scholarly journals Lysine degradation through the saccharopine pathway in mammals: involvement of both bifunctional and monofunctional lysine-degrading enzymes in mouse

1999 ◽  
Vol 344 (2) ◽  
pp. 555 ◽  
Author(s):  
Fabio PAPES ◽  
Edson L. KEMPER ◽  
Germano CORD-NETO ◽  
Francesco LANGONE ◽  
Paulo ARRUDA
Keyword(s):  
Degrading Enzymes ◽  
Lysine Degradation ◽  
Saccharopine Pathway

scholarly journals Lysine degradation through the saccharopine pathway in bacteria: LKR and SDH in bacteria and its relationship to the plant and animal enzymes

FEBS Letters ◽  
2012 ◽  
Vol 586 (6) ◽  
pp. 905-911 ◽  
Author(s):  
Guilherme Coutinho de Mello Serrano ◽  
Thaís Rezende e Silva Figueira ◽  
Eduardo Kiyota ◽  
Natalia Zanata ◽  
Paulo Arruda
Keyword(s):  
Lysine Degradation ◽  
Saccharopine Pathway

scholarly journals Lysine degradation through the saccharopine pathway in mammals: involvement of both bifunctional and monofunctional lysine-degrading enzymes in mouse

1999 ◽  
Vol 344 (2) ◽  
pp. 555-563 ◽  
Author(s):  
Fabio PAPES ◽  
Edson L. KEMPER ◽  
Germano CORD-NETO ◽  
Francesco LANGONE ◽  
Paulo ARRUDA
Keyword(s):  
Mitochondrial Protein ◽  
Bifunctional Enzyme ◽  
Saccharopine Dehydrogenase ◽  
Isolation And Characterization ◽  
Short Transcript ◽  
Liver And Kidney ◽  
Lysine Degradation ◽  
First Time ◽  
Saccharopine Pathway

Lysine-oxoglutarate reductase and saccharopine dehydrogenase are enzymic activities that catalyse the first two steps of lysine degradation through the saccharopine pathway in upper eukaryotes. This paper describes the isolation and characterization of a cDNA clone encoding a bifunctional enzyme bearing domains corresponding to these two enzymic activities. We partly purified those activities from mouse liver and showed for the first time that both a bifunctional lysine-oxoglutarate reductase/saccharopine dehydrogenase and a monofunctional saccharopine dehydrogenase are likely to be present in this organ. Northern analyses indicate the existence of two mRNA species in liver and kidney. The longest molecule, 3.4 kb in size, corresponds to the isolated cDNA and encodes the bifunctional enzyme. The 2.4 kb short transcript probably codes for the monofunctional dehydrogenase. Sequence analyses show that the bifunctional enzyme is likely to be a mitochondrial protein. Furthermore, enzymic and expression analyses suggest that lysine-oxoglutarate reductase/saccharopine dehydrogenase levels increase in livers of mice under starvation. Lysine-injected mice also show an increase in lysine-oxoglutarate reductase and saccharopine dehydrogenase levels.

Effect of Olive Oil Mill Waste Waters on the Edible and Medicinal Mushroom Lentinus edodes (Berk.) Sing. Growth and Lignin Degrading Enzymes

2002 ◽  
Vol 4 (2) ◽  
pp. 10 ◽  
Author(s):  
Slaven Zjalic ◽  
Anna Adele Fabbri ◽  
Alessandra Ricelli ◽  
Massimo Reverberi ◽  
Emanuela Galli ◽  
...  
Keyword(s):  
Olive Oil ◽  
Medicinal Mushroom ◽  
Lentinus Edodes ◽  
Waste Waters ◽  
Degrading Enzymes ◽  
Mill Waste

Nucleotide degrading enzymes inNeurospora crassa

1974 ◽  
Vol 14 (7) ◽  
pp. 581-591 ◽  
Author(s):  
A. K. Mattoo ◽  
Zarna M. Shah
Keyword(s):  
Degrading Enzymes ◽  
Inneurospora Crassa

scholarly journals Cuticle degrading enzyme production by some isolates of the entomopathogenic fungus, Metarhizium anisopliae (Metsch.)

