scholarly journals Covalent modification of substrate-binding sites of Escherichia coli ADP-glucose synthetase. Isolation and structural characterization of 8-azido-ADP-glucose-incorporated peptides.

1986 ◽  
Vol 261 (3) ◽  
pp. 1058-1064
Author(s):  
Y M Lee ◽  
J Preiss
Keyword(s):  
Escherichia Coli ◽  
Structural Characterization ◽  
Binding Sites ◽  
Substrate Binding ◽  
Covalent Modification ◽  
Substrate Binding Sites

Characterization of Dual Substrate Binding Sites in the Homodimeric Structure of Escherichia coli mRNA Interferase MazF

2006 ◽  
Vol 357 (1) ◽  
pp. 139-150 ◽  
Author(s):  
Guang-Yao Li ◽  
Yonglong Zhang ◽  
Mitchell C.Y. Chan ◽  
Tapas K. Mal ◽  
Klaus P. Hoeflich ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Substrate Binding ◽  
Substrate Binding Sites ◽  
Dual Substrate

scholarly journals Genetic and Enzymatic Experiments relating to the Quaternary Structure of ß-Galactosidase

1974 ◽  
Vol 27 (3) ◽  
pp. 321 ◽  
Author(s):  
J Langridge
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Quaternary Structure ◽  
Substrate Binding ◽  
Isolation And Characterization ◽  
Normal Enzyme ◽  
Substrate Binding Sites ◽  
Polypeptide Sequences

The quaternary structure of f:!-galactosidase, which consists of four identical subunits, has been studied by the isolation and characterization of appropriate mutants of Escherichia coli. Of 146 mutants examined, 19 were found to have enzymes with reduced subunit association. These altered enzymes are especially sensitive to inactivation by urea which, at concentrations that do not affect the normal enzyme, causes dissociation into subunits. Mapping with overlapping deletions showed that the mutations affecting quaternary structure are not distributed continuously, but occur in five or six groups within the gene. The mapping indicates that polypeptide sequences involved in subunit association and in substrate binding are contiguous. A model for f:!-galactosidase structure is suggested in which substrate binding sites are provided by the clefts formed between subunits when they associate.

Structural characterization of β‐ketoacyl ACP synthase I bound to platencin and fragment screening molecules at two substrate binding sites

2019 ◽  
Vol 88 (1) ◽  
pp. 47-56 ◽  
Author(s):  
Edward I. Patterson ◽  
Jeffrey D. Nanson ◽  
Jan Abendroth ◽  
Cassie Bryan ◽  
Banumathi Sankaran ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Binding Sites ◽  
Substrate Binding ◽  
Fragment Screening ◽  
Substrate Binding Sites
Sign in / Sign up

Export Citation Format

Share Document