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Biosynthesis of Proline

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Proline is unique in having a cyclic structure with its side chain connected to the amino group to create a secondary amine. As a consequence of its cyclic structure, Proline constrains the structure of proteins where it occurs, disrupting Alpha-helices. Isomerization between the cis and trans forms of Proline in proteins is isomerized by peptidyl-prolyl isomerases like the cyclophilins that contribute to protein folding and are components of signal transduction pathways.

Proline is derived from glutamate. Its biosynthesis begins with the ATP-driven phosphorylation and reduction of the carboxyl side chain of glutamate. The Gamma-carboxylate group of glutamate is activated by phosphorylation with ATP to from a Gamma-Glutamyl Phosphate intermediate (Ref.1). The mixed anhydride is then reduced with NADPH, and the [...]


1.Methanococcus jannaschii generates L-proline by cyclization of L-ornithine.
Graupner M, White RH.
J Bacteriol. 2001 Sep;183(17):5203-5.
2.Multiple genes for the last step of proline biosynthesis in Bacillus subtilis.
Belitsky BR, Brill J, Bremer E, Sonenshein AL.
J Bacteriol. 2001 Jul;183(14):4389-92.
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