2014 ◽  
Vol 20 ◽  
pp. 25-32
Author(s):  
N Sapna Bai ◽  
OK Remadevi ◽  
TO Sasidharan ◽  
M Balachander ◽  
Priyadarsanan Dharmarajan
Keyword(s):  
Pest Control ◽  
Entomopathogenic Fungi ◽  
Enzyme Production ◽  
Insect Pest ◽  
Strong Relationship ◽  
Control Agent ◽  
Mechanical Pressure ◽  
Degrading Enzyme ◽  
Insect Pest Control ◽  
Degrading Enzymes

Context: Entomopathogenic fungi have been recognized as viable alternate options to chemicals in insect pest control. Unlike other potential biocontrol agents, fungi do not have to be ingested to infect their hosts but invade directly through the cuticle. Entry into the host involves both enzymic degradation of the cuticle barrier and mechanical pressure. Production of a range of cuticle degrading enzymes is an important event in the interaction of entomopathogenic fungi and host. Enzyme secretion is believed to be a key contributor for the virulence of a fungal isolate. Objectives: The potentiality of nine isolates of M. anisopliae were tested to produce to produce three important cuticle degrading enzymes, viz., chitinase, protease and lipase. Materials and Methods: Nine isolates of M. anisopliae were evaluated for chitinase, protease and lipase enzyme production by determining the enzyme index and activities. Results: Chitinase index of these isolates were ranged from 1.5 to 2.2 and chitinolytic activity from 0.525 to 1.560 U/ml. The isolates showed protease index in the range of 1.2 to 3.3 and the activity ranged from 0.020 to 0.114 U/ml. Lipase index ranged from 1.15 to 7.0 and the enzyme activity ranged from 0.153 to 0.500 U/ml. A strong relationship was observed between virulence of the isolates and cuticle degrading enzyme production as increased enzyme production was observed for virulent isolates. Conclusion: In the present study three isolates as (MIS2, MIS7 and MIS13) demonstrated cuticle degrading enzyme (CDE) that indicate higher virulence based on the bioassay conducted earlier by the authors as strongly substantiating the role of CDEs is considered the virulence of Metarhizium isolates. So, these isolates may be as ecofriendly insect-pest control agent in future. DOI: http://dx.doi.org/10.3329/jbs.v20i0.17648 J. bio-sci. 20: 25-32, 2012

scholarly journals IsdG and IsdI, Heme-degrading Enzymes in the Cytoplasm ofStaphylococcus aureus

2003 ◽  
Vol 279 (1) ◽  
pp. 436-443 ◽  
Author(s):  
Eric P. Skaar ◽  
Andrew H. Gaspar ◽  
Olaf Schneewind
Keyword(s):  
Ofstaphylococcus Aureus ◽  
Degrading Enzymes

PSIII-18 Super Dose Phytase and Carbohydrase Cocktail Enhance Ileal Nutrient and Energy Digestibility of Corn-soybean Diets in Nursery Pigs

2021 ◽  
Vol 99 (Supplement_1) ◽  
pp. 176-176
Author(s):  
B V Le Thanh ◽  
J R R Bergstrom ◽  
J D Hahn ◽  
L F Wang ◽  
E Beltranena ◽  
...  
Keyword(s):  
Large Intestine ◽  
Soybean Meal ◽  
Synergistic Effects ◽  
Latin Square ◽  
Nursery Pigs ◽  
Ileal Digestibility ◽  
Degrading Enzymes ◽  
Feed Enzymes

Abstract Feed enzymes may ameliorate reduced nutrient and energy digestibility in nursery pigs. The objective was to test effects of super-dosing phytase and fiber-degrading enzymes on digestibility of DM, GE, CP, AA, and Ca. We tested supplementing a super dose (added 1,500 FYT/kg) of phytase (Ronozyme Hi-Phos) with or without carbohydrase cocktail that contained 85 FXU β-xylanase/kg, 587 U/g endo-1,4-β-glucanase, 513 U/g endo-1,3(4)-β-glucanase, 15,000 U/g hemicellulases, and 3,000 U/g pectinases in corn-soybean meal diets in a 2 × 2 factorial arrangement. Diets included 68% corn, 17% SBM, and a basal level of 500 FTU/kg of phytase, and were formulated to contain 2.50 Mcal/kg NE and 5.10 gSID Lys/Mcal NE. Eight ileal-cannulated nursery pigs (initial BW 10 kg) were fed 4 diets at 3.0 × maintenance DE (110 kcal per kg of BW0.75) for four 9-day periods in a double 4 × 4 Latin square. Apparent hindgut fermentation (AHF) was calculated as apparent total tract digestibility (ATTD) minus apparent ileal digestibility (AID). Interactions between super-dosing phytase and carbohydrase cocktail were observed. Supplementing either carbohydrase cocktail or super dose phytase, but not their combination, increased (P < 0.05) diet AID of DM, GE, CP, and most AA by 4–5%-units. Supplementing super dose phytase increased (P < 0.05) AID of P by 16%-units and ATTD of P by 10%-units. Supplementing super dose phytase or carbohydrase cocktail did not affect AID of Ca and ATTD of GE, CP, and Ca, and diet DE value. Supplementing carbohydrase cocktail without super dose phytase decreased (P < 0.05) diet AHF of DM, GE, and CP. In conclusion, dietary inclusion of super dose phytase or carbohydrase cocktail increased ileal digestibility of nutrients in nursery pigs, and thereby reduced protein entering the large intestine. Additive or synergistic effects of carbohydrase cocktail and super dose phytase were not detected.

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