|PROSITE documentation PDOC00148 [for PROSITE entry PS00164]|
Enolase (EC 18.104.22.168) is a glycolytic enzyme that catalyzes the dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate . It is a dimeric enzyme that requires magnesium both for catalysis and stabilizing the dimer. Enolase is probably found in all organisms that metabolize sugars. In vertebrates, there are three different tissue-specific isozymes: α present in most tissues, β in muscles and γ found only in nervous tissues.
Tau-crystallin, one of the major lens proteins in some fish, reptiles and birds, has been shown  to be evolutionary related to enolase.
As a signature pattern for enolase, we selected the best conserved region, it is located in the C-terminal third of the sequence.Last update:
April 2006 / Pattern revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Lebioda L., Stec B., Brewer J.M.|
|Title||The structure of yeast enolase at 2.25-A resolution. An 8-fold beta + alpha-barrel with a novel beta beta alpha alpha (beta alpha)6 topology.|
|Source||J. Biol. Chem. 264:3685-3693(1989).|
|2||Authors||Wistow G., Piatigorsky J.|
|Title||Recruitment of enzymes as lens structural proteins.|