View source for O-pyrocatechuate decarboxylase

{{enzyme
| Name = phenylserine aldolase
| EC_number = 4.1.2.26
| CAS_number = 37290-60-1
| IUBMB_EC_number = 4/1/2/26
| GO_code = 0050179
| image = 
| width = 
| caption = 
}}
In [[enzymology]], a '''phenylserine aldolase''' ({{EC number|4.1.2.26}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:L-threo-3-phenylserine <math>\rightleftharpoons</math> glycine + benzaldehyde

Hence, this enzyme has one [[substrate (biochemistry)|substrate]], [[L-threo-3-phenylserine]], and two [[product (chemistry)|products]], [[glycine]] and [[benzaldehyde]].

This enzyme belongs to the family of [[lyase]]s, specifically the aldehyde-lyases, which cleave carbon-carbon bonds.  The systematic name of this enzyme class is '''L-threo-3-phenylserine benzaldehyde-lyase (glycine-forming)'''. This enzyme is also called '''L-threo-3-phenylserine benzaldehyde-lyase'''.  It employs one [[cofactor (biochemistry)|cofactor]], [[pyridoxal phosphate]].  

==Structural studies==

As of late 2007, only one [[tertiary structure|structure]] has been solved for this class of enzymes, with the [[Protein Data Bank|PDB]] accession code {{PDB link|1V72}}.

==References==
{{reflist|1}}
* {{cite journal | author = BRUNS FH, FIEDLER L | date = 1958 | title = Enzymatic cleavage and synthesis of L-threo-beta-phenylserine and L-erythro-beta-Phenyldrine | journal = Nature.  | volume = 181 | pages = 1533&ndash;4  | pmid = 13566053 | doi = 10.1038/1811533a0 | issue = 4622 }}

{{4.1-enzyme-stub}}

[[Category:EC 4.1.2]]
[[Category:Pyridoxal phosphate enzymes]]
[[Category:Enzymes of known structure]]