View source for Hydroxymandelonitrile lyase

{{enzyme
| Name = L-fuculose-phosphate aldolase
| EC_number = 4.1.2.17
| CAS_number = 9024-54-8
| IUBMB_EC_number = 4/1/2/17
| GO_code = 0008738
| image = 
| width = 
| caption = 
}}
In [[enzymology]], a '''<small>L</small>-fuculose-phosphate aldolase''' ({{EC number|4.1.2.17}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

: <small>L</small>-fuculose-1-phosphate <math>\rightleftharpoons</math> glycerone phosphate + (''S'')-lactaldehyde

Hence, this enzyme has one [[substrate (biochemistry)|substrate]], [[L-fuculose-1-phosphate|<small>L</small>-fuculose-1-phosphate]], and two [[product (chemistry)|products]], [[glycerone phosphate]] and [[(S)-lactaldehyde]].

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-fuculose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming)'''. Other names in common use include '''L-fuculose 1-phosphate aldolase''', '''fuculose aldolase''', and '''L-fuculose-1-phosphate lactaldehyde-lyase'''.  This enzyme participates in [[Fructose metabolism|fructose]] and [[Mannose metabolism|mannose metabolism]]. 

==Structural studies==

As of late 2007, 20 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1DZU}}, {{PDB link|1DZV}}, {{PDB link|1DZW}}, {{PDB link|1DZX}}, {{PDB link|1DZY}}, {{PDB link|1DZZ}}, {{PDB link|1E46}}, {{PDB link|1E47}}, {{PDB link|1E48}}, {{PDB link|1E49}}, {{PDB link|1E4A}}, {{PDB link|1E4B}}, {{PDB link|1E4C}}, {{PDB link|1FUA}}, {{PDB link|2FK5}}, {{PDB link|2FLF}}, {{PDB link|2FUA}}, {{PDB link|2OPI}}, {{PDB link|3FUA}}, and {{PDB link|4FUA}}.

== See also ==

* [[Fuculose]]
* [[L-Fuculose kinase|<small>L</small>-Fuculose kinase]]

==References==
{{reflist|1}}
* {{cite journal | author = Ghalambor MA, Heath EC | date = 1966 | title = The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. IV. Purification and properties of cytidine monophosphate 3-deoxy-d-manno-octulosonate synthetase | journal = J. Biol. Chem.  | volume = 241 | pages = 3216&ndash;21  | pmid = 5330266 | issue = 13 }}
* {{cite journal | author = Dreyer MK, Schulz GE | date = 1993 | title = The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli | journal = J. Mol. Biol.  | volume = 231 | pages = 549&ndash;53  | pmid = 8515438 | doi = 10.1006/jmbi.1993.1307 | issue = 3 }}
* {{cite journal | author = Dreyer MK, Schulz GE | date = 1996 | title = Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure | journal = J. Mol. Biol.  | volume = 259 | pages = 458&ndash;66  | pmid = 8676381 | doi = 10.1006/jmbi.1996.0332 | issue = 3 }}

{{4.1-enzyme-stub}}

[[Category:EC 4.1.2]]
[[Category:Enzymes of known structure]]