PROSITE documentation PDOC00148Enolase signature
Enolase (EC 4.2.1.11) is a glycolytic enzyme that catalyzes the dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate [1]. 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 [2] 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.
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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). | |
| PubMed ID | 2645275 |
| 2 | Authors | Wistow G. Piatigorsky J. |
| Title | Recruitment of enzymes as lens structural proteins. | |
| Source | Science 236:1554-1556(1987). | |
| PubMed ID | 3589669 |
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