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{{enzyme
| Name = glycerophosphodiester phosphodiesterase
| EC_number = 3.1.4.46
| CAS_number = 86280-59-3
| IUBMB_EC_number = 3/1/4/46
| GO_code = 0008889
| image = 
| width = 
| caption = 
}}
In [[enzymology]], a '''glycerophosphodiester phosphodiesterase''' ({{EC number|3.1.4.46}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:a glycerophosphodiester + H<sub>2</sub>O <math>\rightleftharpoons</math> an alcohol + sn-glycerol 3-phosphate

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[glycerophosphodiester]] and [[water|H<sub>2</sub>O]], whereas its two [[product (chemistry)|products]] are [[alcohol]] and [[sn-glycerol 3-phosphate]].

This enzyme belongs to the family of [[hydrolase]]s, specifically those acting on phosphoric [[ester|diester]] bonds.  The systematic name of this enzyme class is '''glycerophosphodiester glycerophosphohydrolase'''. Other names in common use include '''gene hpd protein''', '''glycerophosphoryl diester phosphodiesterase''', and '''IgD-binding protein D'''.  This enzyme participates in [[glycerophospholipid metabolism]].  

==Structural studies==

As of late 2007, 9 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1O1Z}}, {{PDB link|1T8Q}}, {{PDB link|1V8E}}, {{PDB link|1VD6}}, {{PDB link|1YDY}}, {{PDB link|2DXL}}, {{PDB link|2DXN}}, {{PDB link|2OOG}}, and {{PDB link|2P76}}.

==References==
{{reflist|1}}
* {{cite journal | author = Larson TJ, Ehrmann M, Boos W | date = 1983 | title = Periplasmic glycerophosphodiester phosphodiesterase of Escherichia coli, a new enzyme of the glp regulon | journal = J. Biol. Chem.  | volume = 258 | pages = 5428&ndash;32  | pmid = 6304089 | issue = 9 }}

{{hydrolase-stub}}

[[Category:EC 3.1.4]]
[[Category:Enzymes of known structure]]