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| Titel | Protein kinase |
| Verlag | (Kids.Net.au) |
| Datum | 3. May 2007 |
| Anmerkung | Most likely a derivative of the Wikipedia |
| URL | http://web.archive.org/web/20070503031710/http://encyclopedia.kids.net.au/page/pr/Protein_kinase |
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| Fußnoten | no |
| Fragmente | 1 |
| [1.] Dsa/Fragment 019 11 - Diskussion Zuletzt bearbeitet: 2016-08-02 19:19:59 WiseWoman | Dsa, Fragment, Gesichtet, KidsNet Protein kinase 2007, KomplettPlagiat, SMWFragment, Schutzlevel sysop |
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| Untersuchte Arbeit: Seite: 19, Zeilen: 11-23 |
Quelle: KidsNet Protein kinase 2007 Seite(n): 1 (online source), Zeilen: - |
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| - Protein kinase C: protein kinase C is actually a family of protein kinases that require Ca2+, diacylglycerol, and a phospholipid such as phosphatidylcholine for activation. Thus, protein kinase C is activated through the same signal transduction pathway as phospholipase C. At least twelve members of the protein kinase C family have been identified in mammals, due to their high sequence homology. The protein kinase C usually means the protein kinase Cα enzyme.
Structure and regulation Protein kinase C enzymes consist of an N-terminal regulatory domain and a C-terminal catalytic domain. The kinases are inactive in the absence of activating agents, due to autoinhibition of the regulatory domain. They can be activated tumor promoters such as tetradecanoyl-phorbol-acetate (TPA) or by the cofactors Ca2+, diacylglycerol and a phospholipid. The common linear structure of protein kinase C enzymes is: N-pseudosubstrate - TPA-binding - (Ca2+-binding) - ATP-binding - substrate-binding- C. |
Protein kinase C
Protein kinase C is actually a family of protein kinases that require Ca2+, diacylglycerol, and a phospholipid such as phosphatidylcholine[?] for activation. Thus, protein kinase C is activated through the same signal transduction pathway as phospholipase C. At least twelve members of the proteine kinase C family have been identified in mammals, due to their high sequence homology[?]. The protein kinase C usually means the protein kinase Cα enzyme. Structure and regulation Protein kinase C enzymes consist of an N-terminal regulatory domain and a C-terminal catalytic domain. The kinases are inactive in the absence of activating agents, due to autoinhibition of the regulatory domain. They can be activated tumor promotors such as tetradecanoyl-phorbol-acetate[?] (TPA) or by the cofactors Ca2+, diacylglycerol, and a phospholipid. The common linear structure of protein kinase C enzymes is: N - pseudosubstrate - TPA-binding - (Ca2+-binding) - ATP-binding - substrate-binding - C |
The source is not given. Note: the text before and after the documented passage can also be found in this source, but other, more likely sources have been used for the documentation of those fragments. |
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