Pub. Date : 2020 Aug 3
PMID : 32747680
8 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Histone lysine acetyltransferase (KAT)-catalyzed acetylation of lysine residues in histone tails plays a key role in regulating gene expression in eukaryotes. | Lysine | thiosulfate sulfurtransferase like domain containing 1 | Homo sapiens |
| 2 | Histone lysine acetyltransferase (KAT)-catalyzed acetylation of lysine residues in histone tails plays a key role in regulating gene expression in eukaryotes. | Lysine | thiosulfate sulfurtransferase like domain containing 1 | Homo sapiens |
| 3 | Our results demonstrate that human KAT enzymes have an ability to catalyze an efficient acetylation of longer lysine analogs, whereas shorter lysine analogs are not substrates for KATs. | Lysine | thiosulfate sulfurtransferase like domain containing 1 | Homo sapiens |
| 4 | Our results demonstrate that human KAT enzymes have an ability to catalyze an efficient acetylation of longer lysine analogs, whereas shorter lysine analogs are not substrates for KATs. | Lysine | thiosulfate sulfurtransferase like domain containing 1 | Homo sapiens |
| 5 | Kinetics analyses showed that lysine is a superior KAT substrate to its analogs with altered chain length, implying that lysine has an optimal chain length for KAT-catalyzed acetylation reaction. | Lysine | thiosulfate sulfurtransferase like domain containing 1 | Homo sapiens |
| 6 | Kinetics analyses showed that lysine is a superior KAT substrate to its analogs with altered chain length, implying that lysine has an optimal chain length for KAT-catalyzed acetylation reaction. | Lysine | thiosulfate sulfurtransferase like domain containing 1 | Homo sapiens |
| 7 | Kinetics analyses showed that lysine is a superior KAT substrate to its analogs with altered chain length, implying that lysine has an optimal chain length for KAT-catalyzed acetylation reaction. | Lysine | thiosulfate sulfurtransferase like domain containing 1 | Homo sapiens |
| 8 | Kinetics analyses showed that lysine is a superior KAT substrate to its analogs with altered chain length, implying that lysine has an optimal chain length for KAT-catalyzed acetylation reaction. | Lysine | thiosulfate sulfurtransferase like domain containing 1 | Homo sapiens |