Intersubunit cross-linking by cis-dichlorodiammineplatinum(II) stabilizes an .alpha.2-macroglobulin "nascent" state: evidence that thiol ester bond cleavage correlates with receptor recognition site exposure

Biochemistry ◽  
1988 ◽  
Vol 27 (2) ◽  
pp. 759-764 ◽  
Author(s):  
Paul A. Roche ◽  
Poul Erik Hyldgaard Jensen ◽  
Salvatore V. Pizzo
Keyword(s):  
Bond Cleavage ◽  
Recognition Site ◽  
Cross Linking ◽  
Ester Bond ◽  
Thiol Ester ◽  
Receptor Recognition

scholarly journals Use of anti-idiotypic antibodies to establish that monoclonal antibody 7H11D6 binds to the alpha 2-macroglobulin receptor recognition site.

1988 ◽  
Vol 263 (14) ◽  
pp. 6709-6714 ◽  
Author(s):  
I J Isaacs ◽  
J P Steiner ◽  
P A Roche ◽  
S V Pizzo ◽  
D K Strickland
Keyword(s):  
Monoclonal Antibody ◽  
Recognition Site ◽  
Receptor Recognition

scholarly journals Reduction of the beta-Cys-gamma-Glu thiol ester bond of human C3 with sodium borohydride.

1983 ◽  
Vol 258 (22) ◽  
pp. 13580-13586 ◽  
Author(s):  
M L Thomas ◽  
F F Davidson ◽  
B F Tack
Keyword(s):  
Sodium Borohydride ◽  
Ester Bond ◽  
Thiol Ester

scholarly journals Primary receptor-recognition site of human transferrin is in the C-terminal lobe.

1994 ◽  
Vol 269 (10) ◽  
pp. 7110-7114
Author(s):  
O. Zak ◽  
D. Trinder ◽  
P. Aisen
Keyword(s):  
Recognition Site ◽  
Human Transferrin ◽  
Primary Receptor ◽  
Receptor Recognition

A synthesis of biaryl ketones via the C–S bond cleavage of thiol ester by a Cu/Ag salt

2017 ◽  
Vol 58 (28) ◽  
pp. 2751-2756 ◽  
Author(s):  
Prasanjit Ghosh ◽  
Bhaskar Ganguly ◽  
Eliyahu Perl ◽  
Sajal Das
Keyword(s):  
Bond Cleavage ◽  
Thiol Ester

The Kinetic Demonstration of a Metastable Intermediate in a Nucleophilic Displacement at a Thiol-Ester Bond

1964 ◽  
Vol 86 (4) ◽  
pp. 738-739 ◽  
Author(s):  
Thomas C. Bruice ◽  
Leo R. Fedor
Keyword(s):  
Ester Bond ◽  
Thiol Ester ◽  
Nucleophilic Displacement

scholarly journals Probing the receptor recognition site of the FimH adhesin by fimbriae-displayed FimH---FocH hybrids

Microbiology ◽  
1998 ◽  
Vol 144 (7) ◽  
pp. 1919-1929 ◽  
Author(s):  
T. B. Knudsen ◽  
P. Klemm
Keyword(s):  
Recognition Site ◽  
Receptor Recognition

Mapping the receptor-recognition site of human transforming growth factor-α

2009 ◽  
Vol 38 (3) ◽  
pp. 204-211 ◽  
Author(s):  
JAMES P. TAM ◽  
YAO-ZHONG LIN ◽  
WEN LIU ◽  
DE-XIN WANG ◽  
XIAO-HONG KE ◽  
...  
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Recognition Site ◽  
Transforming Growth Factor Α ◽  
Receptor Recognition ◽  
Factor Α

scholarly journals Streptomyces K15 active-site serine dd-transpeptidase: specificity profile for peptide, thiol ester and ester carbonyl donors and pathways of the transfer reactions

1995 ◽  
Vol 307 (2) ◽  
pp. 335-339 ◽  
Author(s):  
J Grandchamps ◽  
M Nguyen-Distèche ◽  
C Damblon ◽  
J M Frère ◽  
J M Ghuysen
Keyword(s):  
Active Site ◽  
Kinetic Data ◽  
Transfer Reactions ◽  
Ester Bond ◽  
Penicillin Binding Protein ◽  
Thiol Ester ◽  
Ester Carbonyl ◽  
Simple Alternative ◽  
Scissile Bond ◽  
Enzyme Intermediate

The Streptomyces K15 transferase is a penicillin-binding protein presumed to be involved in bacterial wall peptidoglycan crosslinking. It catalyses cleavage of the peptide, thiol ester or ester bond of carbonyl donors Z-R1-CONH-CHR2-COX-CHR3-COO- (where X is NH, S or O) and transfers the electrophilic group Z-R1-CONH-CHR2-CO to amino acceptors via an acyl-enzyme intermediate. Kinetic data suggest that the amino acceptor behaves as a simple alternative nucleophile at the level of the acyl-enzyme in the case of thiol ester and ester donors, and that it binds to the enzyme.carbonyl donor Michaelis complex and influences the rate of enzyme acylation by the carbonyl donor in the case of amide donors. Depending on the nature of the scissile bond, the enzyme has different requirements for substituents at positions R1, R2 and R3.

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