ExplorEnz: EC 6.2.1.53

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6.2.1.53

Accepted name:

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

Reaction:

ATP + L-proline + holo-[L-prolyl-carrier protein] = AMP + diphosphate + L-prolyl-[L-prolyl-carrier protein] (overall reaction)
(1a) ATP + L-proline = diphosphate + (L-prolyl)adenylate
(1b) (L-prolyl)adenylate + holo-[L-prolyl-carrier protein] = AMP + L-prolyl-[L-prolyl-carrier protein]

Other name(s):

pltF (gene name); bmp4 (gene name); pigI (gene name)

Systematic name:

L-proline:[L-prolyl-carrier protein] ligase (AMP-forming)

Comments:

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:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Thomas, M.G., Burkart, M.D. and Walsh, C.T. Conversion of L-proline to pyrrolyl-2-carboxyl-S-PCP during undecylprodigiosin and pyoluteorin biosynthesis. Chem. Biol. 9 (2002) 171–184. [DOI] [PMID: 11880032]
2.	Harris, A.K., Williamson, N.R., Slater, H., Cox, A., Abbasi, S., Foulds, I., Simonsen, H.T., Leeper, F.J. and Salmond, G.P. The Serratia gene cluster encoding biosynthesis of the red antibiotic, prodigiosin, shows species- and strain-dependent genome context variation. Microbiology 150 (2004) 3547–3560. [DOI] [PMID: 15528645]
3.	Williamson, N.R., Simonsen, H.T., Ahmed, R.A., Goldet, G., Slater, H., Woodley, L., Leeper, F.J. and 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 (2005) 971–989. [DOI] [PMID: 15853884]

[EC 6.2.1.53 created 2018]