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Journal articles on the topic 'Pectate lyase'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 March 2023

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1

Boland, Whitney E., Emily DeCrescenzo Henriksen, and Joy Doran-Peterson. "Characterization of Two Paenibacillus amylolyticus Strain 27C64 Pectate Lyases with Activity on Highly Methylated Pectin." Applied and Environmental Microbiology 76, no. 17 (July 9, 2010): 6006–9. http://dx.doi.org/10.1128/aem.00043-10.

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ABSTRACT Two pectate lyases were identified from Paenibacillus amylolyticus 27C64; both enzymes demonstrated activity on methylated pectin in addition to polygalacturonic acid. PelA is in a subclass of the pectate lyase family III. PelB shows some features of pectate lyase family I but is highly divergent.

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2

Kikuchi, Taisei, Hajime Shibuya, Takuya Aikawa, and John T. Jones. "Cloning and Characterization of Pectate Lyases Expressed in the Esophageal Gland of the Pine Wood Nematode Bursaphelenchus xylophilus." Molecular Plant-Microbe Interactions® 19, no. 3 (March 2006): 280–87. http://dx.doi.org/10.1094/mpmi-19-0280.

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Two pectate lyase genes (Bx-pel-1 and Bx-pel-2) were cloned from the pine wood nematode, Bursaphelenchus xy-lophilus. The deduced amino acid sequences of these pectate lyases are most similar to polysaccharide lyase family 3 proteins. Recombinant BxPEL1 showed highest activity on polygalacturonic acid and lower activity on more highly methylated pectin. Recombinant BxPEL1 demonstrated full dependency on Ca2+ for activity and optimal activity at 55°C and pH 8 to 10 like other pectate lyases of polysaccharide lyase family 3. The protein sequences have predicted signal peptides at their N-termini

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3

Dubey, Amit Kumar, Sangeeta Yadav, Manish Kumar, Vinay Kumar Singh, Bijaya Ketan Sarangi, and Dinesh Yadav. "In Silico Characterization of Pectate Lyase Protein Sequences from Different Source Organisms." Enzyme Research 2010 (September 19, 2010): 1–11. http://dx.doi.org/10.4061/2010/950230.

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A total of 121 protein sequences of pectate lyases were subjected to homology search, multiple sequence alignment, phylogenetic tree construction, and motif analysis. The phylogenetic tree constructed revealed different clusters based on different source organisms representing bacterial, fungal, plant, and nematode pectate lyases. The multiple accessions of bacterial, fungal, nematode, and plant pectate lyase protein sequences were placed closely revealing a sequence level similarity. The multiple sequence alignment of these pectate lyase protein sequences from different source organisms showe

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4

Ward, L. J., and S. H. De Boer. "Characterization of a monoclonal antibody against active pectate lyase from Erwinia carotovora." Canadian Journal of Microbiology 35, no. 6 (June 1, 1989): 651–55. http://dx.doi.org/10.1139/m89-105.

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A monoclonal antibody (2E2) produced against pectate lyase from Erwinia carotovora ssp. carotovora reacted with a 41-and a 44-kilodalton protein on Western blots of concentrated Erwinia culture supernatants resolved by sodium dodecyl sulphate – polyaerylamide gel electrophoresis. It was unequivocally shown that monoclonal 2E2 reacted with an active form of pectate lyase by affinity purifying the antigen with the monoclonal. The affinity-purified antigen was enzymatically active and moved as a single protein band in a nonequilibrium isoelectric focusing gel. Monoclonal 2E2 reacted with the pect

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5

Shevchik, Vladimir E., Guy Condemine, Janine Robert-Baudouy, and Nicole Hugouvieux-Cotte-Pattat. "The Exopolygalacturonate Lyase PelW and the Oligogalacturonate Lyase Ogl, Two Cytoplasmic Enzymes of Pectin Catabolism in Erwinia chrysanthemi 3937." Journal of Bacteriology 181, no. 13 (July 1, 1999): 3912–19. http://dx.doi.org/10.1128/jb.181.13.3912-3919.1999.

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ABSTRACT Erwinia chrysanthemi 3937 secretes into the external medium several pectinolytic enzymes, among which are eight isoenzymes of the endo-cleaving pectate lyases: PelA, PelB, PelC, PelD, and PelE (family 1); PelI (family 4); PelL (family 3); and PelZ (family 5). In addition, one exo-cleaving pectate lyase, PelX (family 3), has been found in the periplasm of E. chrysanthemi. The E. chrysanthemi 3937 gene kdgC has been shown to exhibit a high degree of similarity to the genes pelY ofYersinia pseudotuberculosis and pelB ofErwinia carotovora, which encode family 2 pectate lyases. However, no

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6

Guevara, M. A., P. Estévez, and M. T. González-Jaén. "Multiple forms of pectic lyases and polygalacturonase from Fusarium oxysporum f,.sp. radicis lycopersici: regulation of their synthesis by galacturonic acid." Canadian Journal of Microbiology 43, no. 3 (March 1, 1997): 245–53. http://dx.doi.org/10.1139/m97-034.

