View source for Pseudoenzyme

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[[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==
* 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==
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[[Category:Pseudoenzyme]]