Pub. Date : 2000 Aug
PMID : 11014304
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Chemical modification of potato apyrase suggests that tryptophan residues are close to the nucleotide binding site. | Tryptophan | apyrase | Solanum tuberosum |
| 2 | Kd values (+/- Ca2+) for the complexes of apyrase with the non-hydrolysable phosphonate adenine nucleotide analogues, adenosine 5"-(beta,gamma-methylene) triphosphate and adenosine 5"-(alpha,beta-methylene) diphosphate, were obtained from quenching of the intrinsic enzyme fluorescence. | phosphonate adenine nucleotide | apyrase | Solanum tuberosum |
| 3 | Kd values (+/- Ca2+) for the complexes of apyrase with the non-hydrolysable phosphonate adenine nucleotide analogues, adenosine 5"-(beta,gamma-methylene) triphosphate and adenosine 5"-(alpha,beta-methylene) diphosphate, were obtained from quenching of the intrinsic enzyme fluorescence. | 5'-adenylyl (beta,gamma-methylene)diphosphonate | apyrase | Solanum tuberosum |
| 4 | Kd values (+/- Ca2+) for the complexes of apyrase with the non-hydrolysable phosphonate adenine nucleotide analogues, adenosine 5"-(beta,gamma-methylene) triphosphate and adenosine 5"-(alpha,beta-methylene) diphosphate, were obtained from quenching of the intrinsic enzyme fluorescence. | alpha,beta-methyleneadenosine 5'-diphosphate | apyrase | Solanum tuberosum |
| 5 | 1,N6-ethenoadenosine triphosphate and 1,N6-ethenoadenosine diphosphate) were hydrolysed by apyrase in the presence of Ca2+, indicating binding to the active site. | 1,n6-ethenoadenosine triphosphate | apyrase | Solanum tuberosum |
| 6 | 1,N6-ethenoadenosine triphosphate and 1,N6-ethenoadenosine diphosphate) were hydrolysed by apyrase in the presence of Ca2+, indicating binding to the active site. | 1,N(6)-ethenoadenosine diphosphate | apyrase | Solanum tuberosum |