Mechanism of action of Escherichia coli formamidopyrimidine N-glycosylase: Role of K155 in substrate binding and product release

2001 ◽  
pp. 223-234 ◽  
Author(s):  
Lois Rabow ◽  
Radhika Venkataraman ◽  
Yoke W Kow
Keyword(s):  
Escherichia Coli ◽  
Mechanism Of Action ◽  
Substrate Binding ◽  
Product Release

scholarly journals Studies on the mechanism of hydroxymethylbilane synthase concerning the role of arginine residues in substrate binding

1991 ◽  
Vol 275 (2) ◽  
pp. 447-452 ◽  
Author(s):  
M Lander ◽  
A R Pitt ◽  
P R Alefounder ◽  
D Bardy ◽  
C Abell ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Kinetic Parameters ◽  
Substrate Binding ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Side Chains ◽  
Enzyme Substrate ◽  
Arginine Residues

The role of conserved arginine residues in hydroxymethylbilane synthase was investigated by replacing these residues in the enzyme from Escherichia coli with leucine residues by using site-directed mutagenesis. The kinetic parameters for these mutant enzymes and studies on the formation of intermediate enzyme-substrate complexes indicate that several of these arginine residues are involved in binding the carboxylate side chains of the pyrromethane cofactor and the growing oligopyrrole chain.

scholarly journals Role of conformational dynamics in the evolution of novel enzyme function

2018 ◽  
Vol 54 (50) ◽  
pp. 6622-6634 ◽  
Author(s):  
Miguel A. Maria-Solano ◽  
Eila Serrano-Hervás ◽  
Adrian Romero-Rivera ◽  
Javier Iglesias-Fernández ◽  
Sílvia Osuna
Keyword(s):  
Chemical Transformation ◽  
Substrate Binding ◽  
Conformational Dynamics ◽  
Enzyme Function ◽  
Product Release ◽  
Substrate Preferences ◽  
Recent Advances

Enzymes exist as a dynamic ensemble of conformations, each potentially playing a key role in substrate binding, the chemical transformation, or product release. We discuss recent advances in the evaluation of the enzyme conformational dynamics and its evolution towards new functions or substrate preferences.

Role of CH/π interactions in substrate binding by Escherichia coli β-galactosidase

2004 ◽  
Vol 339 (13) ◽  
pp. 2275-2280 ◽  
Author(s):  
Vojtěch Spiwok ◽  
Petra Lipovová ◽  
Tereza Skálová ◽  
Eva Buchtelová ◽  
Jindřich Hašek ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Substrate Binding ◽  
Π Interactions

SOME ASPECTS OF THE FUNCTION OF FSH- AND LH-LIKE HORMONES IN NORMAL AND HYPOPHYSECTOMIZED FEMALE RATS, IN CONNECTION WITH RESERPINE ADMINISTRATION

1965 ◽  
Vol 49 (1) ◽  
pp. 28-38
Author(s):  
M. Grönroos ◽  
E. Mäkinen ◽  
K. Lahtinen ◽  
R. Tirri
Keyword(s):  
Mechanism Of Action ◽  
Biological Effect ◽  
Female Rats ◽  
Histological Picture ◽  
Peripheral Effect ◽  
Pituitary Secretion

ABSTRACT The effect of reserpine on the secretion of FSH and LH was studied as well as the role of the peripheral effect of reserpine after hypophysectomy. The results in the unoperated animals suggest that reserpine inhibits the pituitary secretion of both FSH and LH. Both these hormones combined with reserpine had a very different biological effect than was seen without reserpine. HCG (LH-like) and particularly PMS (FSH-like) hormones combined with reserpine caused definite enlargement of the ovaries. In the hypophysectomized groups, the effect of the PMS and HCG hormones administered together with reserpine or without it was the same with regard to the weight of the ovaries, but not with regard to their histological picture. On the basis of these results, reserpine may be said to have a peripheral effect although the nature of its mechanism of action is difficult to state. Reserpine probably affects the ovaries by inhibiting the follicular cycle and, consequently, the formation of new and more mature follicles.

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