Cofactor and Substrate Binding to Vanadium Chloroperoxidase Determined by UV−VIS Spectroscopy and Evidence for High Affinity for Pervanadate†

Biochemistry ◽  
2000 ◽  
Vol 39 (5) ◽  
pp. 1133-1141 ◽  
Author(s):  
Rokus Renirie ◽  
Wieger Hemrika ◽  
Sander R. Piersma ◽  
Ron Wever
Keyword(s):  
Substrate Binding ◽  
High Affinity ◽  
Vis Spectroscopy

scholarly journals Two perfectly conserved arginine residues are required for substrate binding in a high-affinity nitrate transporter

2004 ◽  
Vol 101 (50) ◽  
pp. 17549-17554 ◽  
Author(s):  
S. E. Unkles ◽  
D. A. Rouch ◽  
Y. Wang ◽  
M. Y. Siddiqi ◽  
A. D. M. Glass ◽  
...  
Keyword(s):  
Substrate Binding ◽  
Nitrate Transporter ◽  
High Affinity ◽  
Arginine Residues

scholarly journals To be, or not to be two sites: that is the question about LeuT substrate binding

2011 ◽  
Vol 138 (4) ◽  
pp. 467-471 ◽  
Author(s):  
Nicolas Reyes ◽  
Sotiria Tavoulari
Keyword(s):  
Binding Sites ◽  
Journal Club ◽  
Substrate Binding ◽  
Structural Data ◽  
Transport Proteins ◽  
Model System ◽  
Transport Mechanisms ◽  
High Affinity ◽  
The Central Nervous System ◽  
Substrate Binding Sites

Transport proteins of the neurotransmitter sodium symporter (NSS) family regulate the extracellular concentration of several neurotransmitters in the central nervous system. The only member of this family for which atomic-resolution structural data are available is the prokaryotic homologue LeuT. This protein has been used as a model system to study the molecular mechanism of transport of the NSS family. In this Journal Club, we discuss two strikingly different LeuT transport mechanisms: one involving a single high-affinity substrate binding site and one recently proposed alternative involving two high-affinity substrate binding sites that are allosterically coupled.

scholarly journals Mapping of barley α-amylases and outer subsite mutants reveals dynamic high-affinity subsites and barriers in the long substrate binding cleft

FEBS Letters ◽  
2006 ◽  
Vol 580 (21) ◽  
pp. 5049-5053 ◽  
Author(s):  
Lili Kandra ◽  
Maher Abou Hachem ◽  
Gyöngyi Gyémánt ◽  
Birte Kramhøft ◽  
Birte Svensson
Keyword(s):  
Substrate Binding ◽  
High Affinity ◽  
Binding Cleft

scholarly journals Tripartite ATP-independent Periplasmic (TRAP) Transporters Use an Arginine-mediated Selectivity Filter for High Affinity Substrate Binding

2015 ◽  
Vol 290 (45) ◽  
pp. 27113-27123 ◽  
Author(s):  
Marcus Fischer ◽  
Adam P. Hopkins ◽  
Emmanuele Severi ◽  
Judith Hawkhead ◽  
Daniel Bawdon ◽  
...  
Keyword(s):  
Substrate Binding ◽  
Selectivity Filter ◽  
High Affinity

scholarly journals A Dualistic Conformational Response to Substrate Binding in the Human Serotonin Transporter Reveals a High Affinity State for Serotonin

2015 ◽  
Vol 290 (12) ◽  
pp. 7747-7755 ◽  
Author(s):  
Henriette Bjerregaard ◽  
Kasper Severinsen ◽  
Saida Said ◽  
Ove Wiborg ◽  
Steffen Sinning
Keyword(s):  
Serotonin Transporter ◽  
Substrate Binding ◽  
High Affinity

Biochemical and structural study ofArabidopsishexokinase 1

2015 ◽  
Vol 71 (2) ◽  
pp. 367-375 ◽  
Author(s):  
Juan Feng ◽  
Shun Zhao ◽  
Xuemin Chen ◽  
Wenda Wang ◽  
Wei Dong ◽  
...  
Keyword(s):  
Substrate Binding ◽  
Glucose Sensing ◽  
Wild Type ◽  
Structural Explanation ◽  
High Affinity ◽  
Physiological Processes ◽  
Glucose Binding ◽  
Glucose Signalling ◽  
Dual Functions ◽  
Resolution Structure

Hexokinase 1 fromArabidopsis thaliana(AtHXK1) plays a dual role in glycolysis and sugar sensing for vital metabolic and physiological processes. The uncoupling of glucose signalling from glucose metabolism was demonstrated by the analysis of two mutants (AtHXK1G104DandAtHXK1S177A) that are catalytically inactive but still functional in signalling. In this study, substrate-binding experiments indicate that the two catalytically inactive mutants have a high affinity for glucose, and an ordered substrate-binding mechanism has been observed for wild-typeAtHXK1. The structure ofAtHXK1 was determined both in its inactive unliganded form and in its active glucose-bound form at resolutions of 1.8 and 2.0 Å, respectively. These structures reveal a domain rearrangement ofAtHXK1 upon glucose binding. The 2.1 Å resolution structure ofAtHXK1S177Ain the glucose-bound form shows similar glucose-binding interactions as the wild type. A glucose-sensing network has been proposed based on these structures. Taken together, the results provide a structural explanation for the dual functions ofAtHXK1.

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