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The r2 isolate of Fusarium oxysporum f.sp. radicis-lycopersici produced several pectic enzymes that differ in substrate preference, reaction mechanism, and action pattern. We detected three forms that have lyase activity, four forms with polygalacturonase activity and one form with pectinesterase activity. Lyases had an absolute requirement for calcium and pIs of 9.20, 9.00, and 8.65. The two more alkaline forms had a weak preference for pectin, whereas the other was more active on polygalacturonate. Polygalacturonases had pIs of 9.30, 7.35, 6.85, and 6.55 and were inhibited by calcium ions. L

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7

Doyle, Elizabeth A., and Kris N. Lambert. "Cloning and Characterization of an Esophageal-Gland-Specific Pectate Lyase from the Root-Knot Nematode Meloidogyne javanica." Molecular Plant-Microbe Interactions® 15, no. 6 (June 2002): 549–56. http://dx.doi.org/10.1094/mpmi.2002.15.6.549.

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Root-knot nematodes (Meloidogyne javanica) are obligate sedentary endoparasites that must penetrate the host root to initiate their life cycle. Many enzymes are secreted by the nematode to facilitate host penetration; required enzymes may include pectate lyases and cellulases. Using differential screening, a class III pectate lyase, Mj-pel-1 (M. javanica pectate lyase 1), was cloned from a library enriched for esophageal gland genes. DNA gel blotting confirmed that the Mj-pel-1 gene was of nematode origin and a member of a small multigene family. In situ hybridization localized the expression

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8

Nasser, William, Michel Faelen, Nicole Hugouvieux-Cotte-Pattat, and Sylvie Reverchon. "Role of the Nucleoid-Associated Protein H-NS in the Synthesis of Virulence Factors in the Phytopathogenic Bacterium Erwinia chrysanthemi." Molecular Plant-Microbe Interactions® 14, no. 1 (January 2001): 10–20. http://dx.doi.org/10.1094/mpmi.2001.14.1.10.

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The ability of the enterobacterium Erwinia chrysanthemi to induce pathogenesis in plant tissue is strongly related to the massive production of plant-cell-wall-degrading enzymes (pectinases, cellulases, and proteases). Additional factors, including flagellar proteins and exopolysaccharides (EPS), also are required for the efficient colonization of plants. Production of these virulence factors, particularly pectate lyases, the main virulence determinant, is tightly regulated by environmental conditions. The possible involvement of the protein H-NS in this process was investigated. The E. chrysa

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9

Takeyama, Matheus Mikio, Márcia Corrêa de Carvalho, Helena Sacco Carvalho, Cristiane Rodrigues Silva, Ana Paula Trovatti Uetanabaro, Andrea Miura da Costa, Joseph A. Medeiros Evaristo, Fábio César Sousa Nogueira, Ana Elizabeth Cavalcante Fai, and Maria Gabriela Bello Koblitz. "Pectinases Secretion by Saccharomyces cerevisiae: Optimization in Solid-State Fermentation and Identification by a Shotgun Proteomics Approach." Molecules 27, no. 15 (August 5, 2022): 4981. http://dx.doi.org/10.3390/molecules27154981.

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A sequential design strategy was applied to optimize the secretion of pectinases by a Saccharomyces cerevisiae strain, from Brazilian sugarcane liquor vat, on passion fruit residue flour (PFRF), through solid-state fermentation (SSF). A factorial design was performed to determine the influence variables and two rotational central composite designs were executed. The validated experimental result was of 7.1 U mL−1 using 50% PFRF (w/w), pH 5, 30 °C for 24 h, under static SSF. Polygalacturonase, pectin methyl esterase, pectin–lyase and pectate–lyase activities were 3.5; 0.08; 3.1 and 0.8 U mL−1,

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10

Soriano, Margarita, Pilar Diaz, and Francisco I. Javier Pastor. "Pectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with activity on highly methylated pectin." Microbiology 152, no. 3 (March 1, 2006): 617–25. http://dx.doi.org/10.1099/mic.0.28562-0.

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The gene yvpA from Bacillus subtilis was cloned and expressed in Escherichia coli. It encoded a pectate lyase of 221 amino acids that was denominated PelC. The heterologously expressed enzyme was purified by His-tag affinity chromatography and characterized. PelC depolymerized polygalacturonate and pectins of methyl esterification degree from 22 % to 89 %, exhibiting maximum activity on 22 % esterified citrus pectin. It showed an absolute Ca2+ requirement and the optimum temperature and pH were 65 °C and pH 10, respectively. The deduced amino acid sequence of PelC showed 53 % identity to pecta

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11

Kramer-Haimovich, H., E. Servi, T. Katan, J. Rollins, Y. Okon, and D. Prusky. "Effect of Ammonia Production by Colletotrichum gloeosporioides on pelB Activation, Pectate Lyase Secretion, and Fruit Pathogenicity." Applied and Environmental Microbiology 72, no. 2 (February 2006): 1034–39. http://dx.doi.org/10.1128/aem.72.2.1034-1039.2006.

