| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-121 |
Sentence |
denotes |
Activation of a cyanobacterial adenylate cyclase, CyaC, by autophosphorylation and a subsequent phosphotransfer reaction. |
| T2 |
122-382 |
Sentence |
denotes |
The CyaC protein, a cyanobacterial adenylate cyclase, has a unique primary structure composed of the catalytic domain of adenylate cyclase and the conserved domains of bacterial two-component regulatory systems, one transmitter domain and two receiver domains. |
| T3 |
383-512 |
Sentence |
denotes |
In the present work, CyaC was produced in Escherichia coli as a histidine-tagged recombinant protein and purified to homogeneity. |
| T4 |
513-606 |
Sentence |
denotes |
CyaC showed ability to autophosphorylate in vitro with the gamma-phosphate of [gamma-32P]ATP. |
| T5 |
607-858 |
Sentence |
denotes |
CyaC derivatives were constructed by site-directed mutagenesis in which the highly conserved phosphorylation sites in the transmitter domain (His572) and receiver domains (Asp60 or Asp895) were replaced by glutamine and alanine residues, respectively. |
| T6 |
859-1001 |
Sentence |
denotes |
After autophosphorylation of the CyaC derivatives, the chemical stabilities of the phosphoryl groups bound to the derivatives were determined. |
| T7 |
1002-1139 |
Sentence |
denotes |
It was found that His572 is the initial phosphorylation site and that the phosphoryl group once bound to His572 is transferred to Asp895. |
| T8 |
1140-1242 |
Sentence |
denotes |
The enzyme activities of the CyaC derivatives defective in His572 or Asp895 were considerably reduced. |
| T9 |
1243-1340 |
Sentence |
denotes |
Asp895 is phosphorylated by acetyl [32P]phosphate, a small phosphoryl molecule, but Asp60 is not. |
| T10 |
1341-1423 |
Sentence |
denotes |
Acetyl phosphate stimulates adenylate cyclase activity only when Asp895 is intact. |
| T11 |
1424-1617 |
Sentence |
denotes |
These results suggest that the phosphorylation of Asp895 is essential for the activation of adenylate cyclase and that Asp60 functions differently from Asp895 in regulating the enzyme activity. |
