De novo synthesis

De novo synthesis refers to the synthesis of complex molecules from simple molecules such as sugars or amino acids, as opposed to their being recycled after partial degradation. For example, nucleotides are not needed in the diet as they can be constructed from small precursor molecules such as formate and aspartate. Methionine, on the other hand, is needed in the diet because while it can be degraded to and then regenerated from homocysteine, it cannot be synthesized de novo.

De novo is a Latin phrase, meaning "from the new," anew, from scratch, or from the beginning.

De novo synthesis also refers to DNA replication. Primase is an RNA polymerase, and it can add a primer to an existing strand awaiting replication. DNA polymerase cannot add primers, and therefore, needs primase to add the primer de novo.

De novo pathways

De novo pathways do not use free bases: adenine (abbreviated as A), guanine (G), cytosine (C), thymine (T), or uracil (U). The purine ring is built up one or a few at a time and attached to ribose throughout the process. De novo synthesis enzymes are present as large multienzyme complexes in purines. Pyrimidine ring is synthesized as orotate and attached to ribose phosphate and later converted to common pyrimidine nucleotides.

De novo originates from aspartate, glycine, folate, glutamine and carbon dioxide.

De novo synthesis

• Glutamine PRPP amidotranferase reaction^[1]
• Amidophosphoribosyl tranferase reaction^[2]
• GAR transformylase reaction^[3]
• FGAM synthetase (FGAR amidotransferase) reaction
• FGAM synthetase (cyclase) reaction

External links

• Purine and pyrimidine Metabolism
• De novo synthesis of purine nucleotides

References

1. ^ Smith JL (1998). "Glutamine PRPP amidotransferase: snapshots of an enzyme in action". Current Opinion in Structural Biology 8 (6): 686–694. doi:10.1016/S0959-440X(98)80087-0. PMID 9914248. 
2. ^ Zalkin H (1983). "Structure, function, and regulation of amidophosphoribosyltransferase from prokaryotes". Adv Enzyme Regul 21: 225–37. doi:10.1016/0065-2571(83)90016-X. PMID 6443594. 
3. ^ Nixon AE, Benkovic SJ (200). "Improvement in the efficiency of formyl transfer of a GAR transformylase hybrid enzyme". Protein Engineering 13 (5): 323–327. PMID 10835105. http://peds.oxfordjournals.org/cgi/content/full/13/5/323.