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ABSTRACT The accumulation of ammonia and associated tissue alkalinization predispose avocado fruit to attack by Colletotrichum gloeosporioides. Secretion of ammonia by C. gloeosporioides in the presence of KNO3 was induced by decreasing the pH from 7.0 to 4.0. When the fungus was grown at pH 4.0 or 6.0 in the absence of a nitrogen source, ammonia did not accumulate, and neither pelB (encoding pectate lyase) transcription nor pectate lyase secretion was detected. Under these nitrogen starvation conditions, only transcriptional activation of areA, which encodes the global nitrogen regulator, was

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12

Songpim, Molnapat, Pilanee Vaithanomsat, and Sawitri Chuntranuluck. "Optimization of Pectate Lyase Production from Paenibacillus polymyxa N10 using Response Surface Methodology." Open Biology Journal 3, no. 1 (January 13, 2010): 1–7. http://dx.doi.org/10.2174/18741967010030100001.

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The parameters affecting the production of pectate lyase from P. polymyxa N10 were studied using the response surface methodology agitation rate (X1, 100-300 rpm), temperature (X2, 25-45 °C) and pH (X3, 5.5-9.5). The most significant factors influencing enzyme production were temperature and pH. The second order polynomial regression model obtained was fitted and found adequate, with an R2 of 0.9600 (p < 0.001). A maximum pectate lyase activity of 84.5 U/ml was attained in 72 h of cultivation at agitation rate 200 rpm, temperature 35 °C and pH 8. Optimizations of agitation rate and aeration

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13

Zhou, Cheng, Yuting Cao, Yanfen Xue, Weidong Liu, Jiansong Ju, and Yanhe Ma. "Structure of an Alkaline Pectate Lyase and Rational Engineering with Improved Thermo-Alkaline Stability for Efficient Ramie Degumming." International Journal of Molecular Sciences 24, no. 1 (December 29, 2022): 538. http://dx.doi.org/10.3390/ijms24010538.

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Alkaline pectate lyases have biotechnological applications in plant fiber processing, such as ramie degumming. Previously, we characterized an alkaline pectate lyase from Bacillus clausii S10, named BacPelA, which showed potential for enzymatic ramie degumming because of its high cleavage activity toward methylated pectins in alkaline conditions. However, BacPelA displayed poor thermo-alkaline stability. Here, we report the 1.78 Å resolution crystal structure of BacPelA in apo form. The enzyme has the characteristic right-handed β-helix fold of members of the polysaccharide lyase 1 family and

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14

Bekri, My Ali, Jos Desair, Veerle Keijers, Paul Proost, Marjo Searle-van Leeuwen, Jos Vanderleyden, and Ann vande Broek. "Azospirillum irakense Produces a Novel Type of Pectate Lyase." Journal of Bacteriology 181, no. 8 (April 15, 1999): 2440–47. http://dx.doi.org/10.1128/jb.181.8.2440-2447.1999.

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ABSTRACT The pelA gene from the N2-fixing plant-associated bacterium Azospirillum irakense, encoding a pectate lyase, was isolated by heterologous expression inEscherichia coli. Nucleotide sequence analysis of the region containing pelA indicated an open reading frame of 1,296 bp, coding for a preprotein of 432 amino acids with a typical amino-terminal signal peptide of 24 amino acids. N-terminal amino acid sequencing confirmed the processing of the protein in E. coli at the signal peptidase cleavage site predicted by nucleotide sequence analysis. Analysis of the amino acid sequence of PelA re

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15

Elumalai, R. P., and A. Mahadevan. "Characterization of pectate lyase produced by Pseudomonas marginalis and cloning of pectate lyase genes." Physiological and Molecular Plant Pathology 46, no. 2 (February 1995): 109–19. http://dx.doi.org/10.1006/pmpp.1995.1009.

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16

Yuan, Ye, Xin-Yu Zhang, Yan Zhao, Han Zhang, Yi-Fa Zhou, and Juan Gao. "A Novel PL9 Pectate Lyase from Paenibacillus polymyxa KF-1: Cloning, Expression, and Its Application in Pectin Degradation." International Journal of Molecular Sciences 20, no. 12 (June 22, 2019): 3060. http://dx.doi.org/10.3390/ijms20123060.

