Polygalacturonase: Difference between revisions

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== Function ==
== Function ==


Polygalacturonases hydrolyze α-(1-4) – glycosidic bonds between consecutive galacturonic acid residues in polygalacturonic acids. Structural variation has been identified among differing PGs depending on organismal origins and catalytic functions. For example, endo-polygalacturonases produced from Erwinia carotovora demonstrate functional similarity to pectate lyases in that they cleave polygalacturonic acids in a calcium-depended manner via β-elimination (crystal structure).  
Polygalacturonases hydrolyze α-(1-4) – glycosidic bonds between consecutive galacturonic acid residues in polygalacturonic acids. Structural variation has been identified among differing PGs depending on organismal origins and catalytic functions. For example, endo-polygalacturonases produced from <i>Erwinia carotovora </i> demonstrate functional similarity to pectate lyases in that they cleave polygalacturonic acids in a calcium-depended manner via β-elimination (crystal structure).  


== Disease ==
== Disease ==

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OCA, Marilyn Yoder, Krishna Amin, Michal Harel, Joel L. Sussman, Jaime Prilusky