scholarly journals Ecological selectivity and the evolution of mammalian substrate preference across the K–Pg boundary

2021 ◽  
Author(s):  
Jonathan J. Hughes ◽  
Jacob S. Berv ◽  
Stephen G. B. Chester ◽  
Eric J. Sargis ◽  
Daniel J. Field
Keyword(s):  
Substrate Preference

SUBSTRATE PREFERENCE AND MID-MESOZOIC BRACHIOPOD DECLINE

2016 ◽  
Author(s):  
Marko Manojlovic ◽  
◽  
Matthew E. Clapham
Keyword(s):  
Substrate Preference

scholarly journals A single change of histidine to glutamine alters the substrate preference of a stilbene synthase.

1992 ◽  
Vol 267 (29) ◽  
pp. 20558-20560
Author(s):  
G Schröder ◽  
J Schröder
Keyword(s):  
Stilbene Synthase ◽  
Substrate Preference

Eicosapentaenoic and docosahexaenoic acid affect mitochondrial and peroxisomal fatty acid oxidation in relation to substrate preference

Lipids ◽  
1999 ◽  
Vol 34 (9) ◽  
pp. 951-963 ◽  
Author(s):  
Lise Madsen ◽  
Arild C. Rustan ◽  
Hege Vaagenes ◽  
Kjetil Berge ◽  
Endre Dyrøy ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Docosahexaenoic Acid ◽  
Fatty Acid Oxidation ◽  
Substrate Preference ◽  
Acid Oxidation ◽  
Peroxisomal Fatty Acid Oxidation ◽  
Peroxisomal Fatty Acid

Microbial substrate preference and community dynamics during decomposition of Acer saccharum

2011 ◽  
Vol 4 (6) ◽  
pp. 396-407 ◽  
Author(s):  
Zachary L. Rinkes ◽  
Michael N. Weintraub ◽  
Jared L. DeForest ◽  
Daryl L. Moorhead
Keyword(s):  
Acer Saccharum ◽  
Community Dynamics ◽  
Substrate Preference

Interrelationship between hepatic ureagenesis and gluconeogenesis in early sepsis

1991 ◽  
Vol 260 (3) ◽  
pp. E453-E458 ◽  
Author(s):  
Y. Ohtake ◽  
M. G. Clemens
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Substrate Preference ◽  
Hormone Sensitivity ◽  
Urea Production ◽  
Urea Release ◽  
Amino Acid Levels ◽  
Early Sepsis ◽  
Septic Group

This study was performed to investigate the interrelationship between gluconeogenesis and ureagenesis during sepsis. In isolated perfused livers, gluconeogenesis was assessed using either lactate or a combination of lactate, glutamine, and alanine as substrate. Ureagenesis was assessed using either NH4Cl or glutamine plus alanine as substrate. NH4Cl stimulated urea production in livers from both septic and sham-operated control rats. Urea release was approximately 1.2 and 2.0 mg urea nitrogen.g-1.h-1 for 1 and 5 mM NH4Cl, respectively, and was equal for both groups. With amino acids as substrate, urea production was significantly greater in livers from septic animals compared with controls. Phenylephrine stimulated urea production in the sham-operated group by about twofold, whereas in the septic group urea release was slightly inhibited. Gluconeogenesis from lactate was inhibited by NH4Cl (1 and 5 mM) in both groups, with no difference between groups. In contrast to enhanced ureagenesis from amino acids in septic rats, gluconeogenesis was decreased by approximately 24% (P less than 0.5). Similarly, phenylephrine (1 microM) stimulated gluconeogenesis by 13 +/- 1 mumol.g-1.h-1 in sham-operated rats but only by 9 +/- 1 mumol.g-1.h-1 in septic rats (P less than 0.02). These results suggest that hepatic gluconeogenic and ureagenic pathways are intact in sepsis but that altered substrate preference and hormone sensitivity may result in decreased gluconeogenesis in the presence of elevated amino acid levels.

