| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-139 |
Sentence |
denotes |
Characterization of the Catalytic and Nucleotide Binding Properties of the α-Kinase Domain of Dictyostelium Myosin-II Heavy Chain Kinase A. |
| T2 |
140-299 |
Sentence |
denotes |
The α-kinases are a widely expressed family of serine/threonine protein kinases that exhibit no sequence identity with conventional eukaryotic protein kinases. |
| T3 |
300-457 |
Sentence |
denotes |
In this report, we provide new information on the catalytic properties of the α-kinase domain of Dictyostelium myosin-II heavy chain kinase-A (termed A-CAT). |
| T4 |
458-619 |
Sentence |
denotes |
Crystallization of A-CAT in the presence of MgATP yielded structures with AMP or adenosine in the catalytic cleft together with a phosphorylated Asp-766 residue. |
| T5 |
620-758 |
Sentence |
denotes |
The results show that the β- and α-phosphoryl groups are transferred either directly or indirectly to the catalytically essential Asp-766. |
| T6 |
759-963 |
Sentence |
denotes |
Biochemical assays confirmed that A-CAT hydrolyzed ATP, ADP, and AMP with kcat values of 1.9, 0.6, and 0.32 min(-1), respectively, and showed that A-CAT can use ADP to phosphorylate peptides and proteins. |
| T7 |
964-1161 |
Sentence |
denotes |
Binding assays using fluorescent 2'/3'-O-(N-methylanthraniloyl) analogs of ATP and ADP yielded Kd values for ATP, ADP, AMP, and adenosine of 20 ± 3, 60 ± 20, 160 ± 60, and 45 ± 15 μM, respectively. |
| T8 |
1162-1313 |
Sentence |
denotes |
Site-directed mutagenesis showed that Glu-713, Leu-716, and Lys-645, all of which interact with the adenine base, were critical for nucleotide binding. |
| T9 |
1314-1562 |
Sentence |
denotes |
Mutation of the highly conserved Gln-758, which chelates a nucleotide-associated Mg(2+) ion, eliminated catalytic activity, whereas loss of the highly conserved Lys-722 and Arg-592 decreased kcat values for kinase and ATPase activities by 3-6-fold. |
| T10 |
1563-1821 |
Sentence |
denotes |
Mutation of Asp-663 impaired kinase activity to a much greater extent than ATPase, indicating a specific role in peptide substrate binding, whereas mutation of Gln-768 doubled ATPase activity, suggesting that it may act to exclude water from the active site. |
