Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.2.2.10 (PNL)
 341 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A pectin lyase (PNL; EC 4.2.2.10) was isolated from culture filtrates of Pseudomonas fluorescens W51 and purified to apparent homogeneity. The enzyme catalyzed a random eliminative cleavage of pectin but not sodium polypectate, and it macerated plant tissue. The Mr of the PNL on sodium dodecyl sulfate-polyacrylamide gels was 32,000 +/- 1,000, and the isoelectric point was 9.4 as determined by isoelectric focusing. The enzyme was constitutively produced, since the highest yields were obtained when glycerol was used as a sole carbon source, and addition of pectin to the medium did not increase its production. Antibodies against purified PNL reacted in Western blots (immunoblots) with a pectate lyase (PLb) produced by Erwinia chrysanthemi EC16. The PNL appeared to be the only factor secreted into the culture medium by P. fluorescens W51 which macerated plant tissue and is probably involved in the soft rot disease caused by the bacterium.
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PMID:Purification and characterization of a pectin lyase produced by Pseudomonas fluorescens W51. 311 58

Growth and concomitant production of an extracellular pectin lyase (PL) [poly(methoxylgalactosiduronate) endolyase; EC 4.2.2.10] were investigated in a group of 16 fungi grown in liquid medium containing pectin as a supplementary carbon source. Culture filtrates of both Penicillium italicum (CECT 2294) and P. expansum (CECT 2275) showed the highest PL activity and contained polygalacturonase but not pectinesterase activity. The effect of the inoculum size, the carbon source (sucrose and glucose syrup), and the presence of pectin on the production of PL by P. italicum was studied. The presence of 2.6 mM glycerophosphate in the culture medium enhanced the appearance of PL but was not inhibitory for the in vitro activity. However, glycerol inhibited the enzyme nearly 50% at such a concentration.
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PMID:Pectin Lyase Production by a Penicillium italicum Strain. 1634 54

The CT1 mutant of Penicillium occitanis hyperproduces extracellular pectinases constitutively since it secretes pectinases even on glucose-containing medium. We show here that all other hydrolytic enzymes remain at low activities in CT1, confirming the specificity of the regulatory mutation towards pectinases. We isolated, by RT-PCR and through the construction of a cDNA library, three fragments coding for: a pectin lyase (pnl1), a polygalacturonase (pga1) and a pectate lyase (pal1). These fragments were used as probes in Northern blots analysis of the wild type strain CL100 and the CT1 mutant of P. occitanis grown in three culture conditions. The CT1 mutant showed a very high amount of pnl1, pga1 and pal1 mRNA either in pectin, glucose or glycerol grown cells while in the wild type CL100 strain, all transcripts were undetectable even on pectin. These results suggest that the CT1 mutation affects a trans-regulatory transcriptional factor regulating pectinase expression.
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PMID:Constitutive over-expression of pectinases in Penicillium occitanis CT1 mutant is transcriptionally regulated. 2128 29

Growth and enzymes production by Aspergillus flavipes FP-500 were evaluated on pectin, polygalacturonic acid, galacturonic acid, arabinose, rhamnose, xylose, glycerol and glucose at different initial pH values. We found that the strain produced exopectinases, endopectinases and pectin lyases. Exopectinases and pectin lyase were found to be produced at basal levels as constitutive enzymes and their production was modulated by the available carbon source and pH of culture medium and stimulated by the presence of inducer in the culture medium. Endo-pectinase was basically inducible and was only produced when pectin was used as carbon source. Our results suggest that pectinases in A. flavipes FP-500 are produced in a concerted way. The first enzyme to be produced was exopectinase followed by Pectin Lyase and Endo-pectinase.
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PMID:Constitutive and inducible pectinolytic enzymes from Aspergillus flavipes FP-500 and their modulation by pH and carbon source. 2403 15