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Pectate lyases play an important role in pectin degradation, and therefore are highly useful in the food and textile industries. Here, we report on the cloning of an alkaline pectate lyase gene (pppel9a) from Paenibacillus polymyxa KF-1. The full-length gene (1350 bp) encodes for a 449-residue protein that belongs to the polysaccharide lyase family 9 (PL9). Recombinant PpPel9a produced in Escherichia coli was purified to electrophoretic homogeneity in a single step using Ni2+-NTA affinity chromatography. The enzyme activity of PpPel9a (apparent molecular weight of 45.3 kDa) was found to be opt

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17

Smadja, Bruno, Xavier Latour, Sameh Trigui, Jean François Burini, Sylvie Chevalier, and Nicole Orange. "Thermodependence of growth and enzymatic activities implicated in pathogenicity of twoErwinia carotovorasubspecies (Pectobacteriumspp.)." Canadian Journal of Microbiology 50, no. 1 (January 1, 2004): 19–27. http://dx.doi.org/10.1139/w03-099.

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Erwinia carotovora subsp. atroseptica and Erwinia carotovora subsp. carotovora can cause substantial damage to economically important plant crops and stored products. The occurrence of the disease and the scale of the damage are temperature dependent. Disease development consists first of active multiplication of the bacteria in the infection area and then production of numerous extracellular enzymes. We investigated the effects of various temperatures on these two steps. We assayed the specific growth rate and the pectate lyase and protease activities for eight strains belonging to E. carotov

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18

Saha, Monidipta, Rajib S. Rana, Biswanath Adhikary, and Sabyasachi Mitra. "Screening of bacterial strains for pectate lyase production and detection of optimal growth conditions for enhanced enzyme activity." Journal of Applied and Natural Science 9, no. 1 (March 1, 2017): 370–74. http://dx.doi.org/10.31018/jans.v9i1.1198.

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In the present study, the pectatelyase production by fifty two bacterial strains isolated from ramie grown soils were studied and the strain RDSM01 showed maximum pectate lyase activity. According to sequence homology of Genbank, the strain RDSM01 was identified as Bacillus subtilis (Genbank Accession No. KX035109). Maximum pectate lyase activity of the strain was observed when 1.5% (v/v) inoculum was added to the growth medium and was incubated for 48 hours at 34-370C and at pH 7.0. The relative activity of the strain was 19% higher when apple pectin was used as carbon source compared to citr

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19

RAO, M. Narsimha, Asha A. KEMBHAVI та Aditi PANT. "Role of lysine, tryptophan and calcium in the β-elimination activity of a low-molecular-mass pectate lyase from Fusarium moniliformae". Biochemical Journal 319, № 1 (1 жовтня 1996): 159–64. http://dx.doi.org/10.1042/bj3190159.

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An extracellular pectate lyase from Fusarium moniliformae was purified to homogeneity by affinity chromatography followed by gel filtration, with a yield of 76.5%. Laser desorption MS of the enzyme gave a molecular mass of 12133.5±2.5 Da. The pectate lyase was a glycoprotein with a 5% carbohydrate content and had a pI value of 9.1. Atomic-emission spectrometry showed that Ca2+ was a part of the holoenzyme held by carboxy groups of the protein. These results support the hypothesis of a putative Ca2+ site suggested by Yodder, Keen and Jurnak [(1993) Science 260, 1503–1507] in the crystal structu

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20

BROWN, Ian E., Marie H. MALLEN, Simon J. CHARNOCK, Gideon J. DAVIES, and Gary W. BLACK. "Pectate lyase 10A from Pseudomonas cellulosa is a modular enzyme containing a family 2a carbohydrate-binding module." Biochemical Journal 355, no. 1 (February 26, 2001): 155–65. http://dx.doi.org/10.1042/bj3550155.

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Pectate lyase 10A (Pel10A) enzyme from Pseudomonas cellulosa is composed of 649 residues and has a molecular mass of 68.5kDa. Sequence analysis revealed that Pel10A contained a signal peptide and two serine-rich linker sequences that separate three modules. Sequence similarity was seen between the 9.2kDa N-terminal module of Pel10A and family 2a carbohydrate-binding modules (CBMs). This N-terminal module of Pel10A was shown to encode an independently functional module with affinity to crystalline cellulose. A high sequence identity of 66% was seen between the 14.2kDa central module of Pel10A a

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21

Kaewnum, S., S. Prathuangwong, and T. J. Burr. "A Pectate Lyase Homolog, xagP, in Xanthomonas axonopodis pv. glycines Is Associated with Hypersensitive Response Induction on Tobacco." Phytopathology® 96, no. 11 (November 2006): 1230–36. http://dx.doi.org/10.1094/phyto-96-1230.

