View source for Phosphatidylinositol-4-phosphate 3-kinase

{{enzyme
| Name = phosphomethylpyrimidine kinase
| EC_number = 2.7.4.7
| CAS_number = 37278-18-5
| IUBMB_EC_number = 2/7/4/7
| GO_code = 0008972
| image = 
| width = 
| caption = 
}}
In [[enzymology]], a '''phosphomethylpyrimidine kinase''' ({{EC number|2.7.4.7}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:ATP + (4-amino-2-methylpyrimidin-5-yl)methyl phosphate <math>\rightleftharpoons</math> ADP + (4-amino-2-methylpyrimidin-5-yl)methyl diphosphate

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]] and [[(4-amino-2-methylpyrimidin-5-yl)methyl phosphate]], whereas its two [[product (chemistry)|products]] are [[adenosine diphosphate|ADP]] and [[(4-amino-2-methylpyrimidin-5-yl)methyl diphosphate]].

This enzyme belongs to the family of [[transferase]]s, to be specific, those transferring phosphorus-containing groups ([[phosphotransferase]]s) with a phosphate group as acceptor.  The systematic name of this enzyme class is '''ATP:(4-amino-2-methylpyrimidin-5-yl)methyl-phosphate phosphotransferase'''. Other names in common use include '''hydroxymethylpyrimidine phosphokinase''', and '''ATP:4-amino-2-methyl-5-phosphomethylpyrimidine phosphotransferase'''.  This enzyme participates in [[thiamine metabolism]].  

==Structural studies==

As of late 2007, 4 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1JXH}}, {{PDB link|1JXI}}, {{PDB link|1UB0}}, and {{PDB link|2I5B}}.

==References==
{{reflist|1}}
* {{cite journal | author = Lewin LM and Brown GM | date = 1961 | title = The biosynthesis of thiamine. III. Mechanism of enzymatic formation of the pyrophosphate ester of 2-methyl-4-amino-5-hydroxymethylpyrimidine | journal = J. Biol. Chem.  | volume = 236 | pages = 2768&ndash;2771 }}

{{enzyme-stub}}

[[Category:EC 2.7.4]]
[[Category:Enzymes of known structure]]