View source for Sphinganine-1-phosphate aldolase

{{enzyme
| Name = threonine-phosphate decarboxylase
| EC_number = 4.1.1.81
| CAS_number = 
| IUBMB_EC_number = 4/1/1/81
| GO_code = 0048472
| image = 
| width = 
| caption = 
}}
In [[enzymology]], a '''threonine-phosphate decarboxylase''' ({{EC number|4.1.1.81}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:[[phosphothreonine|L-threonine O-3-phosphate]] <math>\rightleftharpoons</math> (R)-1-aminopropan-2-yl phosphate + CO<sub>2</sub>

Hence, this enzyme has one [[substrate (biochemistry)|substrate]], [[L-threonine O-3-phosphate]], and two [[product (chemistry)|products]], [[(R)-1-aminopropan-2-yl phosphate]] and [[carbon dioxide|CO<sub>2</sub>]].

This enzyme belongs to the family of [[lyase]]s, specifically the carboxy-lyases, which cleave carbon-carbon bonds.  The systematic name of this enzyme class is '''L-threonine-O-3-phosphate carboxy-lyase [(R)-1-aminopropan-2-yl-phosphate-forming]'''. Other names in common use include '''L-threonine-O-3-phosphate decarboxylase''', '''CobD''', and '''L-threonine-O-3-phosphate carboxy-lyase'''.  This enzyme participates in [[porphyrin]] and [[chlorophyll]] metabolism.  

==References==
{{reflist|1}}
* {{cite journal | author = Cheong CG, Bauer CB, Brushaber KR, Escalante-Semerena JC, Rayment I | date = 2002 | title = Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica | journal = Biochemistry.  | volume = 41 | pages = 4798&ndash;808  | pmid = 11939774 | doi = 10.1021/bi012111w | issue = 15 }}
* {{cite journal | author = O'Toole GA, Escalante-Semerena JC | date = 1995 | title = Purification and characterization of the bifunctional CobU enzyme of Salmonella typhimurium LT2. Evidence for a CobU-GMP intermediate | journal = J. Biol. Chem.  | volume = 270 | pages = 23560&ndash;9  | pmid = 7559521 | doi = 10.1074/jbc.270.40.23560 | issue = 40 }}
* {{cite journal | author = Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC | date = 2002 | title = The biosynthesis of adenosylcobalamin (vitamin B12) | journal = Nat. Prod. Rep.  | volume = 19 | pages = 390&ndash;412  | pmid = 12195810 | doi = 10.1039/b108967f | issue = 4 }}

{{4.1-enzyme-stub}}

[[Category:EC 4.1.1]]
[[Category:Enzymes of unknown structure]]