The Enzyme Database

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EC 1.3.8.14     
Accepted name: L-prolyl-[peptidyl-carrier protein] dehydrogenase
Reaction: L-prolyl-[peptidyl-carrier protein] + 2 electron-transfer flavoprotein = 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] + 2 reduced electron-transfer flavoprotein
Other name(s): pigA (gene name); bmp3 (gene name); pltE (gene name); redW (gene name); (L-prolyl)-[peptidyl-carrier protein]:electron-transfer flavoprotein oxidoreductase
Systematic name: L-prolyl-[peptidyl-carrier protein]:electron-transfer flavoprotein oxidoreductase
Comments: Contains FAD. The enzyme participates in the biosynthesis of several pyrrole-containing compounds, such as undecylprodigiosin, prodigiosin, pyoluteorin, and coumermycin A1. It is believed to catalyse the formation of a Δ2-pyrrolin-2-carbonyl-[peptidyl-carrier protein] intermediate, followed by a two-electron oxidation to 1H-pyrrol-2-carbonyl-[peptidyl-carrier protein].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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]
[EC 1.3.8.14 created 2017]
 
 
EC 1.14.19.56     
Accepted name: 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] chlorinase
Reaction: 1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + 2 FADH2 + 2 chloride + 2 O2 = 4,5-dichloro-1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + 2 FAD + 4 H2O (overall reaction)
(1a) 1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + FADH2 + chloride + O2 = 5-chloro-1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + FAD + 2 H2O
(1b) 5-chloro-1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + FADH2 + chloride + O2 = 4,5-dichloro-1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + FAD + H2O
Glossary: pyoluteorin = 4,5-dichloro-1H-pyrrol-2-yl 2,6-dihydroxyphenyl
Other name(s): pltA (gene name)
Systematic name: 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein]:FADH2 oxidoreductase (chlorinating)
Comments: The enzyme, characterized from the bacterium Pseudomonas protegens Pf-5, is a flavin-dependent chlorinase that participates in the biosynthesis of the antibacterial and antifungal compound pyoluteorin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nowak-Thompson, B., Chaney, N., Wing, J.S., Gould, S.J. and Loper, J.E. Characterization of the pyoluteorin biosynthetic gene cluster of Pseudomonas fluorescens Pf-5. J. Bacteriol. 181 (1999) 2166–2174. [PMID: 10094695]
2.  Dorrestein, P.C., Yeh, E., Garneau-Tsodikova, S., Kelleher, N.L. and Walsh, C.T. Dichlorination of a pyrrolyl-S-carrier protein by FADH2-dependent halogenase PltA during pyoluteorin biosynthesis. Proc. Natl. Acad. Sci. USA 102 (2005) 13843–13848. [DOI] [PMID: 16162666]
3.  Pang, A.H., Garneau-Tsodikova, S. and Tsodikov, O.V. Crystal structure of halogenase PltA from the pyoluteorin biosynthetic pathway. J. Struct. Biol. 192 (2015) 349–357. [DOI] [PMID: 26416533]
[EC 1.14.19.56 created 2018]
 
 
EC 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
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]
 
 


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