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Journal articles on the topic 'Penicillin biosynthesis'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 February 2022

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1

Baldwin, Jack E., Edward P. Abraham, Geoffrey L. Burge, and Hong-Hoi Ting. "Penicillin biosynthesis: direct biosynthetic formation of penicillin V and penicillin G." Journal of the Chemical Society, Chemical Communications, no. 24 (1985): 1808. http://dx.doi.org/10.1039/c39850001808.

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2

Spröte, Petra, Axel A. Brakhage, and Michael J. Hynes. "Contribution of Peroxisomes to Penicillin Biosynthesis in Aspergillus nidulans." Eukaryotic Cell 8, no. 3 (2009): 421–23. http://dx.doi.org/10.1128/ec.00374-08.

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ABSTRACT Peroxisomal localization of the third enzyme of the penicillin biosynthesis pathway of Aspergillus nidulans, acyl-coenzyme A:IPN acyltransferase (IAT), is mediated by its atypical peroxisomal targeting signal 1 (PTS1). However, mislocalization of IAT by deletion of either its PTS1 or of genes encoding proteins involved in peroxisome formation or transport does not completely abolish penicillin biosynthesis. This is in contrast to the effects of IAT mislocalization in Penicillium chrysogenum.

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3

Nijland, Jeroen G., Bjorg Ebbendorf, Marta Woszczynska, Rémon Boer, Roel A. L. Bovenberg, and Arnold J. M. Driessen. "Nonlinear Biosynthetic Gene Cluster Dose Effect on Penicillin Production by Penicillium chrysogenum." Applied and Environmental Microbiology 76, no. 21 (2010): 7109–15. http://dx.doi.org/10.1128/aem.01702-10.

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ABSTRACT Industrial penicillin production levels by the filamentous fungus Penicillium chrysogenum increased dramatically by classical strain improvement. High-yielding strains contain multiple copies of the penicillin biosynthetic gene cluster that encodes three key enzymes of the β-lactam biosynthetic pathway. We have analyzed the gene cluster dose effect on penicillin production using the high-yielding P. chrysogenum strain DS17690 that was cured from its native clusters. The amount of penicillin V produced increased with the penicillin biosynthetic gene cluster number but was saturated at

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4

KURZĄTKOWSKI, WIESŁAW, MONIKA STANISZEWSKA, MAŁGORZATA BONDARYK, and ANITA GĘBSKA-KUCZEROWSKA. "Compartmentalization in Penicillin G Biosynthesis by Penicillium chrysogenum PQ-96." Polish Journal of Microbiology 63, no. 4 (2014): 399–408. http://dx.doi.org/10.33073/pjm-2014-054.

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The arrangement of organelles in the sub-apical productive non-growing vacuolated hyphal cells of the high- and the low-penicillin-pro- ducing strains Penicillium chrysogenum was compared using transmission electron microscopy. In the productive cells of the high-yielding strain the endoplasmic reticulum and the polyribosomes with associated peroxisomes are frequently arranged at the periphery of the cytoplasm and around the vacuoles. At the high activity of penicillin G biosynthesis the immuno-label of the cytosolic isopenicillin N synthase is concentrated at the polyribosomes arranged in the

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5

Hajdu, Janos. "PENICILLIN AND CEPHALOSPORIN BIOSYNTHESIS." Biochemical Society Transactions 27, no. 1 (1999): A4. http://dx.doi.org/10.1042/bst027a004.

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6

Hoff, Birgit, Jens Kamerewerd, Claudia Sigl, et al. "Two Components of a velvet-Like Complex Control Hyphal Morphogenesis, Conidiophore Development, and Penicillin Biosynthesis in Penicillium chrysogenum." Eukaryotic Cell 9, no. 8 (2010): 1236–50. http://dx.doi.org/10.1128/ec.00077-10.

