for the compatible solute L-proline. Notably, in one class of mutants, not only substantial L-proline pools but also large pools of L-citrulline were accumulated, a rather uncommon compatible solute in microorganisms. Collectively, our data provide an example of the considerable genetic plasticity and metabolic resourcefulness of B. subtilis to cope with everchanging environmental conditions."],["dc.identifier.doi","10.3389/fmicb.2022.908304"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/111959"],["dc.language.iso","en"],["dc.relation.eissn","1664-302X"],["dc.rights.uri","http://creativecommons.org/licenses/by/4.0/"],["dc.title","L-Proline Synthesis Mutants of Bacillus subtilis Overcome Osmotic Sensitivity by Genetically Adapting L-Arginine Metabolism"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1003199"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLoS Genetics"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T09:02:36Z"],["dc.date.available","2018-11-07T09:02:36Z"],["dc.date.issued","2012"],["dc.identifier.doi","10.1371/journal.pgen.1003199"],["dc.identifier.isi","000312905600062"],["dc.identifier.pmid","23300472"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8547"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24723"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1553-7404"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","A Mystery Unraveled: Essentiality of RNase III in Bacillus subtilis Is Caused by Resident Prophages"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.subtype","letter_note"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","D692"],["dc.bibliographiccitation.issue","D1"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","D698"],["dc.bibliographiccitation.volume","42"],["dc.contributor.author","Michna, Raphael H."],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Toedter, Dominik"],["dc.contributor.author","Zschiedrich, Christopher P."],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T09:46:34Z"],["dc.date.available","2018-11-07T09:46:34Z"],["dc.date.issued","2014"],["dc.description.abstract","Genome annotation and access to information from large-scale experimental approaches at the genome level are essential to improve our understanding of living cells and organisms. This is even more the case for model organisms that are the basis to study pathogens and technologically important species. We have generated SubtiWiki, a database for the Gram-positive model bacterium Bacillus subtilis (http://subtiwiki.uni-goettingen.de/). In addition to the established companion modules of SubtiWiki, SubtiPathways and SubtInteract, we have now created SubtiExpress, a third module, to visualize genome scale transcription data that are of unprecedented quality and density. Today, SubtiWiki is one of the most complete collections of knowledge on a living organism in one single resource."],["dc.identifier.doi","10.1093/nar/gkt1002"],["dc.identifier.isi","000331139800102"],["dc.identifier.pmid","24178028"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11716"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34903"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","SubtiWiki-a database for the model organism Bacillus subtilis that links pathway, interaction and expression information"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","32"],["dc.bibliographiccitation.journal","Frontiers in Molecular Biosciences"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Richts, Björn"],["dc.contributor.author","Rosenberg, Jonathan"],["dc.contributor.author","Commichau, Fabian M."],["dc.date.accessioned","2019-07-09T11:51:21Z"],["dc.date.available","2019-07-09T11:51:21Z"],["dc.date.issued","2019"],["dc.description.abstract","The B6 vitamer pyridoxal 5′-phosphate (PLP) is a co-factor for proteins and enzymes that are involved in diverse cellular processes. Therefore, PLP is essential for organisms from all kingdoms of life. Here we provide an overview about the PLP-dependent proteins from the Gram-positive soil bacterium Bacillus subtilis. Since B. subtilis serves as a model system in basic research and as a production host in industry, knowledge about the PLP-dependent proteins could facilitate engineering the bacteria for biotechnological applications. The survey revealed that the majority of the PLP-dependent proteins are involved in metabolic pathways like amino acid biosynthesis and degradation, biosynthesis of antibacterial compounds, utilization of nucleotides as well as in iron and carbon metabolism. Many PLP-dependent proteins participate in de novo synthesis of the co-factors biotin, folate, heme, and NAD+ as well as in cell wall metabolism, tRNA modification, regulation of gene expression, sporulation, and biofilm formation. A surprisingly large group of PLP-dependent proteins (29%) belong to the group of poorly characterized proteins. This review underpins the need to characterize the PLP-dependent proteins of unknown function to fully understand the “PLP-ome” of B. subtilis."],["dc.identifier.doi","10.3389/fmolb.2019.00032"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16110"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59932"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/H2020/720776/EU//Rafts4Biotech"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","570"],["dc.title","A Survey of Pyridoxal 5′-Phosphate-Dependent Proteins in the Gram-Positive Model Bacterium Bacillus subtilis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1068"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Molecular