L-Rhamnose metabolism in Pichia stipitis and Debaryomyces polymorphus

1994 ◽  
Vol 40 (11) ◽  
pp. 896-902 ◽  
Author(s):  
A. L. Twerdochlib ◽  
F. O. Pedrosa ◽  
S. Funayama ◽  
L. U. Rigo
Keyword(s):  
Carbon Source ◽  
Aldehyde Dehydrogenase ◽  
Enzyme Induction ◽  
Catabolite Repression ◽  
Sole Carbon Source ◽  
Pichia Stipitis ◽  
Oxidative Pathway ◽  
Debaryomyces Polymorphus

The pathway for the breakdown of L-rhamnose by the yeast Pichia stipitis NRC 5568 was shown to involve nonphosphorylated intermediates and to produce pyruvate and L-lactaldehyde. The activities of the enzymes and the nature of several intermediates were determined. The enzymes involved are L-rhamnose dehydrogenase, L-rhamnonate dehydratase, and 2-keto-3-deoxy-L-rhamnonate aldolase. This pathway was found to be inducible by L-rhamnose and repressed by D-glucose. These enzymes were also present in a mutant of P. stipitis (PR1) resistant to catabolite repression and in Debaryomyces polymorphus 1747. Cell-free extracts of P. stipitis and D. polymorphus grown in L-rhamnose as sole carbon source were found to contain NAD+-dependent aldehyde dehydrogenase activities.Key words: Pichia stipitis, enzyme induction, oxidative pathway, catabolite repression.

scholarly journals Azotobacter vinelandii Aldehyde Dehydrogenase Regulated by ς54: Role in Alcohol Catabolism and Encystment

2001 ◽  
Vol 183 (21) ◽  
pp. 6169-6174 ◽  
Author(s):  
Socorro Gama-Castro ◽  
Cinthia Núñez ◽  
Daniel Segura ◽  
Soledad Moreno ◽  
Josefina Guzmán ◽  
...  
Keyword(s):  
Carbon Source ◽  
Aldehyde Dehydrogenase ◽  
Bacterial Growth ◽  
Sole Carbon Source ◽  
Azotobacter Vinelandii ◽  
Gene Encoding ◽  
In Cells

ABSTRACT Encystment in Azotobacter vinelandii is induced byn-butanol or β-hydroxybutyrate (BHB). We identified a gene, encoding an aldehyde dehydrogenase, that was namedaldA. An aldA mutation impaired bacterial growth on n-butanol, ethanol, or hexanol as the sole carbon source. Expression of aldA increased in cells shifted from sucrose to n-butanol and was shown to be dependent on the alternative ς54 factor. A mutation in rpoNencoding the ς54 factor also impaired growth on alcohols. Encystment on n-butanol, but not on BHB, was impaired inaldA or rpoN mutants, indicating thatn-butanol is not an inducer of encystment by itself but must be catabolized in order to induce encystment.

scholarly journals Effect of deregulation of repressor-specific carbon catabolite repression on carbon source consumption in Escherichia coli

2021 ◽  
Vol 64 (1) ◽  
Author(s):  
Hyeon Jeong Seong ◽  
Yu-Sin Jang
Keyword(s):  
Escherichia Coli ◽  
Carbon Source ◽  
Catabolite Repression ◽  
Sole Carbon Source ◽  
Carbon Catabolite Repression ◽  
Cell Factory ◽  
Essential Information ◽  
E Coli ◽  
Marine Biomass ◽  
Galactose Utilization

AbstractEscherichia coli has been used as a host to construct the cell factory for biobased production of chemicals from renewable feedstocks. Because galactose is found in marine biomass as a major component, the strategy for galactose utilization in E. coli has been gained more attention. Although galactose and glucose co-fermentation has been reported using the engineered E. coli strain, few reports have covered fermentation supplemented with galactose as a sole carbon source in the mutant lacking the repressor-specific carbon catabolite repression (CCR). Here, we report the effects of the deregulation of the repressor-specific CCR (galR− and galS−) in fermentation supplemented with galactose as a sole carbon source, using the engineered E. coli strains. In the fermentation using the galR− and galS− double mutant (GR2 strain), an increase of rates in sugar consumption and cell growth was observed compared to the parent strain. In the glucose fermentation, wild-type W3110 and its mutant GR2 and GR2PZ (galR−, galS−, pfkA−, and zwf−) consumed sugar at a higher rate than those values obtained from galactose fermentation. However, the GR2P strain (galR−, galS−, and pfkA−) showed no difference between fermentations using glucose and galactose as a sole carbon source. This study provides essential information for galactose fermentation using the CCR-deregulated E. coli strains.