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ABSTRACT Penicillium chrysogenum is the industrial producer of the antibiotic penicillin, whose biosynthetic regulation is barely understood. Here, we provide a functional analysis of two major homologues of the velvet complex in P. chrysogenum, which we have named P. chrysogenum velA (PcvelA) and PclaeA. Data from array analysis using a ΔPcvelA deletion strain indicate a significant role of PcVelA on the expression of biosynthesis and developmental genes, including PclaeA. Northern hybridization and high-performance liquid chromatography quantifications of penicillin titers clearly show that

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7

Martín, Jorge, Carlos García-Estrada, Ángel Rumbero, et al. "Characterization of an Autoinducer of Penicillin Biosynthesis in Penicillium chrysogenum." Applied and Environmental Microbiology 77, no. 16 (2011): 5688–96. http://dx.doi.org/10.1128/aem.00059-11.

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ABSTRACTFilamentous fungi produce an impressive variety of secondary metabolites; many of them have important biological activities. The biosynthesis of these secondary metabolites is frequently induced by plant-derived external elicitors and appears to also be regulated by internal inducers, which may work in a way similar to that of bacterial autoinducers. The biosynthesis of penicillin inPenicillium chrysogenumis an excellent model for studying the molecular mechanisms of control of gene expression due to a good knowledge of the biochemistry and molecular genetics of β-lactam antibiotics an

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8

García-Estrada, Carlos, Ricardo V. Ullán, Tania Velasco-Conde, et al. "Post-translational enzyme modification by the phosphopantetheinyl transferase is required for lysine and penicillin biosynthesis but not for roquefortine or fatty acid formation in Penicillium chrysogenum." Biochemical Journal 415, no. 2 (2008): 317–24. http://dx.doi.org/10.1042/bj20080369.

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NRPSs (non-ribosomal peptide synthetases) and PKSs (polyketide synthases) require post-translational phosphopantetheinylation to become active. This reaction is catalysed by a PPTase (4′-phosphopantetheinyl transferase). The ppt gene of Penicillium chrysogenum, encoding a protein that shares 50% similarity with the stand-alone large PPTases, has been cloned. This gene is present as a single copy in the genome of the wild-type and high-penicillin-producing strains (containing multiple copies of the penicillin gene cluster). Amplification of the ppt gene produced increases in isopenicillin N and

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9

van de Kamp, Mart, Theo A. Schuurs, Arnold Vos, Ted R. van der Lende, Wil N. Konings, and Arnold J. M. Driessen. "Sulfur Regulation of the Sulfate Transporter GenessutA and sutB in Penicillium chrysogenum." Applied and Environmental Microbiology 66, no. 10 (2000): 4536–38. http://dx.doi.org/10.1128/aem.66.10.4536-4538.2000.

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ABSTRACT Penicillium chrysogenum uses sulfate as a source of sulfur for the biosynthesis of penicillin. Sulfate uptake and the mRNA levels of the sulfate transporter-encoding sutB andsutA genes are all reduced by high sulfate concentrations and are elevated by sulfate starvation. In a high-penicillin-yielding strain, sutB is effectively transcribed even in the presence of excess sulfate. This deregulation may facilitate the efficient incorporation of sulfur into cysteine and penicillin.

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10

Lu, Ying, Robert L. Mach, Karin Affenzeller та Christian P. Kubicek. "Regulation of α-aminoadipate reductase from Penicillium chrysogenum in relation to the flux from α-aminoadipate into penicillin biosynthesis". Canadian Journal of Microbiology 38, № 8 (1992): 758–63. http://dx.doi.org/10.1139/m92-123.

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The activity and regulation of α-aminoadipate reductase in three Penicillium chrysogenum strains (Q176, D6/1014/A, and P2), producing different amounts of penicillin, were studied. The enzyme exhibited decreasing affinity for α-aminoadipate with increasing capacity of the respective strain to produce penicillin. The enzyme from all three strains was inhibited by L-lysine, and the enzyme from the lowest producer, Q176, was least sensitive. Between pH 7.5 and 6.5, inhibition of α-aminoadipate reductase by L-lysine was pH dependent, being more pronounced at lower pH. The highest producer strain,

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11

Jaklitsch, W. M., W. Hampel, M. Röhr, C. P. Kubicek та G. Gamerith. "α-Aminoadipate pool concentration and penicillin biosynthesis in strains of Penicillium chrysogenum". Canadian Journal of Microbiology 32, № 6 (1986): 473–80. http://dx.doi.org/10.1139/m86-087.

