Isomerases: Difference between revisions

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New page: 350px|right|thumb|Reaction Mechanism of an Aldolase Isomerases are enzymes that catalyze the structural rearrangement of isomers. They are classified as EC 5 u...
 
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[[Image: Aldolase1.jpg|350px|right|thumb|Reaction Mechanism of an Aldolase]]
[[Image: Isomerism.png|350px|right|thumb|Different Types of Isomer Rearrangements]]
[[Isomerases]] are enzymes that catalyze the structural rearrangement of isomers. They are classified as EC 5 under the [[EC Number|EC number]] classification.  
[[Isomerases]] are enzymes that catalyze the structural rearrangement of isomers. They are classified as EC 5 under the [[EC Number|EC number]] classification.  


{{#tree:id=IsoTopic|openlevels=0|
Articles in Proteopedia concerning Isomerases include:
Articles in Proteopedia concerning Isomerases include:
* [[Cyclophilin]]
* [[Karen Bulaklak/Sandbox1 Glucosamine 6 Phosphate Synthase|Glucoseamine 6-Phosphate Synthase]] or see: [[User:Nikhita Khanna/sandbox 2: Glucosamine 6 Phosphate future goals|Additional Information]]
* [[User:Laura M. Haynes/Sandbox 1|Ketosteroid Isomerase]]
* [[Triose Phosphate Isomerase]] or see: [[Triose Phosphate Isomerase Structure & Mechanism|Additional Information]] or see [[Triosephosphate Isomerase|Even More Information]]
* [[Phosphoglucoisomerase|Phosphoglucoisomerase]]
* [[UDP-galactopyranose mutase|UDP-Galactopyranose Mutase]]
* [[Ribose-5-phosphate isomerase]]
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To view Isomerases which are [[Proteopedia:Structure Index|Structure Index]] entries see:
* [[Gyrase]]
* [[Recombinase A]]
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Latest revision as of 14:04, 5 December 2019

Different Types of Isomer Rearrangements

Isomerases are enzymes that catalyze the structural rearrangement of isomers. They are classified as EC 5 under the EC number classification.

Articles in Proteopedia concerning Isomerases include:


To view Isomerases which are Structure Index entries see:


To view automatically seeded indices concerning Isomerases See:


Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

David Canner, Jaime Prilusky, Alexander Berchansky