Pub. Date : 1995 Feb 24
PMID : 7876099
4 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | There are important amino acid differences in the alcohol-binding site between the human class IV (sigma) and human class I (beta) alcohol dehydrogenases that appear to explain the high catalytic efficiency for all-trans-retinol, the high kcat for ethanol, and the low catalytic efficiency for secondary alcohols of sigma-ADH relative to beta 1-ADH. | Vitamin A | alcohol dehydrogenase 1B (class I), beta polypeptide | Homo sapiens |
| 2 | There are important amino acid differences in the alcohol-binding site between the human class IV (sigma) and human class I (beta) alcohol dehydrogenases that appear to explain the high catalytic efficiency for all-trans-retinol, the high kcat for ethanol, and the low catalytic efficiency for secondary alcohols of sigma-ADH relative to beta 1-ADH. | Vitamin A | alcohol dehydrogenase 1B (class I), beta polypeptide | Homo sapiens |
| 3 | For example, modeling the binding of all-trans-retinol in the human beta 1-ADH structure suggested that coordination of retinol to the active-site zinc is hindered by a loop from residues 114 to 120 that is at the entrance to the alcohol-binding site. | Vitamin A | alcohol dehydrogenase 1B (class I), beta polypeptide | Homo sapiens |
| 4 | For example, modeling the binding of all-trans-retinol in the human beta 1-ADH structure suggested that coordination of retinol to the active-site zinc is hindered by a loop from residues 114 to 120 that is at the entrance to the alcohol-binding site. | Vitamin A | alcohol dehydrogenase 1B (class I), beta polypeptide | Homo sapiens |