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Intracellular amino acid pools in four Penicillium chrysogenum strains, which differed in their ability to produce penicillin, were determined under conditions supporting growth without penicillin production and under conditions supporting penicillin production. A significant correlation between the rate of pencillin production and the intracellular concentration of α-aminoadipate was observed, which was not shown with any other amino acid in the pool. In replacement cultivation, penicillin production was stimulated by α-aminoadipate, but not by valine or cysteine. Exogenously added α-aminoadi

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12

Brakhage, Axel A. "Molecular Regulation of β-Lactam Biosynthesis in Filamentous Fungi". Microbiology and Molecular Biology Reviews 62, № 3 (1998): 547–85. http://dx.doi.org/10.1128/mmbr.62.3.547-585.1998.

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SUMMARY The most commonly used β-lactam antibiotics for the therapy of infectious diseases are penicillin and cephalosporin. Penicillin is produced as an end product by some fungi, most notably by Aspergillus (Emericella) nidulans and Penicillium chrysogenum. Cephalosporins are synthesized by both bacteria and fungi, e.g., by the fungus Acremonium chrysogenum (Cephalosporium acremonium). The biosynthetic pathways leading to both secondary metabolites start from the same three amino acid precursors and have the first two enzymatic reactions in common. Penicillin biosynthesis is catalyzed by thr

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13

Scheckhuber, Christian Q., Marten Veenhuis, and Ida J. van der Klei. "Improving penicillin biosynthesis in Penicillium chrysogenum by glyoxalase overproduction." Metabolic Engineering 18 (July 2013): 36–43. http://dx.doi.org/10.1016/j.ymben.2013.04.003.

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14

Laich, Federico, Francisco Fierro, Rosa Elena Cardoza, and Juan F. Martin. "Organization of the Gene Cluster for Biosynthesis of Penicillin in Penicillium nalgiovense and Antibiotic Production in Cured Dry Sausages." Applied and Environmental Microbiology 65, no. 3 (1999): 1236–40. http://dx.doi.org/10.1128/aem.65.3.1236-1240.1999.

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ABSTRACT Several fungal isolates obtained from two cured meat products from Spain were identified as Penicillium nalgiovense by their morphological features and by DNA fingerprinting. All P. nalgiovense isolates showed antibiotic activity in agar diffusion assays, and their penicillin production in liquid complex medium ranged from 6 to 38 μg · ml−1. We constructed a restriction map of the penicillin gene cluster of P. nalgiovense and found that the organization of the penicillin biosynthetic genes (pcbAB, pcbC, andpenDE) is the same as in Penicillium chrysogenum and Aspergillus nidulans. Thep

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15

Teijeira, Fernando, Ricardo V. Ullán, Susana M. Guerra, Carlos García-Estrada, Inmaculada Vaca, and Juan F. Martín. "The transporter CefM involved in translocation of biosynthetic intermediates is essential for cephalosporin production." Biochemical Journal 418, no. 1 (2009): 113–24. http://dx.doi.org/10.1042/bj20081180.

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The cluster of early cephalosporin biosynthesis genes (pcbAB, pcbC, cefD1, cefD2 and cefT of Acremonium chrysogenum) contains all of the genes required for the biosynthesis of the cephalosporin biosynthetic pathway intermediate penicillin N. Downstream of the cefD1 gene, there is an unassigned open reading frame named cefM encoding a protein of the MFS (major facilitator superfamily) with 12 transmembrane domains, different from the previously reported cefT. Targeted inactivation of cefM by gene replacement showed that it is essential for cephalosporin biosynthesis. The disrupted mutant accumu

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16

Meijer, Wiebe H., Loknath Gidijala, Susan Fekken, et al. "Peroxisomes Are Required for Efficient Penicillin Biosynthesis in Penicillium chrysogenum." Applied and Environmental Microbiology 76, no. 17 (2010): 5702–9. http://dx.doi.org/10.1128/aem.02327-09.