scholarly journals Melanocortin Receptor 4 Deficiency Affects Body Weight Regulation, Grooming Behavior, and Substrate Preference in the Rat

Obesity ◽  
2012 ◽  
Vol 20 (3) ◽  
pp. 612-621 ◽  
Author(s):  
Joram D. Mul ◽  
Ruben van Boxtel ◽  
Dylan J.M. Bergen ◽  
Maike A.D. Brans ◽  
Jan H. Brakkee ◽  
...  
Keyword(s):  
Body Weight ◽  
Substrate Preference ◽  
Melanocortin Receptor ◽  
Weight Regulation ◽  
Body Weight Regulation ◽  
Grooming Behavior

Rational design of styrene monooxygenase mutants with altered substrate preference

2010 ◽  
Vol 33 (3) ◽  
pp. 611-616 ◽  
Author(s):  
Abeer Ahmed Qaed ◽  
Hui Lin ◽  
De-Fang Tang ◽  
Zhong-Liu Wu
Keyword(s):  
Rational Design ◽  
Substrate Preference ◽  
Styrene Monooxygenase

scholarly journals Synergistic Hydrolysis of Carboxymethyl Cellulose and Acid-Swollen Cellulose by Two Endoglucanases (CelZ and CelY) fromErwinia chrysanthemi

2000 ◽  
Vol 182 (20) ◽  
pp. 5676-5682 ◽  
Author(s):  
Shengde Zhou ◽  
Lonnie O. Ingram
Keyword(s):  
Carboxymethyl Cellulose ◽  
Cell Walls ◽  
Cellulase Activity ◽  
Substrate Preference ◽  
Erwinia Chrysanthemi ◽  
General Mechanism ◽  
Plant Cell Walls ◽  
Enzymatic Modification ◽  
Amorphous Cellulose ◽  
Hydrolysis Of

ABSTRACT Erwinia chrysanthemi produces a battery of hydrolases and lyases which are very effective in the maceration of plant cell walls. Although two endoglucanases (CelZ and CelY; formerly EGZ and EGY) are produced, CelZ represents approximately 95% of the total carboxymethyl cellulase activity. In this study, we have examined the effectiveness of CelY and CelZ alone and of combinations of both enzymes using carboxymethyl cellulose (CMC) and amorphous cellulose (acid-swollen cellulose) as substrates. Synergy was observed with both substrates. Maximal synergy (1.8-fold) was observed for combinations containing primarily CelZ; the ratio of enzyme activities produced was similar to those produced by cultures of E. chrysanthemi. CelY and CelZ were quite different in substrate preference. CelY was unable to hydrolyze soluble cellooligosaccharides (cellotetraose and cellopentaose) but hydrolyzed CMC to fragments averaging 10.7 glucosyl units. In contrast, CelZ readily hydrolyzed cellotetraose, cellopentaose, and amorphous cellulose to produce cellobiose and cellotriose as dominant products. CelZ hydrolyzed CMC to fragments averaging 3.6 glucosyl units. In combination, CelZ and CelY hydrolyzed CMC to products averaging 2.3 glucosyl units. Synergy did not require the simultaneous presence of both enzymes. Enzymatic modification of the substrate by CelY increased the rate and extent of hydrolysis by CelZ. Full synergy was retained by the sequential hydrolysis of CMC, provided CelY was used as the first enzyme. A general mechanism is proposed to explain the synergy between these two enzymes based primarily on differences in substrate preference.

Substrate Preference Pattern ofAgaricus meleagrisPyranose Dehydrogenase Evaluated through Bioelectrochemical Flow Injection Amperometry

2018 ◽  
Vol 6 (3) ◽  
pp. 801-809 ◽  
Author(s):  
Parvin Rafighi ◽  
Paolo Bollella ◽  
Galina Pankratova ◽  
Clemens K. Peterbauer ◽  
Peter Ó Conghaile ◽  
...  
Keyword(s):  
Flow Injection ◽  
Substrate Preference ◽  
Preference Pattern
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