{PDOC00095}
{PS00102; PHOSPHORYLASE}
{BEGIN}
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* Phosphorylase pyridoxal-phosphate attachment site *
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Phosphorylases   (EC  2.4.1.1)  [1]    are   important allosteric  enzymes  in
carbohydrate metabolism.   They catalyze  the formation of glucose 1-phosphate
from polyglucose  such  as  glycogen,  starch  or  maltodextrin.  Enzymes from
different sources  differ  in  their  regulatory  mechanisms and their natural
substrates. However,  all  known phosphorylases share catalytic and structural
properties. They  are  pyridoxal-phosphate  dependent enzymes; the pyridoxal-P
group is  attached  to  a  lysine  residue around which the sequence is highly
conserved and  can  be  used  as  a  signature pattern to detect this class of
enzymes.

-Consensus pattern: E-A-[SC]-G-x-[GS]-x-M-K-x(2)-[LM]-N
                    [K is the pyridoxal-P attachment site]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 1997 / Pattern and text revised.

[ 1] Fukui T., Shimomura S., Nakano K.
     "Potato and rabbit muscle phosphorylases: comparative studies on the
     structure, function and regulation of regulatory and nonregulatory
     enzymes."
     Mol. Cell. Biochem. 42:129-144(1982).
     PubMed=7062910

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