PROSITE documentation PDOC00148

Enolase signature




Description

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.

Technical section

PROSITE method (with tools and information) covered by this documentation:

ENOLASE, PS00164; Enolase signature  (PATTERN)


References

1AuthorsLebioda L., Stec B., Brewer J.M.
TitleThe 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.
SourceJ. Biol. Chem. 264:3685-3693(1989).
PubMed ID2645275

2AuthorsWistow G., Piatigorsky J.
TitleRecruitment of enzymes as lens structural proteins.
SourceScience 236:1554-1556(1987).
PubMed ID3589669



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