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Xanthomonas axonopodis pv. glycines is the causal agent of bacterial pustule disease of soybeans. A transposon insertional mutant (KU-P-M670) of X. axonopodis pv. glycines derived from wild-type strain KU-P-34017 lost the ability to induce the hypersensitive response (HR) on tobacco and pepper but retained its HR induction capacity on cucumber, sesame, and tomato. The mutation also resulted in loss of ability to cause a potato soft rot and express pectolytic activity at pH 6.5. An approximate 1.4-kb DNA fragment carrying the transposon insertion contained a single open reading frame that showe

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22

Cheng, Lifeng, Shengwen Duan, Ke Zheng, Xiangyuan Feng, Qi Yang, Zhiyuan Liu, Zhengchu Liu, and Yuande Peng. "An alkaline pectate lyase D from Dickeya dadantii DCE-01: clone, expression, characterization, and potential application in ramie bio-degumming." Textile Research Journal 89, no. 11 (August 27, 2018): 2075–83. http://dx.doi.org/10.1177/0040517518790971.

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Pectinase plays a crucial role in ramie bio-degumming. A pectate lyase gene ( pel4J4) from the high-efficiency degumming bacteria Dickeya dadantii DCE-01 of bast fibers was cloned and connected to pET28a, and then the recombinant plasmid was successfully transformed into Escherichia coli BL21(DE3). The pectate lyase (Pel4J4) induced was purified by ultrafiltration and Sephadex G-100 gel chromatography. The enzymatic properties of Pel4J4 were studied in detail. pel4J4 (GenBank accession number: KC900167) had a sequence length of 1179 bp, encoding 392 amino acids. The extracellular pectate lyase

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23

Bartling, S., C. Wegener, and O. Olsen. "Synergism between Erwinia pectate lyase isoenzymes that depolymerize both pectate and pectin." Microbiology 141, no. 4 (April 1, 1995): 873–81. http://dx.doi.org/10.1099/13500872-141-4-873.

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24

TEMSAH, M., Y. BERTHEAU, and B. VIAN. "Pectate-lyase fixation and pectate disorganization visualized by immunocytochemistry in infected by." Cell Biology International Reports 15, no. 7 (July 1991): 611–20. http://dx.doi.org/10.1016/0309-1651(91)90008-7.

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25

Sun, Lingxia, Sunchung Park, Martin Bukovac, and Steven van Nocker. "(98) Molecular Analysis of Abscission Layer Activation in Apple Fruit Pedicels." HortScience 41, no. 4 (July 2006): 1030B—1030. http://dx.doi.org/10.21273/hortsci.41.4.1030b.

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Abscission of leaves, floral organs, and fruit is a developmentally and environmentally regulated process initiated in specialized thin layers of cells within abscission zones (AZs). Very little is known about early molecular events that drive abscission, especially of fruit. Commercial apple production relies on the use of flower and fruit abscission-promoting and -inhibiting compounds to enhance fruit quality, control preharvest fruit drop, and maintain consistent annual bearing. The success of chemical treatments is strongly influenced by numerous factors, including environment, genotype, d

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26

Smith, Drummond, and Ian Sumner. "The Stability of Bacillus Subtilis Pectate Lyase." REVIEW OF HIGH PRESSURE SCIENCE AND TECHNOLOGY 7 (1998): 1333–35. http://dx.doi.org/10.4131/jshpreview.7.1333.

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27

., Sathyanarayana N. Gummadi, and D. Sunil Kumar . "Pectin Lyase and Pectate Lyase from Debaryomyces nepalensis Isolated from Apple." Research Journal of Microbiology 1, no. 2 (February 1, 2006): 152–59. http://dx.doi.org/10.3923/jm.2006.152.159.

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28

Xu, Huan, Xiangyuan Feng, Qi Yang, Ke Zheng, Le Yi, Shengwen Duan, and Lifeng Cheng. "Improvement on Thermostability of Pectate Lyase and Its Potential Application to Ramie Degumming." Polymers 14, no. 14 (July 15, 2022): 2878. http://dx.doi.org/10.3390/polym14142878.

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In order to obtain a thermostable pectate lyase for ramie degumming, a rational design based on structural analysis was carried out on a novel pectate lyase (Pel419) derived from the Dickea dadantii DCE-01 for high-efficiency ramie degumming. A total of five potential amino acid sites were chosen to replace residues. Then, the mutant enzymes were subjected to the heterologous expressions in Escherichia coli and their enzymatic characteristics were determined. The optimal reaction temperature for the five mutants kept consistent with that for the wild type. The enzyme activity and thermal stabi

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29

Shevchik, Vladimir E., Harry C. M. Kester, Jacques A. E. Benen, Jaap Visser, Janine Robert-Baudouy, and Nicole Hugouvieux-Cotte-Pattat. "Characterization of the Exopolygalacturonate Lyase PelX of Erwinia chrysanthemi 3937." Journal of Bacteriology 181, no. 5 (March 1, 1999): 1652–63. http://dx.doi.org/10.1128/jb.181.5.1652-1663.1999.

