| Attributes | Values |
|---|
| rdfs:label
| |
| dbkwik:resource/2sEMAEJEKAepi0HDgdGAaw==
| |
| dbkwik:resource/57jW2McNGlE9pqjtgT9qcQ==
| |
| dbkwik:resource/6xQvFwQUuYf5iVHArKKckA==
| |
| dbkwik:resource/7gk-nPZg6shct0rt28HYKw==
| |
| dbkwik:resource/AO1Xwa3zhjchsEWtraQgsA==
| |
| dbkwik:resource/BVnC8Hc44vHx7oL0Uq96xQ==
| |
| dbkwik:resource/QnNqLb9ZSWSpQX201CKLLA==
| |
| dbkwik:resource/QseLpQRy423bxxL2KmhCog==
| |
| dbkwik:resource/cOQ63AVwiZYf3UUTa8fbjA==
| |
| dbkwik:resource/eDhPLpw7o8B5wk3WJ-2kTA==
| |
| dbkwik:resource/p9TOJUtbeeejfnk5AAQHUg==
| - Serine/threonine-specific protein kinase
[...]
Serine/threonine protein kinases phosphorylate the OH group of serine or threonine . Activity of these protein kinases can be regulated by specific events , as well as numerous chemical signals, including:
* cAMP/cGMP
* Diacylglycerol
* Ca2+/calmodulin
While serine/threonine kinases all phosphorylate serine or threonine residues in their substrates, they select specific residues to phosphorylate on the basis of residues that flank the phosphoacceptor site, which together comprise the consensus sequence. Since the consensus sequence residues of the substrate to be phosphorylated make contact with the catalytic cleft of the kinase at several key amino acids , a kinase is usually not specific to a single substrate, but instead can phosphorylate a whole "substrate family" having common recognition sequences. While the catalytic domain of these kinases is highly conserved, the sequence variation that is observed in the kinome provides for recognition of distinct substrates. Most kinases are inhibited by a pseudosubstrate that binds to the kinase like a real substrate but lacks the amino acid to be phosphorylated. When the pseudosubstrate is removed, the kinase can perform its normal function.
[...]
Phosphorylase kinase
Phosphorylase kinase was in fact, the first Ser/Thr protein kinase to be discovered .
Protein kinase A
[...]
Protein kinase A consists of two domains, a small domain with several β sheet structures and a larger domain containing several α helices. The binding sites for substrate and ATP are located in the catalytic cleft between the domains . When ATP and substrate bind, the two lobes rotate so that the terminal phosphate group of the ATP and the target amino acid of the substrate move into the correct positions for the catalytic reaction to take place.
|
| dbkwik:resource/rhO74gMtkkCwMnnTXRSfyw==
| |
| dbkwik:resource/svXw5xiEpS-Kv-aSR_SE7w==
| |
| dbkwik:de.vronipla...iPageUsesTemplate
| |
| Quelle
| - Wikipedia Serine-threonine-specific protein kinase 2006
|
| dbkwik:resource/XhOMK2reAaqeAKQ0pQhkhA==
| |
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