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ABSTRACT In the fungus Penicillium chrysogenum, penicillin (PEN) production is compartmentalized in the cytosol and in peroxisomes. Here we show that intact peroxisomes that contain the two final enzymes of PEN biosynthesis, acyl coenzyme A (CoA):6-amino penicillanic acid acyltransferase (AT) as well as the side-chain precursor activation enzyme phenylacetyl CoA ligase (PCL), are crucial for efficient PEN synthesis. Moreover, increasing PEN titers are associated with increasing peroxisome numbers. However, not all conditions that result in enhanced peroxisome numbers simultaneously stimulate P

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17

Šmidák, Roman, Martina Kralovičová, Beatrica Ševčíková, et al. "Sequence analysis and gene amplification study of the penicillin biosynthesis gene cluster from different strains of Penicillium chrysogenum." Biologia 65, no. 1 (2010): 1–6. http://dx.doi.org/10.2478/s11756-009-0216-2.

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AbstractIndustrial strains of Penicillium chrysogenum possess many genomic changes leading to higher levels of penicillin. In this work several production and wild-type strains of Penicillium chrysogenum were used in comparative nucleotide sequence analysis of the biosynthesis cluster. The alignments confirmed sequence conservation not only in promoter regions of the biosynthesis genes but also throughout the entire 44.7-kbp genomic fragment comprising the whole biosynthesis cluster with 15.5-kbp and 13.1-kbp flanking regions. As another titre-enhancing mechanism we subsequently examined gene

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18

García-Estrada, Carlos, Juan F. Martín, Laura Cueto, and Carlos Barreiro. "Omics Approaches Applied to Penicillium chrysogenum and Penicillin Production: Revealing the Secrets of Improved Productivity." Genes 11, no. 6 (2020): 712. http://dx.doi.org/10.3390/genes11060712.

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Penicillin biosynthesis by Penicillium chrysogenum is one of the best-characterized biological processes from the genetic, molecular, biochemical, and subcellular points of view. Several omics studies have been carried out in this filamentous fungus during the last decade, which have contributed to gathering a deep knowledge about the molecular mechanisms underlying improved productivity in industrial strains. The information provided by these studies is extremely useful for enhancing the production of penicillin or other bioactive secondary metabolites by means of Biotechnology or Synthetic B

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19

Brakhage, A. A., P. Browne, and G. Turner. "Regulation of Aspergillus nidulans penicillin biosynthesis and penicillin biosynthesis genes acvA and ipnA by glucose." Journal of Bacteriology 174, no. 11 (1992): 3789–99. http://dx.doi.org/10.1128/jb.174.11.3789-3799.1992.

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20

Schofield, Christopher J., Jack E. Baldwin, Michael F. Byford, et al. "Proteins of the penicillin biosynthesis pathway." Current Opinion in Structural Biology 7, no. 6 (1997): 857–64. http://dx.doi.org/10.1016/s0959-440x(97)80158-3.

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21

Müller, Wally H., Roelof A. L. Bovenberg, Marloes H. Groothuis, et al. "Involvement of microbodies in penicillin biosynthesis." Biochimica et Biophysica Acta (BBA) - General Subjects 1116, no. 2 (1992): 210–13. http://dx.doi.org/10.1016/0304-4165(92)90118-e.

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22

Müller, W. H., T. P. van der Krift, A. J. Krouwer, et al. "Localization of the pathway of the penicillin biosynthesis in Penicillium chrysogenum." EMBO Journal 10, no. 2 (1991): 489–95. http://dx.doi.org/10.1002/j.1460-2075.1991.tb07971.x.

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23

Campos, C., T. G. Lázaro-Rodríguez, E. Hernández-Pérez, R. Rincón-Heredia, and F. J. Fernández. "Pexophagy modes during penicillin biosynthesis in Penicillium rubens P2-32-T." Archives of Microbiology 202, no. 8 (2020): 2337–41. http://dx.doi.org/10.1007/s00203-020-01939-3.

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24

Martín, Juan-Francisco, Carlos García-Estrada та Ricardo V. Ullán. "Transport of substrates into peroxisomes: the paradigm of β-lactam biosynthetic intermediates". BioMolecular Concepts 4, № 2 (2013): 197–211. http://dx.doi.org/10.1515/bmc-2012-0048.

