Does the detoxification of penicillin side-chain precursors depend on microsomal monooxygenase and glutathione S-transferase in Penicillium chrysogenum?

2003 ◽  
Vol 43 (4) ◽  
pp. 287-300 ◽  
Author(s):  
Tamás Emri ◽  
Brigitta Oláh ◽  
László Sámi ◽  
István Pócsi
Keyword(s):  
Penicillium Chrysogenum ◽  
Side Chain ◽  
Glutathione S Transferase ◽  
Microsomal Monooxygenase

Utilization of side-chain precursors for penicillin biosynthesis in a high-producing strain of Penicillium chrysogenum

1994 ◽  
Vol 40 (6) ◽  
pp. 883-887 ◽  
Author(s):  
Susanne Havn Eriksen ◽  
Bo Jensen ◽  
Ib Schneider ◽  
Svend Kaasgaard ◽  
Jørgen Olsen
Keyword(s):  
Penicillium Chrysogenum ◽  
Side Chain ◽  
Penicillin Biosynthesis

scholarly journals Peroxisomes Are Required for Efficient Penicillin Biosynthesis in Penicillium chrysogenum

2010 ◽  
Vol 76 (17) ◽  
pp. 5702-5709 ◽  
Author(s):  
Wiebe H. Meijer ◽  
Loknath Gidijala ◽  
Susan Fekken ◽  
Jan A. K. W. Kiel ◽  
Marco A. van den Berg ◽  
...  
Keyword(s):  
Penicillium Chrysogenum ◽  
Coenzyme A ◽  
Antibiotic Production ◽  
Hyphal Growth ◽  
Side Chain ◽  
Penicillin Biosynthesis ◽  
Peroxisome Proliferation ◽  
Coa Ligase ◽  
Penicillanic Acid ◽  
Acyl Coenzyme A

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 PEN production. We find that conditions that lead to peroxisome proliferation but simultaneously interfere with the normal physiology of the cell may be detrimental to antibiotic production. We furthermore show that peroxisomes develop in germinating conidiospores from reticule-like structures. During subsequent hyphal growth, peroxisome proliferation occurs at the tip of the growing hyphae, after which the organelles are distributed over newly formed subapical cells. We observed that the organelle proliferation machinery requires the dynamin-like protein Dnm1.

scholarly journals Resolving Phenylalanine Metabolism Sheds Light on Natural Synthesis of Penicillin G in Penicillium chrysogenum

2011 ◽  
Vol 11 (2) ◽  
pp. 238-249 ◽  
Author(s):  
Tânia Veiga ◽  
Daniel Solis-Escalante ◽  
Gabriele Romagnoli ◽  
Angela ten Pierick ◽  
Mark Hanemaaijer ◽  
...  
Keyword(s):  
Nitrogen Source ◽  
Transcriptome Analysis ◽  
Penicillium Chrysogenum ◽  
Penicillin G ◽  
Side Chain ◽  
Acid Decarboxylase ◽  
Content Type ◽  
Chemostat Cultures ◽  
Phenylpyruvate Decarboxylase ◽  
Dual Substrate

ABSTRACTThe industrial production of penicillin G byPenicillium chrysogenumrequires the supplementation of the growth medium with the side chain precursor phenylacetate. The growth ofP. chrysogenumwith phenylalanine as the sole nitrogen source resulted in the extracellular production of phenylacetate and penicillin G. To analyze this natural pathway for penicillin G production, chemostat cultures were switched to [U-13C]phenylalanine as the nitrogen source. The quantification and modeling of the dynamics of labeled metabolites indicated that phenylalanine was (i) incorporated in nascent protein, (ii) transaminated to phenylpyruvate and further converted by oxidation or by decarboxylation, and (iii) hydroxylated to tyrosine and subsequently metabolized via the homogentisate pathway. The involvement of the homogentisate pathway was supported by the comparative transcriptome analysis ofP. chrysogenumcultures grown with phenylalanine and with (NH4)2SO4as the nitrogen source. This transcriptome analysis also enabled the identification of two putative 2-oxo acid decarboxylase genes (Pc13g9300 and Pc18g01490). cDNAs of both genes were cloned and expressed in the 2-oxo-acid-decarboxylase-freeSaccharomyces cerevisiaestrain CEN.PK711-7C (pdc1 pdc5 pdc6Δ aro10Δ thi3Δ). The introduction of Pc13g09300 restored the growth of thisS. cerevisiaemutant on glucose and phenylalanine, thereby demonstrating that Pc13g09300 encodes a dual-substrate pyruvate and phenylpyruvate decarboxylase, which plays a key role in an Ehrlich-type pathway for the production of phenylacetate inP. chrysogenum. These results provide a basis for the metabolic engineering ofP. chrysogenumfor the production of the penicillin G side chain precursor phenylacetate.