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ABSTRACT Erwinia chrysanthemi 3937 secretes several pectinolytic enzymes, among which eight isoenzymes of pectate lyases with an endo-cleaving mode (PelA, PelB, PelC, PelD, PelE, PelI, PelL, and PelZ) have been identified. Two exo-cleaving enzymes, the exopolygalacturonate lyase, PelX, and an exo-poly-α-d-galacturonosidase, PehX, have been previously identified in other E. chrysanthemi strains. Using a genomic bank of a 3937 mutant with the major pelgenes deleted, we cloned a pectinase gene identified aspelX, encoding the exopolygalacturonate lyase. The deduced amino acid sequence of the 3937

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30

Yakoby, Nir, Delila Beno-Moualem, Noel T. Keen, Amos Dinoor, Ophry Pines, and Dov Prusky. "Colletotrichum gloeosporioides pelB Is an Important Virulence Factor in Avocado Fruit-Fungus Interaction." Molecular Plant-Microbe Interactions® 14, no. 8 (August 2001): 988–95. http://dx.doi.org/10.1094/mpmi.2001.14.8.988.

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Colletotrichum gloeosporioides is an important pathogen of tropical and subtropical fruits. The C. gloeosporioides pelB gene was disrupted in the fungus via homologous recombination. Three independent isolates, GD-14, GD-23, and GD-29, did not produce or secrete pectate lyase B (PLB) and exhibited 25% lower pectate lyase (PL) and pectin lyase (PNL) activities and 15% higher polygalacturonase (PG) activity than the wild type. The PLB mutants exhibited no growth reduction on glucose, Na polypectate, or pectin as the sole carbon source at pH 3.8 or 6.0, except for a 15% reduction on pectin at pH

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31

Akita, Masatake, Atsuo Suzuki, Tohru Kobayashi, Susumu Ito, and Takashi Yamane. "The first structure of pectate lyase belonging to polysaccharide lyase family 3." Acta Crystallographica Section D Biological Crystallography 57, no. 12 (November 21, 2001): 1786–92. http://dx.doi.org/10.1107/s0907444901014482.

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32

Konno, Naotake, Kiyohiko Igarashi, Naoto Habu, Masahiro Samejima, and Akira Isogai. "Cloning of the Trichoderma reesei cDNA Encoding a Glucuronan Lyase Belonging to a Novel Polysaccharide Lyase Family." Applied and Environmental Microbiology 75, no. 1 (October 31, 2008): 101–7. http://dx.doi.org/10.1128/aem.01749-08.

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ABSTRACT The filamentous fungus Trichoderma reesei produces glucuronan lyase (TrGL) when it is grown on β-(1→4)-polyglucuronate (cellouronate) as a sole carbon source. The cDNA encoding TrGL was cloned, and the recombinant enzyme was heterologously expressed in Pichia pastoris. The cDNA of TrGL includes a 777-bp open reading frame encoding a 20-amino-acid signal peptide and the 238-amino-acid mature protein. The amino acid sequence showed no similarity to the amino acid sequences of previously described functional proteins, indicating that the enzyme should be classified in a novel polysacchar

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33

Nasser, William, Sylvie Reverchon, Regine Vedel, and Martine Boccara. "PecS and PecT Coregulate the Synthesis of HrpN and Pectate Lyases, Two Virulence Determinants in Erwinia chrysanthemi 3937." Molecular Plant-Microbe Interactions® 18, no. 11 (November 2005): 1205–14. http://dx.doi.org/10.1094/mpmi-18-1205.

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Erwinia chrysanthemi strain 3937 is a necrotrophic bacterial plant pathogen. Pectinolytic enzymes and, in particular, pectate lyases play a key role in soft rot symptoms; however, the efficient colonization of plants by E. chrysanthemi requires additional factors. These factors include HrpN (harpin), a heat-stable, glycine-rich hydrophilic protein, which is secreted by the type III secretion system. We investigated the expression of hrpN in E. chrysanthemi 3937 in various environmental conditions and different regulatory backgrounds. Using lacZ fusions, hrpN expression was markedly influenced

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34

Dubey, Amit, Sangeeta Yadav, Manish Kumar, Gautam Anand, and Dinesh Yadav. "Molecular Biology of Microbial Pectate Lyase: A Review." British Biotechnology Journal 13, no. 1 (January 10, 2016): 1–26. http://dx.doi.org/10.9734/bbj/2016/24893.

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Miyairi, Kazuo, Ai Ogasawara, Akio Tonouchi, Kouzou Hosaka, Makiko Kudou, and Toshikatsu Okuno. "Low-Molecular-Weight Pectate Lyase from Streptomyces thermocarboxydus." Journal of Applied Glycoscience 51, no. 1 (2004): 1–7. http://dx.doi.org/10.5458/jag.51.1.