Induction, purification, and characterization of two extracellular α-L-arabinofuranosidases from Fusarium oxysporum

2003 ◽  
Vol 49 (10) ◽  
pp. 639-644 ◽  
Author(s):  
Gianni Panagiotou ◽  
Evagelos Topakas ◽  
Lina Economou ◽  
Dimitris Kekos ◽  
Basil J Macris ◽  
...  
Keyword(s):  
Carbon Source ◽  
Sugar Beet ◽  
Fusarium Oxysporum ◽  
Enzyme Induction ◽  
Enzyme Purification ◽  
Sole Carbon Source ◽  
Purification And Characterization ◽  
Optimal Activity ◽  
Molecular Masses

In the presence of L-arabinose as sole carbon source, Fusarium oxysporum produces two α-L-arabinofuranosidases (ABFs) named ABF1 and ABF2, with molecular masses of 200 and 180 kDa, respectively. The two F. oxysporum proteins have been purified to homogeneity. The purified enzymes are composed of three equal subunits and are neutral proteins with pIs of 6.0 and 7.3 for ABF1 and ABF2, respectively. With p-nitrophenyl α-L-arabinofuranoside (pNPA) as the substrate, ABF1 and ABF2 exhibited Km values of 0.39 and 0.28 mmol·L–1, respectively, and Vmax values of 1.6 and 4.6 µmol·min–1·(mg of protein)–1, respectively, and displayed optimal activity at pH 6.0 and 50–60 °C. ABFs released arabinose only from sugar beet arabinan and not from wheat soluble and insoluble arabinoxylans. The enzymes were not active on substrates containing ferulic acid ester linked to C-5 and C-2 linkages of pNPA showing that phenolic substituents of pNPA sterically hindered the action of ABFs.Key words: α-L-arabinofuranosidase, enzyme purification, enzyme induction.

Pichia stipitisL-rhamnose dehydrogenase and a catabolite-resistant mutant able to utilize 2-deoxy-D-glucose

1992 ◽  
Vol 38 (5) ◽  
pp. 417-422 ◽  
Author(s):  
E. H. Pardo ◽  
S. Funayama ◽  
F. O. Pedrosa ◽  
L. U. Rigo
Keyword(s):  
Carbon Source ◽  
Sole Carbon Source ◽  
Glucose Repression ◽  
Resistant Mutant ◽  
Pichia Stipitis ◽  
Enzyme Synthesis ◽  
Selective Medium ◽  
Wild Type ◽  
Dehydrogenase Enzyme ◽  
In The Wild

The yeast Pichia stipitis, strain NRC 5568, when grown on L-rhamnose as sole carbon source produced an NAD+-dependent L-rhamnose dehydrogenase enzyme, which is repressed by D-glucose. Mutants defective in carbon catabolite repression were isolated, using a selective medium containing 2-deoxy-D-glucose. Six of eight mutants resistant to 2-deoxy-D-glucose showed L-rhamnose dehydrogenase synthesis insensitive to D-glucose repression. All eight mutants, named PR mutants, as well as the parent strain, were found to grow on D-glucose, L-rhamnose, and glycerol. In addition, they were all capable of growing on 2-deoxy-D-glucose as sole carbon source, D-Glucose and 2-deoxy-D-glucose caused almost complete inhibition of L-rhamnose dehydrogenase synthesis in the wild-type strain but only a slight decrease in the enzyme synthesis in the mutant strain PR1. The wild-type and mutant strains showed the same pattern of inhibition by cycloheximide, 8-hydroxyquinoline, and benomyl. Key words: Pichia stipitis, L-rhamnose dehydrogenase, catabolite-resistant mutant, 2-deoxy-D-glucose.