An efficient synthesis of δ-(L-α-aminoadipyl)-L-seryl-D-valine (LLD ASV), a naturally occuring tripeptide from the fermentation of Penicillium chrysogenum

1988 ◽  
Vol 53 (11) ◽  
pp. 2854-2856
Author(s):  
Bogdan Liberek ◽  
Regina Kasprzykowska
Keyword(s):  
Efficient Method ◽  
Carboxy Group ◽  
Penicillium Chrysogenum ◽  
Side Chain ◽  
Cephalosporin C ◽  
Efficient Synthesis ◽  
Isopenicillin N

The synthesis of δ-(L-α-aminoadipyl)-L-seryl-D-valine (LLD ASV), a naturally occuring congener of the well known tripeptide δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine (LLD ACV) which is the linear precursor of isopenicillin N, penicillin N, cephalosporin C is described. An efficient method for producing the requisite α-monobenzyl ester of N-benzyloxycarbonyl-L-homoglutamic acid for subsequent condesation at the side chain δ-carboxy group is presented.

Utilization of side-chain precursors for penicillin biosynthesis in a high-producing strain of Penicillium chrysogenum

1994 ◽  
Vol 40 (6) ◽  
pp. 883-887 ◽  
Author(s):  
Susanne Havn Eriksen ◽  
Bo Jensen ◽  
Ib Schneider ◽  
Svend Kaasgaard ◽  
J�rgen Olsen
Keyword(s):  
Penicillium Chrysogenum ◽  
Side Chain ◽  
Penicillin Biosynthesis

Glutathione system participation in thoracic aneurysms from patients with Marfan syndrome

VASA ◽  
2017 ◽  
Vol 46 (3) ◽  
pp. 177-186 ◽  
Author(s):  
Alejandra María Zúñiga-Muñoz ◽  
Israel Pérez-Torres ◽  
Verónica Guarner-Lans ◽  
Elías Núñez-Garrido ◽  
Rodrigo Velázquez Espejel ◽  
...  
Keyword(s):  
Aortic Aneurysm ◽  
Marfan Syndrome ◽  
Aortic Aneurysms ◽  
Aortic Dilatation ◽  
Glutathione S Transferase ◽  
Reduced And Oxidized Glutathione ◽  
Total Antioxidant ◽  
Elevated Activity ◽  
Acute Dissection ◽  
Thoracic Aneurysms

Abstract. Background: Aortic dilatation in Marfan syndrome (MFS) is progressive. It is associated with oxidative stress and endothelial dysfunction that contribute to the early acute dissection of the vessel and can result in rupture of the aorta and sudden death. We evaluated the participation of the glutathione (GSH) system, which could be involved in the mechanisms that promote the formation and progression of the aortic aneurysms in MFS patients. Patients and methods: Aortic aneurysm tissue was obtained during chest surgery from eight control subjects and 14 MFS patients. Spectrophotometrical determination of activity of glutathione peroxidase (GPx), glutathione-S-transferase (GST), glutathione reductase (GR), lipid peroxidation (LPO) index, carbonylation, total antioxidant capacity (TAC), and concentration of reduced and oxidized glutathione (GSH and GSSG respectively), was performed in the homogenate from aortic aneurysm tissue. Results: LPO index, carbonylation, TGF-β1, and GR activity were increased in MFS patients (p < 0.04), while TAC, GSH/GSSG ratio, GPx, and GST activity were significantly decreased (p < 0.04). Conclusions: The depletion of GSH, in spite of the elevated activity of GR, not only diminished the activity of GSH-depend GST and GPx, but increased LPO, carbonylation and decreased TAC. These changes could promote the structural and functional alterations in the thoracic aorta of MFS patients.

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