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<ref>PMID: 23559232</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 <ref>PMID: 12471243</ref>. 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>. | ||
==3D structures of Pseudoenzymes== | ==3D structures of Pseudoenzymes== | ||
* C-terminal domain of splicing factor Prp8p | * Toxoplasma virulence factor, ROP5 [[pseudokinase]] ([[3q5z]] and [[3q60]]) | ||
* C-terminal domain of splicing factor Prp8p ([[2og4]]) resembles an isopeptidase converted to a platform | |||
* the structure of a fragment of integrin-like kinase ([[3kmu]] and [[3kmw]]) demonstrated it is not a kinase and instead serves a structural role linking the cell's cytoskeleton to surface receptors | |||
*RLCK family member, the Brassinosteroid signaling kinase ([[4i92]], [[ 4i93]], [[ 4i94]]) | |||
* the [[pseudokinase]] MLKL ([[4btf]]) involved in triggering cell death by necroptosis | |||
*[[Journal:Acta Cryst D:S2059798319002912|Crystal structure of the pseudoenzyme PDX1.2 in complex with its cognate enzyme PDX1.3]] | |||
</ | ==Related== | ||
* [[pseudokinase]] | |||
* CASK ([[3c0i]], [[3c0h]], and [[3c0g]]) 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, see Mukherjee et al., 2008 <ref>PMID: 18423203 </ref> and Kanaan and Taylor, 2008 <ref>PMID:18423189</ref> | |||
* [[Conservation, Evolutionary]] | |||
* [[Evolution]] | |||
* [[Introduction to Evolutionary Conservation]] | |||
==References== | ==References== | ||
<references/> | <references/> | ||
[[Category:Pseudoenzyme]] | [[Category:Pseudoenzyme]] | ||
Latest revision as of 10:53, 2 January 2020
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 [1]. 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 [2][3].
3D structures of Pseudoenzymes
- Toxoplasma virulence factor, ROP5 pseudokinase (3q5z and 3q60)
- C-terminal domain of splicing factor Prp8p (2og4) resembles an isopeptidase converted to a platform
- the structure of a fragment of integrin-like kinase (3kmu and 3kmw) demonstrated it is not a kinase and instead serves a structural role linking the cell's cytoskeleton to surface receptors
- RLCK family member, the Brassinosteroid signaling kinase (4i92, 4i93, 4i94)
- the pseudokinase MLKL (4btf) involved in triggering cell death by necroptosis
- Crystal structure of the pseudoenzyme PDX1.2 in complex with its cognate enzyme PDX1.3
Related
- pseudokinase
- CASK (3c0i, 3c0h, and 3c0g) 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, see Mukherjee et al., 2008 [4] and Kanaan and Taylor, 2008 [5]
- Conservation, Evolutionary
- Evolution
- Introduction to Evolutionary Conservation
References
- ↑ Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S. The protein kinase complement of the human genome. Science. 2002 Dec 6;298(5600):1912-34. PMID:12471243 doi:10.1126/science.1075762
- ↑ 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:https://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:https://dx.doi.org/10.1126/science.340.6128.27
- ↑ Mukherjee K, Sharma M, Urlaub H, Bourenkov GP, Jahn R, Sudhof TC, Wahl MC. CASK Functions as a Mg2+-independent neurexin kinase. Cell. 2008 Apr 18;133(2):328-39. PMID:18423203 doi:10.1016/j.cell.2008.02.036
- ↑ Kannan N, Taylor SS. Rethinking pseudokinases. Cell. 2008 Apr 18;133(2):204-5. doi: 10.1016/j.cell.2008.04.005. PMID:18423189 doi:https://dx.doi.org/10.1016/j.cell.2008.04.005
