Pub. Date : 2000 Aug 4
PMID : 10801859
12 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Palmitoyl-protein thioesterase-1 (PPT1) is a newly described lysosomal enzyme that hydrolyzes long chain fatty acids from lipid-modified cysteine residues in proteins. | long chain fatty acids | palmitoyl-protein thioesterase 1 | Homo sapiens |
| 2 | Palmitoyl-protein thioesterase-1 (PPT1) is a newly described lysosomal enzyme that hydrolyzes long chain fatty acids from lipid-modified cysteine residues in proteins. | long chain fatty acids | palmitoyl-protein thioesterase 1 | Homo sapiens |
| 3 | Palmitoyl-protein thioesterase-1 (PPT1) is a newly described lysosomal enzyme that hydrolyzes long chain fatty acids from lipid-modified cysteine residues in proteins. | Cysteine | palmitoyl-protein thioesterase 1 | Homo sapiens |
| 4 | Palmitoyl-protein thioesterase-1 (PPT1) is a newly described lysosomal enzyme that hydrolyzes long chain fatty acids from lipid-modified cysteine residues in proteins. | Cysteine | palmitoyl-protein thioesterase 1 | Homo sapiens |
| 5 | Although the primary structure of PPT1 contains a serine lipase consensus sequence, the enzyme is insensitive to commonly used serine-modifying reagents phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. | Serine | palmitoyl-protein thioesterase 1 | Homo sapiens |
| 6 | Although the primary structure of PPT1 contains a serine lipase consensus sequence, the enzyme is insensitive to commonly used serine-modifying reagents phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. | Phenylmethylsulfonyl Fluoride | palmitoyl-protein thioesterase 1 | Homo sapiens |
| 7 | Although the primary structure of PPT1 contains a serine lipase consensus sequence, the enzyme is insensitive to commonly used serine-modifying reagents phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. | Phenylmethylsulfonyl Fluoride | palmitoyl-protein thioesterase 1 | Homo sapiens |
| 8 | Although the primary structure of PPT1 contains a serine lipase consensus sequence, the enzyme is insensitive to commonly used serine-modifying reagents phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. | Isoflurophate | palmitoyl-protein thioesterase 1 | Homo sapiens |
| 9 | In the current paper, we show that the active site serine in PPT1 is modified by a substrate analog of PMSF, hexadecylsulfonylfluoride (HDSF) in a specific and site-directed manner. | Serine | palmitoyl-protein thioesterase 1 | Homo sapiens |
| 10 | In the current paper, we show that the active site serine in PPT1 is modified by a substrate analog of PMSF, hexadecylsulfonylfluoride (HDSF) in a specific and site-directed manner. | Phenylmethylsulfonyl Fluoride | palmitoyl-protein thioesterase 1 | Homo sapiens |
| 11 | In the current paper, we show that the active site serine in PPT1 is modified by a substrate analog of PMSF, hexadecylsulfonylfluoride (HDSF) in a specific and site-directed manner. | hexadecanesulfonyl fluoride | palmitoyl-protein thioesterase 1 | Homo sapiens |
| 12 | In the current paper, we show that the active site serine in PPT1 is modified by a substrate analog of PMSF, hexadecylsulfonylfluoride (HDSF) in a specific and site-directed manner. | hexadecanesulfonyl fluoride | palmitoyl-protein thioesterase 1 | Homo sapiens |