Pub. Date : 1998 May
PMID : 9605314
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The pyridoxal-P binding sites of the two isoforms of human glutamate decarboxylase (GAD65 and GAD67) were modeled by using PROBE (a recently developed algorithm for multiple sequence alignment and database searching) to align the primary sequence of GAD with pyridoxal-P binding proteins of known structure. | Pyridoxal Phosphate | glutamate decarboxylase 1 | Homo sapiens |
| 2 | The pyridoxal-P binding sites of the two isoforms of human glutamate decarboxylase (GAD65 and GAD67) were modeled by using PROBE (a recently developed algorithm for multiple sequence alignment and database searching) to align the primary sequence of GAD with pyridoxal-P binding proteins of known structure. | Pyridoxal Phosphate | glutamate decarboxylase 1 | Homo sapiens |
| 3 | The pyridoxal-P binding sites of the two isoforms of human glutamate decarboxylase (GAD65 and GAD67) were modeled by using PROBE (a recently developed algorithm for multiple sequence alignment and database searching) to align the primary sequence of GAD with pyridoxal-P binding proteins of known structure. | Pyridoxal Phosphate | glutamate decarboxylase 1 | Homo sapiens |
| 4 | The pyridoxal-P binding sites of the two isoforms of human glutamate decarboxylase (GAD65 and GAD67) were modeled by using PROBE (a recently developed algorithm for multiple sequence alignment and database searching) to align the primary sequence of GAD with pyridoxal-P binding proteins of known structure. | Pyridoxal Phosphate | glutamate decarboxylase 1 | Homo sapiens |
| 5 | The key residues that interact directly with pyridoxal-P were identical in ornithine decarboxylase and the two GADs, thus allowing us to make a specific structural prediction of the cofactor binding site of GAD. | Pyridoxal Phosphate | glutamate decarboxylase 1 | Homo sapiens |