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AbstractPeroxisomes are ubiquitous organelles that enclose catalases, fatty acid-oxidizing enzymes, and a variety of proteins involved in different cellular processes. Interestingly, the late enzymes involved in penicillin biosynthesis, and the isopenicillin N epimerization enzymes involved in cephalosporin biosynthesis are located inside peroxisomes in the producer fungi Penicillium chrysogenum and Acremonium chrysogenum. Peroxisome proteins are targeted to those organelles by peroxisomal targeting signals located at the C-terminus (PTS1) or near the N-terminal end (PTS2) of those proteins. P

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25

Wiharyani, Risma, Dudi Hardianto, Hermin Pancasakti Kusumaningrum, and Anto Budiharjo. "Kloning Gen pcbC dari Penicillium chrysogenum ke dalam Plasmid pPICZA untuk Pengembangan Produksi Penisilin G." Bioma : Berkala Ilmiah Biologi 16, no. 1 (2014): 33. http://dx.doi.org/10.14710/bioma.16.1.33-38.

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Availability of drugs in Indonesia is still limited by the high prices of drugs due to on the imported raw materials that reaches 95%. Developing antibiotic raw materials can be achieved by increasing of penicillin G production, which is the raw material for the formation of semisynthetic penicillin derivatives through the production of 6-aminopenisillanic acid (6-APA). One of the important enzyme in the penicillin G biosynthesis is Isopenisilin N Synthase (IPNS) that encodes by pcbC gene on Penicillium chrysogenum. This study aimed to obtain a recombinant of pcbC gene fragments that is insert

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26

Peñalva, Miguel A., Robert T. Rowlands, and Geoffrey Turner. "The optimization of penicillin biosynthesis in fungi." Trends in Biotechnology 16, no. 11 (1998): 483–89. http://dx.doi.org/10.1016/s0167-7799(98)01229-3.

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27

Queener, S. W. "Molecular biology of penicillin and cephalosporin biosynthesis." Antimicrobial Agents and Chemotherapy 34, no. 6 (1990): 943–48. http://dx.doi.org/10.1128/aac.34.6.943.

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28

Kopke, Katarina, Birgit Hoff, Sandra Bloemendal, Alexandra Katschorowski, Jens Kamerewerd, and Ulrich Kück. "Members of the Penicillium chrysogenum Velvet Complex Play Functionally Opposing Roles in the Regulation of Penicillin Biosynthesis and Conidiation." Eukaryotic Cell 12, no. 2 (2012): 299–310. http://dx.doi.org/10.1128/ec.00272-12.

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ABSTRACT A velvet multisubunit complex was recently detected in the filamentous fungus Penicillium chrysogenum , the major industrial producer of the β-lactam antibiotic penicillin. Core components of this complex are P. chrysogenum VelA (PcVelA) and PcLaeA, which regulate secondary metabolite production, hyphal morphology, conidiation, and pellet formation. Here we describe the characterization of PcVelB, PcVelC, and PcVosA as novel subunits of this velvet complex. Using yeast two-hybrid analysis and bimolecular fluorescence complementation (BiFC), we demonstrate that all velvet proteins are

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29

Brakhage, Axel A., and Geoffrey Turner. "l-Lysine repression of penicillin biosynthesis and the expression of penicillin biosynthesis genes acvA and ipnA inAspergillus nidulans." FEMS Microbiology Letters 98, no. 1-3 (1992): 123–27. http://dx.doi.org/10.1111/j.1574-6968.1992.tb05500.x.

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30

Brakhage, A. "?-Lysine repression of penicillin biosynthesis and the expression of penicillin biosynthesis genes acvA and ipnA in Aspergillus nidulans." FEMS Microbiology Letters 98, no. 1-3 (1992): 123–27. http://dx.doi.org/10.1016/0378-1097(92)90142-b.

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31

Trzciński, Krzysztof, Adam MacNeil, Keith P. Klugman, and Marc Lipsitch. "Capsule Homology Does Not Increase the Frequency of Transformation of Linked Penicillin Binding Proteins PBP 1a and PBP 2x in Streptococcus pneumoniae." Antimicrobial Agents and Chemotherapy 49, no. 4 (2005): 1591–92. http://dx.doi.org/10.1128/aac.49.4.1591-1592.2005.

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ABSTRACT Penicillin resistance is mainly confined to a limited number of Streptococcus pneumoniae serotypes. Given linkage between the capsular biosynthesis locus and two penicillin binding proteins, we tested whether capsule homology increases transformation rates of penicillin resistance. Transformation rates in homologous donor-recipient pairs were no higher than expected, falsifying this hypothesis.

