L-Phenylalanine ammonia-lyase (maize, potato, and Rhodotorula glutinis). Studies of the prosthetic group with nitromethane

Biochemistry ◽  
1975 ◽  
Vol 14 (8) ◽  
pp. 1620-1626 ◽  
Author(s):  
Evelyn A. Havir ◽  
Kenneth R. Hanson
Keyword(s):  
Phenylalanine Ammonia Lyase ◽  
Rhodotorula Glutinis ◽  
Prosthetic Group

scholarly journals The effect of proteinases on phenylalanine ammonia-lyase from the yeast Rhodotorula glutinis

1981 ◽  
Vol 199 (3) ◽  
pp. 715-723 ◽  
Author(s):  
H J Gilbert ◽  
G W Jack
Keyword(s):  
Phenylalanine Ammonia Lyase ◽  
Bond Cleavage ◽  
Rhodotorula Glutinis ◽  
Peptide Bond ◽  
Enzymic Activity ◽  
Duodenal Juice ◽  
Prosthetic Group ◽  
Prolonged Incubation ◽  
Peptide Bond Cleavage ◽  
Site Binding

Phenylalanine ammonia-lyase (EC 4.3.1.5) of the yeast Rhodotorula glutinis was rapidly inactivated by duodenal juice. It was susceptible to chymotrypsin and subtilisin and to a lesser extent trypsin. Initial proteolysis of the enzyme by chymotrypsin and trypsin resulted in cleavage of the monomeric subunit (75 000 Mr) into a large (65 000 Mr) and a small (10 000 Mr) peptide. The small peptide was rapidly degraded. The 65 000-Mr fragment was resistant to prolonged incubation with chymotrypsin, but was degraded by trypsin under the same conditions. Phenylalanine ammonia-lyase was cleaved into several polypeptides by subtilisin, the 65 000-Mr peptide being totally absent. The N-terminal region of the enzyme was contained in the 65 000-Mr fragment, as was the dehydroalanine moiety, the prosthetic group. Active-site-binding ligands protect the enzyme from inactivation by the three proteinases, and peptide-bond cleavage by trypsin and chymotrypsin. Several chemical modifications were performed on phenylalanine ammonia-lyase. Some decreased its antigenicity, and ethyl acetimidate decreased the rate of degradation of the 65 000-Mr peptide by trypsin. The modification did not protect the enzyme from proteolytic inactivation of the enzymic activity. These observations are discussed in terms of the structure of phenylalanine ammonia-lyase and site of action of the proteinases.

scholarly journals Rhodotorula glutinis: STRAIN ENRICHMENT AND EVALUATION OF PHENYLALANINE AMMONIA LYASE

2007 ◽  
Vol 44 (1) ◽  
Author(s):  
M. Jason MacDonald ◽  
Godwin B. D'Cunha
Keyword(s):  
Nous Avons ◽  
Yeast Extract ◽  
Phenylalanine Ammonia Lyase ◽  
Rhodotorula Glutinis ◽  
Yeast Cells ◽  
Pal Activity ◽  
Yeast Extract Medium ◽  
Extract Medium ◽  
Phenylalanine Methyl Ester

2006 NSIS Honourable Mention, Undergraduate Student ResearchPrize Winning PaperThe enrichment of a Rhodotorula glufinis strain and the determination of itsphenylalanine ammonia lyase (E.C.4.3.1.5 - PAL) activity and attempts to measure peroxidase (E.C.1.11.1. 7) activity included conventional mycological procedures along with chemical and microscopic examination. Sabouraud dextrose medium was found to be the most suitable for cell growth, but cells grown on yeast-extract medium exhibited optimal enzyme activity. Growth and PAL activity were measured in yeast cells grown in yeast-extract broth medium for 24-27 h. The appearance of a reddish pink color associated with the yeast cells coincided with the appearance of appreciable PAL activity. The maximum PAL activity and biomass of yeast obtained in the yeast extract medium ranged from 33 to 35 unitslmg dry cells and 7.5 to 8.0 g dry cells/l, respectively. In addition to phenylalanine, Rhodatowla PAL also used phenylalanine methyl-ester as a substrate. No peroxidase activity was found in these R. glutinis cells.L'enrichissement de la souche de Rhodatarula glutinis et la detenmination de l'activite de la phenylalanine ammoniac-lyase (E.C.4.3.1.5 - PAL) chez cette souche, de meme que les tentatives de mesure de I'activite de la peroxydase (E.C.1 .11.1 .7), ont compris I'utilisation de procedures mycologiques traditionnelles ainsi que des examens microscopiques et chimiques. Nous avons constate que la gelose Sabouraud au dextrose est Ie meilleur milieu pour assurer la croissance cellulaire, mais que l'activite enzymatique est optimale dans les cellules cultivees sur un milieu a base d'extrait de levure. Nousavons mesure la croissance de cellulesde levure culliveesdans un bouillon a base d'extrait de levure pendant 24 a 27 heures et nous avons mesure I'activite de la PAL dans ces memes cellules. L'apparition d'une couleur rose rougeatre associee aux cellules de levure a coIncide avec Ie debut d'une periode d'activite notable de laPAL. L'activite maxima Ie de la PAL obtenue dans Ie milieu a base d'exlrait de levure a varie de 33 a 35 unites par mg de cellules seches, tandis que la biomasse de levure maximale obtenue dans Ie meme milieu a varie de 7,5 a 8,0 9 de cellules seches par litre. En plus de la phenylalanine, la PAlde Rhodotorula a utilise I'ester methylique de la phenylalanine comme substrat. Aucune activite de la peroxydase n'a ete observee dans ces cellules de R. glutinis.•