BioSystems"],["dc.bibliographiccitation.lastpage","1075"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Pietack, Nico"],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T09:30:00Z"],["dc.date.available","2018-11-07T09:30:00Z"],["dc.date.issued","2013"],["dc.description.abstract","In 2003, an initial study on essential genes in the Gram-positive model bacterium described 271 genes as essential. In the past decade, the functions of many unknown genes and their encoded proteins have been elucidated. Moreover, detailed analyses have revealed that 31 genes that were thought to be essential are in fact non-essential whereas 20 novel essential genes have been described. Thus, 261 genes coding for 259 proteins and two functional RNAs are regarded essential as of January 2013. Among the essential proteins, the largest group is involved in protein synthesis, secretion and protein quality control. Other large sets of essential proteins are involved in lipid biosynthesis, cell wall metabolism and cell division, and DNA replication. Another interesting group of essential proteins protects the cell against endogenous toxic proteins, metabolites, or other intermediates. There are only six essential proteins in B. subtilis, for which no function is known. The functional analysis of these important proteins is predicted to be a key issue in the research on this model organism in the coming years."],["dc.identifier.doi","10.1039/c3mb25595f"],["dc.identifier.isi","000318557100003"],["dc.identifier.pmid","23420519"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10469"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31197"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Royal Soc Chemistry"],["dc.relation.issn","1742-206X"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Essential genes in Bacillus subtilis: a re-evaluation after ten years"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e66120"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Stannek, Lorena"],["dc.contributor.author","Care, Rachel A."],["dc.contributor.author","Commichau, Fabian M."],["dc.date.accessioned","2018-11-07T09:23:41Z"],["dc.date.available","2018-11-07T09:23:41Z"],["dc.date.issued","2013"],["dc.description.abstract","Soil bacteria like Bacillus subtilis can cope with many growth conditions by adjusting gene expression and metabolic pathways. Alternatively, bacteria can spontaneously accumulate beneficial mutations or shape their genomes in response to stress. Recently, it has been observed that a B. subtilis mutant lacking the catabolically active glutamate dehydrogenase (GDH), RocG, mutates the cryptic gudB(CR) gene at a high frequency. The suppressor mutants express the active GDH GudB, which can fully replace the function of RocG. Interestingly, the cryptic gudB(CR) allele is stably inherited as long as the bacteria synthesize the functional GDH RocG. Competition experiments revealed that the presence of the cryptic gudB(CR) allele provides the bacteria with a selective growth advantage when glutamate is scarce. Moreover, the lack of exogenous glutamate is the driving force for the selection of mutants that have inactivated the active gudB gene. In contrast, two functional GDHs are beneficial for the cells when glutamate was available. Thus, the amount of GDH activity strongly affects fitness of the bacteria depending on the availability of exogenous glutamate. At a first glance the high mutation frequency of the cryptic gudB(CR) allele might be attributed to stress-induced adaptive mutagenesis. However, other loci on the chromosome that could be potentially mutated during growth under the selective pressure that is exerted on a GDH-deficient mutant remained unaffected. Moreover, we show that a GDH-proficient B. subtilis strain has a strong selective growth advantage in a glutamate-dependent manner. Thus, the emergence and rapid clonal expansion of the active gudB allele can be in fact explained by spontaneous mutation and growth under selection without an increase of the mutation rate. Moreover, this study shows that the selective pressure that is exerted on a maladapted bacterium strongly affects the apparent mutation frequency of mutational hot spots."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2013"],["dc.identifier.doi","10.1371/journal.pone.0066120"],["dc.identifier.isi","000321038800048"],["dc.identifier.pmid","23785476"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9123"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29637"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Selection-Driven Accumulation of Suppressor Mutants in Bacillus subtilis: The Apparent High Mutation Frequency of the Cryptic gudB Gene and the Rapid Clonal Expansion of gudB(+) Suppressors Are Due to Growth under Selection"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Microbiology"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Dormeyer, Miriam"],["dc.contributor.author","Lentes, Sabine"],["dc.contributor.author","Richts, Björn"],["dc.contributor.author","Heermann, Ralf"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Commichau, Fabian M."],["dc.date.accessioned","2020-12-10T18:44:28Z"],["dc.date.available","2020-12-10T18:44:28Z"],["dc.date.issued","2019"],["dc.description.abstract","The Gram-positive soil bacterium Bacillus subtilis relies on the glutamine synthetase and the glutamate synthase for glutamate biosynthesis from ammonium and 2-oxoglutarate. During growth with the carbon source glucose, the LysR-type transcriptional regulator GltC activates the expression of the gltAB glutamate synthase genes. With excess of intracellular glutamate, the gltAB genes are not transcribed because the glutamate-degrading glutamate dehydrogenases (GDHs) inhibit GltC. Previous in vitro studies revealed that 2-oxoglutarate and glutamate stimulate the activator and repressor