You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output.
Click here to find out more.
Mendeley readers
| Title |
Crystallographic and molecular dynamics simulation analysis of Escherichia coli dihydroneopterin aldolase
|
|---|---|
| Published in |
Cell & Bioscience, September 2014
|
| DOI | 10.1186/2045-3701-4-52 |
| Pubmed ID | |
| Authors |
Jaroslaw Blaszczyk, Zhenwei Lu, Yue Li, Honggao Yan, Xinhua Ji |
| Abstract |
Dihydroneopterin aldolase (DHNA) catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin and also the epimerization of DHNP to 7,8-dihydromonapterin. Previously, we determined the crystal structure of Staphylococcus aureus DHNA (SaDHNA) in complex with the substrate analogue neopterin (NP). We also showed that Escherichia coli DHNA (EcDHNA) and SaDHNA have significantly different binding and catalytic properties by biochemical analysis. On the basis of these structural and functional data, we proposed a catalytic mechanism involving two proton wires. |
Mendeley readers
The data shown below were compiled from readership statistics for 13 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 13 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 5 | 38% |
| Researcher | 3 | 23% |
| Professor | 1 | 8% |
| Unknown | 4 | 31% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 5 | 38% |
| Pharmacology, Toxicology and Pharmaceutical Science | 1 | 8% |
| Agricultural and Biological Sciences | 1 | 8% |
| Unknown | 6 | 46% |