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32

Teves, Franco, Mónica Lamas-Maceiras, Carlos García-Estrada, et al. "Transcriptional upregulation of four genes of the lysine biosynthetic pathway by homocitrate accumulation in Penicillium chrysogenum: homocitrate as a sensor of lysine-pathway distress." Microbiology 155, no. 12 (2009): 3881–92. http://dx.doi.org/10.1099/mic.0.031005-0.

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The lysine biosynthetic pathway has to supply large amounts of α-aminoadipic acid for penicillin biosynthesis in Penicillium chrysogenum. In this study, we have characterized the P. chrysogenum L2 mutant, a lysine auxotroph that shows highly increased expression of several lysine biosynthesis genes (lys1, lys2, lys3, lys7). The L2 mutant was found to be deficient in homoaconitase activity since it was complemented by the Aspergillus nidulans lysF gene. We have cloned a gene (named lys3) that complements the L2 mutation by transformation with a P. chrysogenum genomic library, constructed in an

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33

Koetsier, Martijn J., Peter A. Jekel, Marco A. van den Berg, Roel A. L. Bovenberg, and Dick B. Janssen. "Characterization of a phenylacetate–CoA ligase from Penicillium chrysogenum." Biochemical Journal 417, no. 2 (2008): 467–76. http://dx.doi.org/10.1042/bj20081257.

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Enzymatic activation of PAA (phenylacetic acid) to phenylacetyl-CoA is an important step in the biosynthesis of the β-lactam antibiotic penicillin G by the fungus Penicillium chrysogenum. CoA esters of PAA and POA (phenoxyacetic acid) act as acyl donors in the exchange of the aminoadipyl side chain of isopenicillin N to produce penicillin G or penicillin V. The phl gene, encoding a PCL (phenylacetate–CoA ligase), was cloned in Escherichia coli as a maltose-binding protein fusion and the biochemical properties of the enzyme were characterized. The recombinant fusion protein converted PAA into p

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34

Cohen, G., A. Argaman, R. Schreiber, M. Mislovati, and Y. Aharonowitz. "The thioredoxin system of Penicillium chrysogenum and its possible role in penicillin biosynthesis." Journal of Bacteriology 176, no. 4 (1994): 973–84. http://dx.doi.org/10.1128/jb.176.4.973-984.1994.

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35

Baldwin, Jack E., Robert M. Adlington, Nicholas G. Robinson та Hong-Hoi Ting. "Stereospecificity of β-lactam formation in penicillin biosynthesis". J. Chem. Soc., Chem. Commun., № 5 (1986): 409–11. http://dx.doi.org/10.1039/c39860000409.

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36

Baldwin, Jack E., Robert M. Adlington, Juliette W. Bird, and Christopher J. Schofield. "The fate of valine-oxygen during penicillin biosynthesis." Journal of the Chemical Society, Chemical Communications, no. 21 (1989): 1615. http://dx.doi.org/10.1039/c39890001615.

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37

Casqueiro, Javier, Santiago Gutiérrez, Oscar Bañuelos, Maria Jose Hijarrubia, and Juan Francisco Martín. "Gene Targeting in Penicillium chrysogenum: Disruption of the lys2 Gene Leads to Penicillin Overproduction." Journal of Bacteriology 181, no. 4 (1999): 1181–88. http://dx.doi.org/10.1128/jb.181.4.1181-1188.1999.

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ABSTRACT Two strategies have been used for targeted integration at thelys2 locus of Penicillium chrysogenum. In the first strategy the disruption of lys2 was obtained by a single crossing over between the endogenous lys2 and a fragment of the same gene located in an integrative plasmid.lys2-disrupted mutants were obtained with 1.6% efficiency when the lys2 homologous region was 4.9 kb, but no homologous integration was observed with constructions containing a shorter homologous region. Similarly,lys2-disrupted mutants were obtained by a double crossing over (gene replacement) with an efficienc

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38

Smith, Anthony M., and Keith P. Klugman. "Alterations in MurM, a Cell Wall Muropeptide Branching Enzyme, Increase High-Level Penicillin and Cephalosporin Resistance in Streptococcus pneumoniae." Antimicrobial Agents and Chemotherapy 45, no. 8 (2001): 2393–96. http://dx.doi.org/10.1128/aac.45.8.2393-2396.2001.