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Miyazaki, Yoshimitsu. "Purification and Characterization ofEndo-Pectate Lyase fromBacillus macerans." Agricultural and Biological Chemistry 55, no. 1 (January 1991): 25–30. http://dx.doi.org/10.1080/00021369.1991.10870530.

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Heikinheimo, Riikka. "Characterization of a Novel Pectate Lyase fromErwinia carotovorasubsp.carotovora." Molecular Plant-Microbe Interactions 8, no. 2 (1995): 207. http://dx.doi.org/10.1094/mpmi-8-0207.

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Diolez, A., F. Richaud, and A. Coleno. "Pectate lyase gene regulatory mutants of Erwinia chrysanthemi." Journal of Bacteriology 167, no. 1 (1986): 400–403. http://dx.doi.org/10.1128/jb.167.1.400-403.1986.

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Payasi, Anurag, and G. G. Sanwal. "Pectate lyase activity during ripening of banana fruit." Phytochemistry 63, no. 3 (June 2003): 243–48. http://dx.doi.org/10.1016/s0031-9422(03)00027-x.

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Novoa de Armas, H., A. Rabijns, C. Verboven, J. Desair, A. Vande Broeck, J. Vanderleyden, and C. De Ranter. "Structure of a novel pectate lyase fromAzospirillum irakense." Acta Crystallographica Section A Foundations of Crystallography 58, s1 (August 6, 2002): c110. http://dx.doi.org/10.1107/s0108767302089419.

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Hotchkiss, Jr, A. T., L. G. Revear, and K. B. Hicks. "Substrate depolymerization pattern ofPseudomonas viridiflavaSF-312 pectate lyase." Physiological and Molecular Plant Pathology 48, no. 1 (January 1996): 1–9. http://dx.doi.org/10.1006/pmpp.1996.0001.

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Denis, S., S. Terr�, Y. Bertheau, and P. Boyaval. "Factors affecting pectate lyase activity during membrane filtration." Biotechnology Techniques 4, no. 2 (1990): 127–32. http://dx.doi.org/10.1007/bf00163286.

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Xu, Huan, Shengwen Duan, Xiangyuan Feng, Qi Yang, Ke Zheng, Yuande Peng, and Lifeng Cheng. "Improving the Thermo-Activity and -Stability of Pectate Lyase from Dickeya dadantii DCE-01 for Ramie Degumming." Processes 9, no. 12 (November 24, 2021): 2106. http://dx.doi.org/10.3390/pr9122106.

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To improve the thermal stability of pectate lyase for ramie degumming, we modified the novel pectate lyase gene (pelG403) derived from the Dickeya dadantii DCE-01 high-efficiency ramie degumming strain by site-directed mutagenesis. Twelve mutants were acquired, wherein a prospective mutant (A129V) showed better enzyme activity and thermal stability. Compared with the wild type (PelG403), the specific enzyme activity and the optimal reaction temperature of A129V in the fermentation broth increased by 20.1%, and 5 °C, respectively. Under the conditions of 55 °C and pH 9.0, the weightlessness rat

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Yang, Shihui, Qiu Zhang, Jianhua Guo, Amy O. Charkowski, Bernard R. Glick, A. Mark Ibekwe, Donald A. Cooksey, and Ching-Hong Yang. "Global Effect of Indole-3-Acetic Acid Biosynthesis on Multiple Virulence Factors of Erwinia chrysanthemi 3937." Applied and Environmental Microbiology 73, no. 4 (December 22, 2006): 1079–88. http://dx.doi.org/10.1128/aem.01770-06.

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ABSTRACT Production of the plant hormone indole-3-acetic acid (IAA) is widespread among plant-associated microorganisms. The non-gall-forming phytopathogen Erwinia chrysanthemi 3937 (strain Ech3937) possesses iaaM (ASAP16562) and iaaH (ASAP16563) gene homologues. In this work, the null knockout iaaM mutant strain Ech138 was constructed. The IAA production by Ech138 was reduced in M9 minimal medium supplemented with l-tryptophan. Compared with wild-type Ech3937, Ech138 exhibited reduced ability to produce local maceration, but its multiplication in Saintpaulia ionantha was unaffected. The pecta

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Jafra, Sylwia, Izabela Figura, Nicole Hugouvieux-Cotte-Pattat, and Ewa Lojkowska. "Expression of Erwinia chrysanthemi Pectinase Genes pelI, pelL, and pelZ During Infection of Potato Tubers." Molecular Plant-Microbe Interactions® 12, no. 10 (October 1999): 845–51. http://dx.doi.org/10.1094/mpmi.1999.12.10.845.

