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1axr
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1axr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1axr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1axr RCSB], [http://www.ebi.ac.uk/pdbsum/1axr PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1axr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1axr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1axr RCSB], [http://www.ebi.ac.uk/pdbsum/1axr PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT]] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 06:59, 24 December 2014
COOPERATIVITY BETWEEN HYDROGEN-BONDING AND CHARGE-DIPOLE INTERACTIONS IN THE INHIBITION OF BETA-GLYCOSIDASES BY AZOLOPYRIDINES: EVIDENCE FROM A STUDY WITH GLYCOGEN PHOSPHORYLASE B
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