Optimization of Fe3O4 nanozyme activity via single amino acid modification mimicking an enzyme active site

2017 ◽  
Vol 53 (2) ◽  
pp. 424-427 ◽  
Author(s):  
Kelong Fan ◽  
Hui Wang ◽  
Juqun Xi ◽  
Qi Liu ◽  
Xiangqin Meng ◽  
...  
Keyword(s):  
Amino Acid ◽  
Active Site ◽  
Catalytic Efficiency ◽  
Single Amino Acid ◽  
Acid Modification ◽  
Histidine Modification ◽  
Enzyme Active Site ◽  
Amino Acid Modification

Histidine modification effectively improved the affinity of Fe3O4 nanozyme to H2O2, enhancing its catalytic efficiency by mimicking peroxidase active site.

scholarly journals Single Amino Acid Modification of Adeno-Associated Virus Capsid Changes Transduction and Humoral Immune Profiles

2012 ◽  
Vol 86 (15) ◽  
pp. 7752-7759 ◽  
Author(s):  
C. Li ◽  
N. Diprimio ◽  
D. E. Bowles ◽  
M. L. Hirsch ◽  
P. E. Monahan ◽  
...  
Keyword(s):  
Amino Acid ◽  
Single Amino Acid ◽  
Acid Modification ◽  
Virus Capsid ◽  
Adeno Associated Virus ◽  
Humoral Immune ◽  
Amino Acid Modification

Two forms of poliovirus VPg result from amino acid modification of a single viral protein

Virology ◽  
1984 ◽  
Vol 136 (2) ◽  
pp. 453-456 ◽  
Author(s):  
Oliver C. Richards ◽  
Kathryn Morton ◽  
Susan C. Martin ◽  
Ellie Ehrenfeld
Keyword(s):  
Amino Acid ◽  
Viral Protein ◽  
Acid Modification ◽  
Amino Acid Modification

Post-Translational Amino Acid Modification

2010 ◽  
pp. 1052-1052
Author(s):  
R. Hamish McAllister-Williams ◽  
Daniel Bertrand ◽  
Hans Rollema ◽  
Raymond S. Hurst ◽  
Linda P. Spear ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Modification ◽  
Amino Acid Modification

P219L substitution in human D-amino acid oxidase impacts the ligand binding and catalytic efficiency

2020 ◽  
Vol 168 (5) ◽  
pp. 557-567
Author(s):  
Wanitcha Rachadech ◽  
Yusuke Kato ◽  
Rabab M Abou El-Magd ◽  
Yuji Shishido ◽  
Soo Hyeon Kim ◽  
...  
Keyword(s):  
Amino Acid ◽  
Conformational Changes ◽  
Active Site ◽  
Structural Changes ◽  
Catalytic Efficiency ◽  
Acid Oxidase ◽  
Wild Type ◽  
Amino Acid Oxidase ◽  
Adenine Ring ◽  
The Impact

Abstract Human D-amino acid oxidase (DAO) is a flavoenzyme that is implicated in neurodegenerative diseases. We investigated the impact of replacement of proline with leucine at Position 219 (P219L) in the active site lid of human DAO on the structural and enzymatic properties, because porcine DAO contains leucine at the corresponding position. The turnover numbers (kcat) of P219L were unchanged, but its Km values decreased compared with wild-type, leading to an increase in the catalytic efficiency (kcat/Km). Moreover, benzoate inhibits P219L with lower Ki value (0.7–0.9 µM) compared with wild-type (1.2–2.0 µM). Crystal structure of P219L in complex with flavin adenine dinucleotide (FAD) and benzoate at 2.25 Å resolution displayed conformational changes of the active site and lid. The distances between the H-bond-forming atoms of arginine 283 and benzoate and the relative position between the aromatic rings of tyrosine 224 and benzoate were changed in the P219L complex. Taken together, the P219L substitution leads to an increase in the catalytic efficiency and binding affinity for substrates/inhibitors due to these structural changes. Furthermore, an acetic acid was located near the adenine ring of FAD in the P219L complex. This study provides new insights into the structure–function relationship of human DAO.

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