Pseudoenzyme
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== Pseudoenzyme == | == Pseudoenzyme == | ||
[[Pseudoenzyme|Pseudoenzymes]] are proteins that cannot catalyze chemical reactions despite being clearly related structurally to functioning enzymes. Many enzyme families contain inactive members. For example, a number of human kinases lack at least one of the key amino acids necessary for catalysis of phosphate transfer. Often [[Pseudoenzyme|pseudoenzymes]] still have biological roles, albeit non-catalytic. Some assist true enzymes in obtaining functional folds, some server as platforms for other proteins to interact, and some are escorts for proteins <ref>PMID: 23559232</ref><ref>PMID: 23559233</ref>. | [[Pseudoenzyme|Pseudoenzymes]] are proteins that cannot catalyze chemical reactions despite being clearly related structurally to functioning enzymes. Many enzyme families contain inactive members. For example, a number of human kinases lack at least one of the key amino acids necessary for catalysis of phosphate transfer. Often [[Pseudoenzyme|pseudoenzymes]] still have biological roles, albeit non-catalytic. Some assist true enzymes in obtaining functional folds, some server as platforms for other proteins to interact, and some are escorts for proteins <ref>PMID: 23559232</ref><ref>PMID: 23559233</ref>. | ||
Revision as of 23:24, 15 December 2013
Pseudoenzyme
Pseudoenzymes are proteins that cannot catalyze chemical reactions despite being clearly related structurally to functioning enzymes. Many enzyme families contain inactive members. For example, a number of human kinases lack at least one of the key amino acids necessary for catalysis of phosphate transfer. Often pseudoenzymes still have biological roles, albeit non-catalytic. Some assist true enzymes in obtaining functional folds, some server as platforms for other proteins to interact, and some are escorts for proteins [1][2].
3D structures of Pseudoenzymes
- C-terminal domain of splicing factor Prp8p (2og4) resembles an isopeptidase converted to a platform
- the structure of a fragment of integrin-like kinase (GET PDB ID) demonstrated it is not a kinase and instead serves a structural role linking the cell's cytoskeleton to surface receptors GET PDB ID BY LOOKING UP
References
- ↑ Leslie M. Molecular biology. 'Dead' enzymes show signs of life. Science. 2013 Apr 5;340(6128):25-7. doi: 10.1126/science.340.6128.25. PMID:23559232 doi:http://dx.doi.org/10.1126/science.340.6128.25
- ↑ Leslie M. Dead or alive? Science. 2013 Apr 5;340(6128):27. doi: 10.1126/science.340.6128.27. PMID:23559233 doi:http://dx.doi.org/10.1126/science.340.6128.27
Related
- GET PDB ID by LOOKING UP CASK and Konark Mukherjee -- may be a 2008 Cell paper, hard to tell from citation if same - CASK was originally thought to be a [Pseudoenzyme|pseudoenzyme]], but after the structural was solved it was apparent it could use alternative amino acids in the kinase reaction
