Pub. Date : 2018 Apr
PMID : 29476645
4 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Angiotensin-1-converting enzyme (ACE) is a zinc metallopeptidase that consists of two homologous catalytic domains (known as nACE and cACE) with different substrate specificities. | nace | angiotensin I converting enzyme | Homo sapiens |
| 2 | Angiotensin-1-converting enzyme (ACE) is a zinc metallopeptidase that consists of two homologous catalytic domains (known as nACE and cACE) with different substrate specificities. | nace | angiotensin I converting enzyme | Homo sapiens |
| 3 | Based on kinetic studies it was previously reported that sampatrilat, a tight-binding inhibitor of ACE, Ki = 13.8 nm and 171.9 nm for cACE and nACE respectively [Sharma et al., Journal of Chemical Information and Modeling (2016), 56, 2486-2494], was 12.4-fold more selective for cACE. | nace | angiotensin I converting enzyme | Homo sapiens |
| 4 | Here, we report a detailed three-dimensional structural analysis of sampatrilat and samAsp binding to ACE using high-resolution crystal structures elucidated by X-ray crystallography, which provides a molecular basis for differences in inhibitor affinity and selectivity for nACE and cACE. | nace | angiotensin I converting enzyme | Homo sapiens |