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ABSTRACT We report that alteration in MurM, an enzyme involved in the biosynthesis of branched-stem cell wall muropeptides, is required for maximal expression of penicillin and cefotaxime resistance in the pneumococcus. Hungarian isolate 3191 (penicillin MIC, 16 μg/ml; cefotaxime MIC, 4 μg/ml) was a source of donor DNA in transformation experiments. Penicillin-binding protein DNA was insufficient to transform recipient strain R6 to full resistance. Further transformation with altered murM DNA was required for full expression of donor penicillin and cefotaxime resistance.

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39

Rodrı́guez-Sáiz, M., J. L. Barredo, M. A. Moreno, J. M. Fernández-Cañón, M. A. Peñalva, and B. Dı́ez. "Reduced Function of a Phenylacetate-Oxidizing Cytochrome P450 Caused Strong Genetic Improvement in Early Phylogeny of Penicillin-Producing Strains." Journal of Bacteriology 183, no. 19 (2001): 5465–71. http://dx.doi.org/10.1128/jb.183.19.5465-5471.2001.

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ABSTRACT The single-copy pahA gene from Penicillium chrysogenum encodes a phenylacetate 2-hydroxylase that catalyzes the first step of phenylacetate catabolism, an oxidative route that decreases the precursor availability for penicillin G biosynthesis. PahA protein is homologous to cytochrome P450 monooxygenases involved in the detoxification of xenobiotic compounds, with 84% identity to the Aspergillus nidulans homologue PhacA. Expression level of pahA displays an inverse correlation with the penicillin productivity of the strain and is subject to induction by phenylacetic acid. Gene expressi

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40

Martín, Juan F. "Insight into the Genome of Diverse Penicillium chrysogenum Strains: Specific Genes, Cluster Duplications and DNA Fragment Translocations." International Journal of Molecular Sciences 21, no. 11 (2020): 3936. http://dx.doi.org/10.3390/ijms21113936.

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Background: There are eighteen species within the Penicillium genus section chrysogena, including the original penicillin producers Penicillium notatum (Fleming strain) and Penicillium chrysogenum NRRL 1951. Other wild type isolates of the Penicillium genus are relevant for the production of useful proteins and primary or secondary metabolites. The aim of this article is to characterize strain specific genes and those genes which are involved in secondary metabolite biosynthesis, particularly the mutations that have been introduced during the β-lactams strain improvement programs. Results: The

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Román-Hurtado, Fernando, Marina Sánchez-Hidalgo, Jesús Martín, et al. "One Pathway, Two Cyclic Non-ribosomal Pentapeptides: Heterologous Expression of BE-18257 Antibiotics and Pentaminomycins from Streptomyces cacaoi CA-170360." Microorganisms 9, no. 1 (2021): 135. http://dx.doi.org/10.3390/microorganisms9010135.

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The strain Streptomyces cacaoi CA-170360 produces the cyclic pentapeptides pentaminomycins A–H and BE-18257 A–C, two families of cyclopeptides synthesized by two non-ribosomal peptide synthetases encoded in tandem within the same biosynthetic gene cluster. In this work, we have cloned and confirmed the heterologous expression of this biosynthetic gene cluster, demonstrating that each of the non-ribosomal peptide synthetases present in the cluster is involved in the biosynthesis of each group of cyclopeptides. In addition, we discuss the involvement of a stand-alone enzyme belonging to the Peni

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42

Román-Hurtado, Fernando, Marina Sánchez-Hidalgo, Jesús Martín, et al. "One Pathway, Two Cyclic Non-Ribosomal Pentapeptides: Heterologous Expression of BE-18257 Antibiotics and Pentaminomycins from Streptomyces cacaoi CA-170360." Microorganisms 9, no. 1 (2021): 135. http://dx.doi.org/10.3390/microorganisms9010135.