scholarly journals Induction of Phytoalexins Gliceoline and Proteins Related to Defense in Soybean Cotyledon Treated With Yeast

2020 ◽  
Vol 12 (12) ◽  
pp. 156
Author(s):  
Eloisa Lorenzetti ◽  
Jeferson Carlos Carvalho ◽  
Alfredo José Alves Neto ◽  
Camila Hendges ◽  
Taís Regina Kohler ◽  
...  
Keyword(s):  
Phenylalanine Ammonia Lyase ◽  
Rhodotorula Glutinis ◽  
Soybean Seeds ◽  
Cryptococcus Laurentii ◽  
Distilled Water ◽  
Defense Enzymes ◽  
Pichia Guilliermondii ◽  
Total Proteins ◽  
Soybean Cotyledon ◽  
Sporidiobolus Johnsonii

Yeasts can induce mechanisms of plant resistance due to compounds with eliciting characteristics, so the aim of this work was to evaluate the effect of yeast on the induction of phytoalexins gliceoline, peroxidase, polyphenoloxidase and phenylalanine ammonia-lyase from soy cotyledons. To determine the defense enzymes, soybean seeds were sown and the cotyledons treated with sterile distilled water, Cryptococcus laurentii (AH 03-1), Pichia guilliermondii (AH 16-2), Rhodotorula glutinis (AH 14-3), Sporidiobolus johnsonii (AH 16-1) and Zygoascus hellenicus (AH 14-1). Biochemical analyzes of the formation of phytoalexins and the activity of the enzymes peroxidase, polyphenoloxidase, phenylalanine ammonia-lyase and total proteins were performed. For phytoalexins glycerolins the yeasts Cryptococcus laurentii (AH 03-1) and Zygoascus hellenicus (AH 14-1) promoted an increase of 83.65% and 78.75% in the formation of this compound. Cryptococcus laurentii (AH 03-1) increased peroxidase activity by 36.84%, while for polyphenoloxidase, the Pichiaguilliermondii e yeasts (AH 16-2), Rhodotorula glutinis (AH 14-3), Sporidiobolus johnsonii (AH 16-1) and Zygoascus hellenicus (AH 14-1), increased the activity of this enzyme by 33.33%, 28.00%, 33.33% and 33.33%, respectively. For phenylalanine ammonia-lyase, Cryptococcus laurentii (AH 03-1) and Zygoascushellenicus (AH 14-1) promoted an increase of 75.57% and 78.86%, respectively, in their activity. The results demonstrate the potential of yeasts studied in the induction of phytoalexins glyceolins and in the activity of peroxidase, polyphenoloxidase and phenylalanine ammonia-lyase in soybean cotyledons.

Optimization of oligomeric enzyme activity in ionic liquids using Rhodotorula glutinis yeast phenylalanine ammonia lyase

2017 ◽  
Vol 96 ◽  
pp. 151-156 ◽  
Author(s):  
Christiaan C. Barron ◽  
Brandon J.D. Sponagle ◽  
Pugazhendhi Arivalagan ◽  
Godwin B. D’Cunha
Keyword(s):  
Enzyme Activity ◽  
Ionic Liquids ◽  
Phenylalanine Ammonia Lyase ◽  
Rhodotorula Glutinis

Biosynthesis of 15NL-phenylalanine by phenylalanine ammonia-lyase from Rhodotorula glutinis

Amino Acids ◽  
2008 ◽  
Vol 36 (2) ◽  
pp. 231-233 ◽  
Author(s):  
Wenya Wang ◽  
Haiyan Yue ◽  
Qipeng Yuan ◽  
Wenchuan Wang
Keyword(s):  
Phenylalanine Ammonia Lyase ◽  
Rhodotorula Glutinis
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