EC - L-proline—[L-prolyl-carrier protein] ligase

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IntEnz Enzyme Nomenclature


Accepted name:
L-proline—[L-prolyl-carrier protein] ligase
Other names:
pltF (gene name)
bmp4 (gene name)
pigI (gene name)
Systematic name:
L-proline:[L-prolyl-carrier protein] ligase (AMP-forming)



The enzyme participates in the biosynthesis of several pyrrole-containing compounds, such as undecylprodigiosin, prodigiosin, pyoluteorin, and coumermycin A1. It catalyses the activation of L-proline to an adenylate form, followed by its transfer to the 4'-phosphopantheine moiety of an L-prolyl-carrier protein.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Thomas, M. G., Burkart, M. D., Walsh, C. T.
    Conversion of L-proline to pyrrolyl-2-carboxyl-S-PCP during undecylprodigiosin and pyoluteorin biosynthesis.
    Chem. Biol. 9: 171-184 (2002). [PMID: 11880032]
  2. Harris, A. K., Williamson, N. R., Slater, H., Cox, A., Abbasi, S., Foulds, I., Simonsen, H. T., Leeper, F. J., Salmond, G. P.
    The Serratia gene cluster encoding biosynthesis of the red antibiotic, prodigiosin, shows species- and strain-dependent genome context variation.
    Microbiology (Reading, Engl.) 150: 3547-3560 (2004). [PMID: 15528645]
  3. Williamson, N. R., Simonsen, H. T., Ahmed, R. A., Goldet, G., Slater, H., Woodley, L., Leeper, F. J., Salmond, G. P.
    Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces.
    Mol. Microbiol. 56: 971-989 (2005). [PMID: 15853884]

[EC created 2018]