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Information on EC 1.3.8.14 - L-prolyl-[peptidyl-carrier protein] dehydrogenase for references in articles please use BRENDA:EC1.3.8.14
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IUBMB 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 Delta2-pyrrolin-2-carbonyl-[peptidyl-carrier protein] intermediate, followed by a two-electron oxidation to 1H-pyrrol-2-carbonyl-[peptidyl-carrier protein].
The enzyme appears in viruses and cellular organisms
Synonyms
bmp3, L-prolyl-PCP dehydrogenase, L-prolyl-S-PCP dehydrogenase, PigA, pltE, redW, SC2E9.20,
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L-prolyl-PCP dehydrogenase
L-prolyl-S-PCP dehydrogenase
L-prolyl-PCP dehydrogenase
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L-prolyl-PCP dehydrogenase
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L-prolyl-PCP dehydrogenase
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L-prolyl-S-PCP dehydrogenase
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L-prolyl-S-PCP dehydrogenase
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PigA
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gene name
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pltE
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gene name
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redW
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gene name
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SC2E9.20
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L-prolyl-[peptidyl-carrier protein] + 2 electron-transfer flavoprotein = 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] + 2 reduced electron-transfer flavoprotein
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(L-prolyl)-[peptidyl-carrier protein]:electron-transfer flavoprotein oxidoreductase
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 Delta2-pyrrolin-2-carbonyl-[peptidyl-carrier protein] intermediate, followed by a two-electron oxidation to 1H-pyrrol-2-carbonyl-[peptidyl-carrier protein].
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S-(L-prolyl)-[peptidyl-carrier protein PigG] + electron-transfer flavoprotein
S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein PigG] + reduced electron-transfer flavoprotein
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S-(L-prolyl)-[peptidyl-carrier protein] + electron-transfer flavoprotein
S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + reduced electron-transfer flavoprotein
additional information
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S-(L-prolyl)-[peptidyl-carrier protein] + electron-transfer flavoprotein
S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + reduced electron-transfer flavoprotein
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S-(L-prolyl)-[peptidyl-carrier protein] + electron-transfer flavoprotein
S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + reduced electron-transfer flavoprotein
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S-(L-prolyl)-[peptidyl-carrier protein] + electron-transfer flavoprotein
S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + reduced electron-transfer flavoprotein
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S-(L-prolyl)-[peptidyl-carrier protein] + electron-transfer flavoprotein
S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + reduced electron-transfer flavoprotein
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S-(L-prolyl)-[peptidyl-carrier protein] + electron-transfer flavoprotein
S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + reduced electron-transfer flavoprotein
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additional information
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no activity with L-prolyl-S-CoA
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additional information
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no activity with L-prolyl-S-CoA
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S-(L-prolyl)-[peptidyl-carrier protein PigG] + electron-transfer flavoprotein
S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein PigG] + reduced electron-transfer flavoprotein
Q5W271
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S-(L-prolyl)-[peptidyl-carrier protein] + electron-transfer flavoprotein
S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + reduced electron-transfer flavoprotein
S-(L-prolyl)-[peptidyl-carrier protein] + electron-transfer flavoprotein
S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + reduced electron-transfer flavoprotein
Q5W271
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S-(L-prolyl)-[peptidyl-carrier protein] + electron-transfer flavoprotein
S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + reduced electron-transfer flavoprotein
Q5W271
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S-(L-prolyl)-[peptidyl-carrier protein] + electron-transfer flavoprotein
S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + reduced electron-transfer flavoprotein
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S-(L-prolyl)-[peptidyl-carrier protein] + electron-transfer flavoprotein
S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + reduced electron-transfer flavoprotein
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S-(L-prolyl)-[peptidyl-carrier protein] + electron-transfer flavoprotein
S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + reduced electron-transfer flavoprotein
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FAD
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UniProt
brenda
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UniProt
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UniProt
brenda
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brenda
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brenda
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REDW_STRCO
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
391
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41624
Swiss-Prot
PLTE_PSEF5
Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
380
0
41058
Swiss-Prot
PIGA_SERS3
Serratia sp. (strain ATCC 39006)
386
0
42048
Swiss-Prot
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Serratia sp. (strain ATCC 39006)
Serratia sp. (strain ATCC 39006)
Serratia sp. (strain ATCC 39006)
Serratia sp. (strain ATCC 39006)
Serratia sp. (strain ATCC 39006)
Serratia sp. (strain ATCC 39006)
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x * 42000, SDS-PAGE
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x * 40000, SDS-PAGE
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Q sepharose column chromatography
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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Thomas, M.; Burkart, M.; Walsh, C.
Conversion of L-proline to pyrrolyl-2-carboxyl-S-PCP during undecylprodigiosin and pyoluteorin biosynthesis
Chem. Biol.
9
171-184
2002
Streptomyces coelicolor, Streptomyces coelicolor A(3)2
brenda
Garneau-Tsodikova, S.; Dorrestein, P.; Kelleher, N.; Walsh, C.
Protein assembly line components in prodigiosin biosynthesis Characterization of PigA,G,H,I,J
J. Am. Chem. Soc.
128
12600-12601
2006
Serratia sp. (Q5W271)
brenda
Harris, A.; Williamson, N.; Slater, H.; Cox, A.; Abbasi, S.; Foulds, I.; Simonsen, H.; Leeper, F.; Salmond, G.
The Serratia gene cluster encoding biosynthesis of the red antibiotic, prodigiosin, shows species- and strain-dependent genome context variation
Microbiology
150
3547-3560
2004
Serratia marcescens (Q5W271), Serratia marcescens ATCC 274 (Q5W271), Serratia sp. (Q5W271)
brenda
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1.3.8.14 L-prolyl-[peptidyl-carrier protein] dehydrogenase
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