scholarly journals Discovery and Mechanistic Characterization of Selective Inhibitors of H2S-producing Enzyme: 3-Mercaptopyruvate Sulfurtransferase (3MST) Targeting Active-site Cysteine Persulfide

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Kenjiro Hanaoka ◽  
Kiyoshi Sasakura ◽  
Yusuke Suwanai ◽  
Sachiko Toma-Fukai ◽  
Kazuhito Shimamoto ◽  
...  
Keyword(s):  
Active Site ◽  
Selective Inhibitors ◽  
Active Site Cysteine ◽  
Mercaptopyruvate Sulfurtransferase

Characterization of anEscherichia coliSulfite Oxidase Homologue Reveals the Role of a Conserved Active Site Cysteine in Assembly and Function†

Biochemistry ◽  
2005 ◽  
Vol 44 (30) ◽  
pp. 10339-10348 ◽  
Author(s):  
Stephen J. Brokx ◽  
Richard A. Rothery ◽  
Guijin Zhang ◽  
Derek P. Ng ◽  
Joel H. Weiner
Keyword(s):  
Active Site ◽  
Active Site Cysteine ◽  
And Function

Abstract 2757: Discovery and characterization of covalent Pin1 inhibitors targeted to an active site cysteine

2019 ◽  
Author(s):  
Benika Pinch ◽  
Zainab Doctor ◽  
Christopher M. Browne ◽  
Hyuk-Soo Seo ◽  
Behnam Nabet ◽  
...  
Keyword(s):  
Active Site ◽  
Active Site Cysteine

Abstract 2757: Discovery and characterization of covalent Pin1 inhibitors targeted to an active site cysteine

2019 ◽  
Author(s):  
Benika Pinch ◽  
Zainab Doctor ◽  
Christopher M. Browne ◽  
Hyuk-Soo Seo ◽  
Behnam Nabet ◽  
...  
Keyword(s):  
Active Site ◽  
Active Site Cysteine

Characterization of an Abnormal Antithrombin (Milano 2) with Defective Thrombin Binding

1986 ◽  
Vol 56 (03) ◽  
pp. 349-352 ◽  
Author(s):  
A Tripodi ◽  
A Krachmalnicoff ◽  
P M Mannucci
Keyword(s):  
Venous Thromboembolism ◽  
Active Site ◽  
Inhibitory Activity ◽  
Antithrombin Iii ◽  
Factor Xa ◽  
Molecular Defect ◽  
Affinity Adsorption ◽  
Italian Family ◽  
Crossed Immunoelectrophoresis

SummaryFour members of an Italian family (two with histories of venous thromboembolism) had a qualitative defect of antithrombin III reflected by normal antigen concentrations and halfnormal antithrombin activity with or without heparin. Anti-factor Xa activities were consistently borderline low (about 70% of normal). For the propositus’ plasma and serum the patterns of antithrombin III in crossed-immunoelectrophoresis with or without heparin were indistinguishable from those of normal plasma or serum. A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chromatography. Affinity adsorption of the propositus’ plasma to human α-thrombin immobilized on sepharose beads revealed defective binding of the anti thrombin III to thrombin-sepharose. Hence the molecular defect of this variant appears to be at the active site responsible for binding and neutralizing thrombin, thus accounting for the low thrombin inhibitory activity.

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