TY - JOUR
T1 - The transformylase enzymes of de novo purine biosynthesis
AU - Warren, Mark S.
AU - Mattia, Karen M.
AU - Marolewski, Ariane E.
AU - Benkovic, Stephen J.
N1 - Funding Information:
Acknowledgments This work was supported by the National Institutes of Health through PHS Grant GM24129 (S.J.B.) and postdoctoral fellowship GM16559-02 (K.M.M.).
PY - 1996/11
Y1 - 1996/11
N2 - Formyl transfer reactions play a key role in the construction of the purine heterocycle during de novo purine biosynthesis. Formylation is catalyzed early in the pathway by the purN glycinamide ribonucleotide transformylase (GAR Transformylase, EC 2.1.2.2) in a tetrahydrofolate-dependent manner and also by the purT GAR transformylase in a tetrahydrofolate-independent manner in bacteria. Late in the pathway, 5-aminoimidazole-4-carboxamide ribonucleotide transformylase (AICAR Transformylase, EC 2.1.2.3) catalyzes the second and final formylation involved in purine nucleotide biosynthesis. This article summarizes the salient properties and mechanistic knowledge on the transformylases with special emphasis on the mechanism of the purN GAR transformylase as explored by mutagenesis studies.
AB - Formyl transfer reactions play a key role in the construction of the purine heterocycle during de novo purine biosynthesis. Formylation is catalyzed early in the pathway by the purN glycinamide ribonucleotide transformylase (GAR Transformylase, EC 2.1.2.2) in a tetrahydrofolate-dependent manner and also by the purT GAR transformylase in a tetrahydrofolate-independent manner in bacteria. Late in the pathway, 5-aminoimidazole-4-carboxamide ribonucleotide transformylase (AICAR Transformylase, EC 2.1.2.3) catalyzes the second and final formylation involved in purine nucleotide biosynthesis. This article summarizes the salient properties and mechanistic knowledge on the transformylases with special emphasis on the mechanism of the purN GAR transformylase as explored by mutagenesis studies.
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U2 - 10.1351/pac199668112029
DO - 10.1351/pac199668112029
M3 - Article
AN - SCOPUS:0001584726
SN - 0033-4545
VL - 68
SP - 2029
EP - 2036
JO - Pure and Applied Chemistry
JF - Pure and Applied Chemistry
IS - 11
ER -