scholarly journals The Wide-Domain Carbon Catabolite Repressor CreA Indirectly Controls Expression of the Aspergillus nidulans xlnBGene, Encoding the Acidic Endo-β-(1,4)-Xylanase X24

2001 ◽  
Vol 183 (5) ◽  
pp. 1517-1523 ◽  
Author(s):  
Margarita Orejas ◽  
Andrew P. MacCabe ◽  
JoséAntonio Pérez-González ◽  
Sudeep Kumar ◽  
Daniel Ramón
Keyword(s):  
Carbon Source ◽  
Aspergillus Nidulans ◽  
Catabolite Repression ◽  
Sole Carbon Source ◽  
Carbon Catabolite Repression ◽  
Target Sites ◽  
Wide Domain ◽  
Catabolite Repressor ◽  
Functional Analyses

ABSTRACT The Aspergillus nidulans xlnB gene, which encodes the acidic endo-β-(1,4)-xylanase X24, is expressed when xylose is present as the sole carbon source and repressed in the presence of glucose. That the mutation creAd30results in considerably elevated levels of xlnB mRNA indicates a role for the wide-domain repressor CreA in the repression of xlnB promoter (xlnBp) activity. Functional analyses of xlnBp::goxC reporter constructs show that none of the four CreA consensus target sites identified in xlnBp are functional in vivo. The CreA repressor is thus likely to exert carbon catabolite repression via an indirect mechanism rather than to influence xlnB expression by acting directly on xlnB.

scholarly journals Pandrug-resistant Pseudomonas sp. expresses New Delhi metallo-β-lactamase-1 and consumes ampicillin as sole carbon source

2020 ◽  
Author(s):  
Vivek Kumar Ranjan ◽  
Shriparna Mukherjee ◽  
Subarna Thakur ◽  
Krutika Gupta ◽  
Ranadhir Chakraborty
Keyword(s):  
Carbon Source ◽  
Sole Carbon Source ◽  
New Delhi ◽  
Pseudomonas Sp

scholarly journals Study of a plugging microbial consortium using crude oil as sole carbon source

2008 ◽  
Vol 5 (4) ◽  
pp. 367-374 ◽  
Author(s):  
Jing Wang ◽  
Guiwen Yan ◽  
Mingquan An ◽  
Jieli Liu ◽  
Houming Zhang ◽  
...  
Keyword(s):  
Carbon Source ◽  
Crude Oil ◽  
Sole Carbon Source ◽  
Microbial Consortium

scholarly journals Mutants affecting histidine utilization inAspergillus nidulans

1975 ◽  
Vol 25 (2) ◽  
pp. 119-135 ◽  
Author(s):  
Meryl Polkinghorne ◽  
M. J. Hynes
Keyword(s):  
Carbon Source ◽  
Nitrogen Source ◽  
Sole Carbon Source ◽  
Nitrogen Sources ◽  
Limiting Factor ◽  
Sole Nitrogen Source ◽  
Wild Type ◽  
Exogenous Substrate ◽  
Growth Properties ◽  
Type Strains

SUMMARYWild-type strains ofAspergillus nidulansgrow poorly onL-histidine as a sole nitrogen source. The synthesis of the enzyme histidase (EC. 4.3.1.3) appears to be a limiting factor in the growth of the wild type, as strains carrying the mutantareA102 allele have elevated histidase levels and grow strongly on histidine as a sole nitrogen source.L-Histidine is an extremely weak sole carbon source for all strains.Ammonium repression has an important role in the regulation of histidase synthesis and the relief of ammonium repression is dependent on the availability of a good carbon source. The level of histidase synthesis does not respond to the addition of exogenous substrate.Mutants carrying lesions in thesarA orsarB loci (suppressor ofareA102) have been isolated. The growth properties of these mutants on histidine as a sole nitrogen source correlate with the levels of histidase synthesized. Mutation at thesarA andsarB loci also reduces the utilization of a number of other nitrogen sources. The data suggest that these two genes may code for regulatory products involved in nitrogen catabolism. No histidase structural gene mutants were identified and possible explanations of this are discussed.

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