scholarly journals Macromolecular crowding effects on the kinetics of opposing reactions catalyzed by alcohol dehydrogenase

2021 ◽  
Vol 26 ◽  
pp. 100956
Author(s):  
Xander E. Wilcox ◽  
Charmaine B. Chung ◽  
Kristin M. Slade
Keyword(s):  
Alcohol Dehydrogenase ◽  
Macromolecular Crowding ◽  
Crowding Effects ◽  
Kinetics Of

scholarly journals Kinetics of polymer looping with macromolecular crowding: effects of volume fraction and crowder size

Soft Matter ◽  
2015 ◽  
Vol 11 (3) ◽  
pp. 472-488 ◽  
Author(s):  
Jaeoh Shin ◽  
Andrey G. Cherstvy ◽  
Ralf Metzler
Keyword(s):  
Volume Fraction ◽  
Macromolecular Crowding ◽  
Crowding Effects ◽  
Kinetics Of

Depending on the size of crowding molecules and their volume fraction the looping rates of polymers are facilitated or impeded.

Cosolvent and crowding effects on the polymerization kinetics of actin

2015 ◽  
Vol 17 (13) ◽  
pp. 8330-8337 ◽  
Author(s):  
Christopher Rosin ◽  
Paul Hendrik Schummel ◽  
Roland Winter
Keyword(s):  
Macromolecular Crowding ◽  
Polymerization Kinetics ◽  
Lag Phase ◽  
Crowding Effects ◽  
Kinetics Of

Effects of cosolvents and macromolecular crowding agents on the G-to-F-transformation of actin are studied. Drastic and diverse changes in the lag phase and association rates of polymerizing actin are observed under different solvent conditions.

Iodoacetate inactivation of rape alcohol dehydrogenase

1980 ◽  
Vol 45 (5) ◽  
pp. 1601-1607 ◽  
Author(s):  
Marie Stiborová ◽  
Sylva Leblová
Keyword(s):  
Alcohol Dehydrogenase ◽  
Protein Molecule ◽  
Sulfhydryl Groups ◽  
Inactivation Rate ◽  
First Order ◽  
Ph Dependent ◽  
Kinetics Of

Iodoacetate inactivates rape alcohol dehydrogenase (ADH, EC 1.1.1.1). The inactivation rate follows the kinetics of the first order, is pH-dependent, and decreases below pH 7.5. Besides irreversible alkylation of the sulfhydryl groups of the enzyme iodoacetate also forms a reversible complex with rape ADH. The coenzyme (NAD) and its analogs (ATP, ADP, AMP) competitively protect the enzyme against alkylation; o-phenanthroline also protects the enzyme against alkylation yet noncompetitively with respect to iodoacetate. Imidazole and o-phenanthroline compete with one another for binding to the protein molecule of rape ADH. Whereas o-phenanthroline decreases the inactivation rate imidazole increases the rate of iodoacetate inactivation.

scholarly journals Macromolecular Crowding Effects on Reactions of TePixD (Tll0078)†

2010 ◽  
Vol 87 (3) ◽  
pp. 584-589 ◽  
Author(s):  
Tsuguyoshi Toyooka ◽  
Keisuke Tanaka ◽  
Koji Okajima ◽  
Masahiko Ikeuchi ◽  
Satoru Tokutomi ◽  
...  
Keyword(s):  
Macromolecular Crowding ◽  
Crowding Effects

scholarly journals Thermodynamics and Molecular Kinetics of Liver Alcohol Dehydrogenase.

1963 ◽  
Vol 17 supl. ◽  
pp. 27-33 ◽  
Author(s):  
Keith Dalziel ◽  
Gad Yagil ◽  
Warren F. Diven ◽  
Mark Takahashi
Keyword(s):  
Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Kinetics Of

scholarly journals Residue-Level Interrogation of Macromolecular Crowding Effects on Protein Stability

2008 ◽  
Vol 130 (21) ◽  
pp. 6826-6830 ◽  
Author(s):  
Lisa M. Charlton ◽  
Christopher O. Barnes ◽  
Conggang Li ◽  
Jillian Orans ◽  
Gregory B. Young ◽  
...  
Keyword(s):  
Protein Stability ◽  
Macromolecular Crowding ◽  
Residue Level ◽  
Crowding Effects

Macromolecular crowding: effects on actin polymerisation

1997 ◽  
Vol 66 (1) ◽  
pp. 57-66 ◽  
Author(s):  
Robyn A. Lindner ◽  
Gregory B. Ralston
Keyword(s):  
Macromolecular Crowding ◽  
Crowding Effects
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