function, respectively, of GltC. Here, we have isolated GltC variants with enhanced activator or repressor function. The majority of the GltC variants with enhanced activator function differentially responded to the GDHs and to glutamate. The GltC variants with enhanced repressor function were still capable of activating the PgltA promoter in the absence of a GDH. Using PgltA promoter variants (PgltA∗) that are active independent of GltC, we show that the wild type GltC and the GltC variants with enhanced repressor function inactivate PgltA∗ promoters in the presence of the native GDHs. These findings suggest that GltC may also act as a repressor of the gltAB genes in vivo. We discuss a model combining previous models that were derived from in vivo and in vitro experiments."],["dc.identifier.doi","10.3389/fmicb.2019.02321"],["dc.identifier.eissn","1664-302X"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16483"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78464"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","1664-302X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Variants of the Bacillus subtilis LysR-Type Regulator GltC With Altered Activator and Repressor Function"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","129"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Molecular Microbiology and Biotechnology"],["dc.bibliographiccitation.lastpage","140"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Pietack, Nico"],["dc.contributor.author","Becher, Doerte"],["dc.contributor.author","Schmidl, Sebastian R."],["dc.contributor.author","Saier, Milton H."],["dc.contributor.author","Hecker, Michael"],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T08:48:00Z"],["dc.date.available","2018-11-07T08:48:00Z"],["dc.date.issued","2010"],["dc.description.abstract","Phosphorylation is an important mechanism of protein modification. In the Gram-positive soil bacterium Bacillus subtilis, about 5% of all proteins are subject to phosphorylation, and a significant portion of these proteins is phosphorylated on serine or threonine residues. We were interested in the regulation of the basic metabolism in B. subtilis. Many enzymes of the central metabolic pathways are phosphorylated in this organism. In an attempt to identify the responsible protein kinase(s), we identified four candidate kinases, among them the previously studied kinase PrkC. We observed that PrkC is indeed able to phosphorylate several metabolic enzymes in vitro. Determination of the phosphorylation sites revealed a remarkable preference of PrkC for threonine residues. Moreover, PrkC often used several phosphorylation sites in one protein. This feature of PrkC-dependent protein phosphorylation resembles the multiple phosphorylations often observed in eukaryotic proteins. The HPr protein of the phosphotransferase system is one of the proteins phosphorylated by PrkC, and PrkC phosphorylates a site (Ser-12) that has recently been found to be phosphorylated in vivo. The agreement between in vivo and in vitro phosphorylation of HPr on Ser-12 suggests that our in vitro observations reflect the events that take place in the cell. Copyright (C) 2010 S. Karger AG, Basel"],["dc.identifier.doi","10.1159/000308512"],["dc.identifier.isi","000278674200001"],["dc.identifier.pmid","20389117"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9309"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21096"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","1464-1801"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","In vitro Phosphorylation of Key Metabolic Enzymes from Bacillus subtilis: PrkC Phosphorylates Enzymes from Different Branches of Basic Metabolism"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","18"],["dc.bibliographiccitation.journal","Current Opinion in Biotechnology"],["dc.bibliographiccitation.lastpage","29"],["dc.bibliographiccitation.volume","56"],["dc.contributor.author","Acevedo-Rocha, Carlos G."],["dc.contributor.author","Gronenberg, Luisa S."],["dc.contributor.author","Mack, Matthias"],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Genee, Hans J."],["dc.date.accessioned","2019-07-09T11:51:53Z"],["dc.date.available","2019-07-09T11:51:53Z"],["dc.date.issued","2019"],["dc.description.abstract","Vitamins are essential compounds in human and animal diets. Their demand is increasing globally in food, feed, cosmetics, chemical and pharmaceutical industries. Most current production methods are unsustainable because they use non-renewable sources and often generate hazardous waste. Many microorganisms produce vitamins naturally, but their corresponding metabolic pathways are tightly regulated since vitamins are needed only in catalytic amounts. Metabolic engineering is accelerating the development of microbial cell factories for vitamins that could compete with chemical methods that have been optimized over decades, but scientific hurdles remain. Additional technological and regulatory issues need to be overcome for innovative bioprocesses to reach the market. Here, we review the current state of development and challenges for fermentative processes for the B vitamin group."],["dc.identifier.doi","10.1016/j.copbio.2018.07.006"],["dc.identifier.pmid","30138794"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16220"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60034"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/H2020/686070/EU//DD-DeCaF"],["dc.relation","info:eu-repo/grantAgreement/EC/H2020/720776/EU//Rafts4Biotech"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","570"],["dc.title","Microbial cell factories for the sustainable manufacturing of B vitamins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]