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Erwinia chrysanthemi mutants, containing transcriptional fusions of one of the minor pectate lyase genes (pelI, pelL, pelZ) with the reporter gene encoding β-glucuronidase activity, were studied for their ability to cause disease symptoms and to synthesize pectinases after inoculation of potato tubers. The strains affected in pelI and pelL genes displayed reduced virulence on potato tubers, demonstrating the important role of these isoenzymes in soft rot disease. Inactivation of the pelZ gene slightly influences the ability to macerate. Analysis of the bacterial population showed rapid multipl

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Zhao, Yan, Ye Yuan, Xinyu Zhang, Yumei Li, Qiang Li, Yifa Zhou, and Juan Gao. "Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from Paenibacillus polymyxa KF-1: Cloning, Expression and Characterization." Molecules 23, no. 11 (October 26, 2018): 2774. http://dx.doi.org/10.3390/molecules23112774.

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Pectate lyase (EC 4.2.2.2) catalyzes the cleavage of α-1,4-glycosidic bonds of pectin polymers, and it has potential uses in the textile industry. In this study, a novel pectate lyase belonging to polysaccharide lyase family 10 was screened from the secreted enzyme extract of Paenibacillus polymyxa KF-1 and identified by liquid chromatography-MS/MS. The gene was cloned from P. polymyxa KF-1 genomic DNA and expressed in Escherichia coli. The recombinant enzyme PpPel10a had a predicted Mr of 45.2 kDa and pI of 9.41. Using polygalacturonic acid (PGA) as substrate, the optimal conditions for PpPel

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Yamazaki, Akihiro, Jin Li, William C. Hutchins, Lixia Wang, Jincai Ma, A. Mark Ibekwe, and Ching-Hong Yang. "Commensal Effect of Pectate Lyases Secreted fromDickeya dadantiion Proliferation ofEscherichia coliO157:H7 EDL933 on Lettuce Leaves." Applied and Environmental Microbiology 77, no. 1 (November 12, 2010): 156–62. http://dx.doi.org/10.1128/aem.01079-10.

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ABSTRACTThe outbreaks caused by enterohemorrhagicEscherichia coliO157:H7 on leafy greens have raised serious and immediate food safety concerns. It has been suggested that several phytopathogens aid in the persistence and proliferation of the human enteropathogens in the phyllosphere. In this work, we examined the influence of virulence mechanisms ofDickeya dadantii3937, a broad-host-range phytopathogen, on the proliferation of the human pathogenE. coliO157:H7 EDL933 (EDL933) on postharvest lettuce by coinoculation of EDL933 withD. dadantii3937 derivatives that have mutations in virulence-rela

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Wagner, Christian, Olov Sterner, and Heidrun Anke. "Verticillium rexianum (SACC.) SACC., a New Producer of Monacolin K." Zeitschrift für Naturforschung C 53, no. 3-4 (April 1, 1998): 289–90. http://dx.doi.org/10.1515/znc-1998-3-421.

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Abstract From the broth of submerged cultures of Verticillium rexianum (teleomorph: Nectriopsis exigua), a mycophilic fungus growing on myxomycetes, monacolin K was isolated as a weak inhibitor of pectate lyase. Monacolin K is the first secondary metabolite described from V. rexianum.

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KLUSKENS, Leon D., Gert-Jan W. M. van ALEBEEK, Alphons G. J. VORAGEN, Willem M. de VOS, and John van der OOST. "Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima." Biochemical Journal 370, no. 2 (March 1, 2003): 651–59. http://dx.doi.org/10.1042/bj20021595.

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The ability of the hyperthermophilic bacterium Thermotoga maritima to grow on pectin as a sole carbon source coincides with the secretion of a pectate lyase A (PelA) in the extracellular medium. The pelA gene of T. maritima was functionally expressed in Escherichia coli as the first heterologously produced thermophilic pectinase, and purified to homogeneity. Gel filtration indicated that the native form of PelA is tetrameric. Highest activity (422units/mg, with a Km of 0.06mM) was demonstrated on polygalacturonic acid (PGA), whereas pectins with an increasing degree of methylation were degrade

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Barre, Annick, Hélène Sénéchal, Christophe Nguyen, Claude Granier, Pierre Rougé, and Pascal Poncet. "Identification of Potential IgE-Binding Epitopes Contributing to the Cross-Reactivity of the Major Cupressaceae Pectate-Lyase Pollen Allergens (Group 1)." Allergies 2, no. 3 (September 5, 2022): 106–18. http://dx.doi.org/10.3390/allergies2030010.

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Pectate-lyase allergens, the group 1 of allergens from Cupressaceae pollen, consist of glycoproteins exhibiting an extremely well-conserved three-dimensional structure and sequential IgE-binding epitopes. Up to 10 IgE-binding epitopic regions were identified on the molecular surface, which essentially cluster at both extremities of the long, curved β-prism-shaped allergens. Most of these IgE-binding epitopes possess very similar conformations that provide insight into the IgE-binding cross-reactivity and cross-allergenicity commonly observed among Cupressaceae pollen allergens. Some of these e

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