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Abstract:

The strain Streptomyces cacaoi CA-170360 produces the cyclic pentapeptides pentaminomycins A–H and BE-18257 A–C, two families of cyclopeptides synthesized by two non-ribosomal peptide synthetases encoded in tandem within the same biosynthetic gene cluster. In this work, we have cloned and confirmed the heterologous expression of this biosynthetic gene cluster, demonstrating that each of the non-ribosomal peptide synthetases present in the cluster is involved in the biosynthesis of each group of cyclopeptides. In addition, we discuss the involvement of a stand-alone enzyme belonging to the Peni

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43

Baldwin, Jack E., Robert M. Adlington, H.-H. Ting, Duilio Arigoni, Paul Graf, and Bruno Martinoni. "Penicillin biosynthesis the immediate origin of the sulphur atom." Tetrahedron 41, no. 16 (1985): 3339–43. http://dx.doi.org/10.1016/s0040-4020(01)96685-2.

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Baldwin, Jack E., Robert M. Adlington, Barbara P. Domayne-Hayman, Hong-Hoi Ting, and Nicholas J. Turner. "Stereospecificity of carbon–sulphur bond formation in penicillin biosynthesis." J. Chem. Soc., Chem. Commun., no. 2 (1986): 110–13. http://dx.doi.org/10.1039/c39860000110.

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Brakhage, Axel A. "Molecular regulation of penicillin biosynthesis in Aspergillus (Emericella) nidulans." FEMS Microbiology Letters 148, no. 1 (2006): 1–10. http://dx.doi.org/10.1111/j.1574-6968.1997.tb10258.x.

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Martin, Juan F. "Cloning of genes involved in penicillin and cephalosporin biosynthesis." Trends in Biotechnology 5, no. 11 (1987): 306–8. http://dx.doi.org/10.1016/0167-7799(87)90082-5.

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Van den Brulle, Jan, Stefan Steidl, and Axel A. Brakhage. "Cloning and Characterization of anAspergillus nidulans Gene Involved in the Regulation of Penicillin Biosynthesis." Applied and Environmental Microbiology 65, no. 12 (1999): 5222–28. http://dx.doi.org/10.1128/aem.65.12.5222-5228.1999.

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ABSTRACT To identify regulators of penicillin biosynthesis, a previously isolated mutant of Aspergillus nidulans (Prg-1) which carried the trans-acting prgA1 mutation was used. This mutant also contained fusions of the penicillin biosynthesis genes acvA and ipnA with reporter genes (acvA-uidA andipnA-lacZ) integrated in a double-copy arrangement at the chromosomal argB gene. TheprgA1 mutant strain exhibited only 20 to 50% of theipnA-lacZ and acvA-uidAexpression exhibited by the wild-type strain and had only 20 to 30% of the penicillin produced by the wild-type strain. Here, using complementati

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Cantoral, J. M., S. Gutiérrez, F. Fierro, S. Gil-Espinosa, H. van Liempt, and J. F. Martín. "Biochemical characterization and molecular genetics of nine mutants of Penicillium chrysogenum impaired in penicillin biosynthesis." Journal of Biological Chemistry 268, no. 1 (1993): 737–44. http://dx.doi.org/10.1016/s0021-9258(18)54214-9.

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García-Rico, Ramón O., Francisco Fierro, Elba Mauriz, Ana Gómez, María Ángeles Fernández-Bodega та Juan F. Martín. "The heterotrimeric Gα protein Pga1 regulates biosynthesis of penicillin, chrysogenin and roquefortine in Penicillium chrysogenum". Microbiology 154, № 11 (2008): 3567–78. http://dx.doi.org/10.1099/mic.0.2008/019091-0.

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Herrmann, Martina, Petra Spröte, and Axel A. Brakhage. "Protein Kinase C (PkcA) of Aspergillus nidulans Is Involved in Penicillin Production." Applied and Environmental Microbiology 72, no. 4 (2006): 2957–70. http://dx.doi.org/10.1128/aem.72.4.2957-2970.2006.

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ABSTRACT The biosynthesis of the β-lactam antibiotic penicillin in the filamentous fungus Aspergillus nidulans is catalyzed by three enzymes that are encoded by the acvA, ipnA, and aatA genes. A variety of cis-acting DNA elements and regulatory factors form a complex regulatory network controlling these β-lactam biosynthesis genes. Regulators involved include the CCAAT-binding complex AnCF and AnBH1. AnBH1 acts as a repressor of the penicillin biosynthesis gene aatA. Until now, however, little information has been available on the signal transduction cascades leading to the transcription facto

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