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4.1.1.81 |
Activity |
4.1.1.81 |
Description |
Threonine-phosphate decarboxylase |
Notes |
Family built around the characterized enzyme from Salmonella enterica.
The proteins are most similar to histidinol phosphate aminotransferases (family 2.6.1.9) |
PDB |
1LKC; |
PLP Fold Type |
I |
PLP-dependent Domain |
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Number of sequences |
9 |
Sequences in seed alignment |
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Reference sequence |
1LC7A |
Domain interval |
24-353 |
Catalytic site |
216 K |
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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 |
2008/01/31 12:24 |
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