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B6db activities: 4.1.1.81

4.1.1.81
Description Threonine-phosphate decarboxylase.
Alternative names L-threonine-O-3-phosphate decarboxylase;
CobD.
Catalyzed reaction L-threonine O-3-phosphate = (R)-1-aminopropan-2-ol phosphate + CO(2).
Cofactor Pyridoxal-phosphate
Comments This enzyme is unable to decarboxylate the D-isomer of threonine O-3-phosphate.
The product of this reaction, (R)-1-aminopropan-2-yl phosphate, is the substrate of EC 6.3.1.10, adenosylcobinamide phosphate synthase, which converts adenosylcobyric acid into adenosylcobinamide phosphate in the anaerobic cobalamin biosynthesis pathway.
In Salmonella enterica, this enzyme is coded by the CobD gene, and its role in cobalamin biosynthesis has been established. Structurally the Salmonella protein shows a strong similarity to histidinol phosphate aminotransferase (2.6.1.9).
PDB 1LKC;
Organisms -Bacteria
 

Family 

4.1.1.81 (9)
 
Links Enzyme (activities) 4.1.1.81
BRENDA (activities) 4.1.1.81
KEGG (pathways) 4.1.1.81
PLPMDB (PLP mutants) 4.1.1.81
 
References
 Santos F, Vera JL, van der Heijden R, Valdez G, de Vos WM, Sesma F, Hugenholtz J. (2008) The complete coenzyme B12 biosynthesis gene cluster of Lactobacillus reuteri CRL1098 Microbiology 154 81-93.

 Cheong, C.G.; Bauer, C.B.; Brushaber, K.R.; Escalante-Semerena, J.C.; Rayment, I. (2002) Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica Biochemistry 41 4798-808.

 Brushaber, K.R.; O'Toole, G.A.;Escalante-Semerena, J.C. (1998) CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis in Salmonella typhimurium LT2 J Biol Chem 273 2684-91.

Articles on 4.1.1.81
 
last changed 2009/07/10 16:42

B6db activities