{PDOC00148}
{PS00164; ENOLASE}
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* Enolase signature *
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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: alpha present in most tissues,
beta in muscles and gamma 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.

-Consensus pattern: [LIVTMS]-[LIVP]-[LIV]-[KQ]-x-[ND]-Q-[INV]-[GA]-[ST]-
                    [LIVM]-[STL]-[DERKAQG]-[STA]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2006 / Pattern revised.

[ 1] Lebioda L., Stec B., Brewer J.M.
     "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."
     J. Biol. Chem. 264:3685-3693(1989).
     PubMed=2645275
[ 2] Wistow G., Piatigorsky J.
     "Recruitment of enzymes as lens structural proteins."
     Science 236:1554-1556(1987).
     PubMed=3589669

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